|
Name |
Accession |
Description |
Interval |
E-value |
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
18-145 |
4.09e-76 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 249.13 E-value: 4.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 18 QAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIA 97
Cdd:cd21236 1 QAYENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 40849888 98 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 145
Cdd:cd21236 81 LDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
32-136 |
7.23e-76 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 247.70 E-value: 7.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 32 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 111
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 40849888 112 RNDDIADGNPKLTLGLIWTIILHFQ 136
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
29-147 |
2.82e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 240.70 E-value: 2.82e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 108
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 40849888 109 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 147
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
149-254 |
1.02e-71 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 235.69 E-value: 1.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 40849888 229 PEDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
150-254 |
1.10e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 40849888 230 EDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
29-146 |
7.56e-63 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 211.04 E-value: 7.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 108
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 40849888 109 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 146
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
150-254 |
9.55e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.59 E-value: 9.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 229
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 40849888 230 EDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
148-254 |
5.13e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 176.77 E-value: 5.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 148 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 227
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 40849888 228 DPEDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
34-137 |
1.19e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 112
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 40849888 113 NDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
20-133 |
7.16e-48 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 167.93 E-value: 7.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 20 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 97
Cdd:cd21246 1 FERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 40849888 98 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21246 81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
150-250 |
2.46e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 40849888 230 EDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
33-361 |
3.57e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRLFNAII 188
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 189 HRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 255
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 256 VPGAQDGVRANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KNRSKG 332
Cdd:COG5069 245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
|
330 340
....*....|....*....|....*....
gi 40849888 333 IYQSLEgAVQAGQLKIPPGYHPLDVEKEW 361
Cdd:COG5069 323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
150-250 |
1.81e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.94 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 40849888 230 EDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
20-133 |
3.85e-44 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 157.07 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 20 YEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 97
Cdd:cd21193 1 FEKGRiRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 40849888 98 LDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21193 81 LAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
30-137 |
4.88e-44 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 156.77 E-value: 4.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 105
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 40849888 106 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
30-137 |
2.09e-43 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 155.04 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 102
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 40849888 103 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
137-252 |
2.98e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 149.05 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 137 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 216
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 217 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
149-254 |
6.89e-41 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 147.85 E-value: 6.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 40849888 229 PEDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
29-133 |
6.71e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 145.94 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 107
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 40849888 108 LVNIRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
20-133 |
4.79e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 143.27 E-value: 4.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 20 YEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 97
Cdd:cd21317 16 FERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKA 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 40849888 98 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21317 96 LQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1340-1963 |
5.60e-39 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 160.87 E-value: 5.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAElEARELQRRMQEevtrreeaavdaqqqkRSIQEELQHLRQSs 1418
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAE-RYRELKEELKE----------------LEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1419 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1498
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1499 KRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVELQSKRASFAEKT 1578
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1579 AQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1658
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1659 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEATAA 1735
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1736 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1810
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1811 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1890
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1891 SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKE-------LAEQEAARQRQ 1963
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEalgpvnlLAIEEYEELEE 795
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
146-250 |
1.61e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 141.35 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 146 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 225
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 40849888 226 LLDPEDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
34-135 |
1.89e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 111
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 40849888 112 RNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
32-133 |
2.21e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 140.22 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 32 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 110
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 40849888 111 IRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
30-137 |
2.59e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 140.35 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 107
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 40849888 108 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
146-250 |
2.74e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.53 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 146 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 225
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 40849888 226 LLDPEDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1467-2050 |
2.08e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 155.48 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1467 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQR---KRQAE-AELALRVKAEAEaAREKQRALQALDELKLQAEEAER 1539
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLeplERQAEkAERYRELKEELK-ELEAELLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1540 RLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERE 1619
Cdd:COG1196 247 ELEELEAELEE-----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1620 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1699
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1700 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1779
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1780 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALkEKEAENERLRRLA 1859
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY-EAALEAALAAALQ 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1860 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGR 1939
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1940 IRSNAEDTMRSK---ELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2016
Cdd:COG1196 630 ARLEAALRRAVTlagRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
570 580 590
....*....|....*....|....*....|....
gi 40849888 2017 AEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQR 2050
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
149-250 |
6.69e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 136.15 E-value: 6.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 40849888 229 PEDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
29-137 |
1.59e-36 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 135.44 E-value: 1.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 107
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 40849888 108 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
153-254 |
4.79e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.71 E-value: 4.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 40849888 232 VDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1438-2038 |
6.19e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 150.86 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1438 RIEEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1517
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1518 REKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtqlre 1597
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1598 eaERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1677
Cdd:COG1196 340 --EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1757
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1758 ASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 1834
Cdd:COG1196 498 EAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1835 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglVEDTLRQRRQVEE 1914
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1915 EIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRK 1994
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 40849888 1995 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2038
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
134-250 |
1.99e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.87 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 134 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 213
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 214 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1669-2231 |
4.70e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.16 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1669 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1748
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1749 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKL 1828
Cdd:COG1196 300 LEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1829 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQ 1908
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1909 RRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEE 1988
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1989 AARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL 2068
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2069 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2148
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2149 KQAADAEMEKHKKFAE-QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQME 2227
Cdd:COG1196 698 ALLAEEEEERELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
....
gi 40849888 2228 ELGK 2231
Cdd:COG1196 778 ALGP 781
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1303-1890 |
5.02e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.69 E-value: 5.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1374
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1375 AELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTE 1454
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1455 RQRGGAEDELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1516
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1517 AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLR 1596
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1597 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQ 1671
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1672 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRA 1751
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1752 EMEVLLASKARAEEESRSTSEKSKQRleaeagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI 1831
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1832 SEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 1890
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
33-138 |
1.73e-33 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 127.18 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 109
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
150-250 |
5.34e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.21 E-value: 5.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 40849888 230 EDVDVPQPDEKSIITYVSSLY 250
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
34-137 |
1.43e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 123.94 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 111
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 40849888 112 RNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
34-137 |
1.72e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 123.58 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 112
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 40849888 113 NDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1334-2040 |
2.80e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 139.89 E-value: 2.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1334 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELqrrmqeEVTRREEAAVDAQQQKRSiqEELQH 1413
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA------EEARKAEDAKRVEIARKA--EDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1414 LRQSSEAEiqaKAQQVEAAERS-RMRIEEEIRvvrlqletterqrgGAEDELQALRARAEEAEAQKRQAQ--EEAERLRR 1490
Cdd:PTZ00121 1166 AEEARKAE---DAKKAEAARKAeEVRKAEELR--------------KAEDARKAEAARKAEEERKAEEARkaEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1491 QVQDESQRKRQAEAELALRVKaEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVA--LETAQRSAEVELQ 1568
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1569 SKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAlrlRLQAEEVAQQKSLAQ 1648
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1649 ADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELAR 1727
Cdd:PTZ00121 1385 KKAEEKKKADEAKK----KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1728 LQHEATAATQKRQeleAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAlAEEAKRQRQ 1807
Cdd:PTZ00121 1459 AEEAKKKAEEAKK---ADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK-AEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1808 LAEEDAARQRAEAERVLTEKLA-AISEATRLKT-----EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE 1881
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1882 ERLAQLRKASESEL--------ERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDtMRSKEL 1953
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIkaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1954 AEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2033
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
....*..
gi 40849888 2034 KRLQAEE 2040
Cdd:PTZ00121 1766 EEKKAEE 1772
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
12-133 |
6.02e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 124.00 E-value: 6.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 12 DEQDFIQAYEEVREK-YKDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFH 89
Cdd:cd21316 30 NENSSARLFERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIH 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 40849888 90 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 133
Cdd:cd21316 110 CLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
149-247 |
6.54e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 122.15 E-value: 6.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 40849888 229 PEDVDVPQPDEKSIITYVS 247
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
137-252 |
9.30e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 121.87 E-value: 9.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 137 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 216
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 217 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 252
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
153-254 |
9.85e-32 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 121.22 E-value: 9.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 40849888 232 VDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
155-250 |
1.27e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.22 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 155 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 233
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 40849888 234 VPQPDEKSIITYVSSLY 250
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
153-255 |
2.07e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 117.72 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 230
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 40849888 231 DVDVPQPDEKSIITYVSSLYDAMPR 255
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
149-247 |
2.91e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 117.24 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 40849888 229 PEDVDVPQPDEKSIITYVS 247
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
30-139 |
3.55e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.30 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 105
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 40849888 106 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 139
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
135-262 |
3.62e-30 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 117.88 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 135 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 214
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 40849888 215 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQDG 262
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF---SGAQKA 123
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
33-135 |
8.48e-30 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 116.04 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1772-2455 |
1.74e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.06 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1772 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedaaRQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1851
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1852 NERLRRLAEDEAFQRRRLEEQAAqhkadiEERLAQLRKASESELERQkglvEDTLRQRRQVEEEIMALKASFEKAAAGKA 1931
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1932 ELELELgrIRSNAEDTMRSKELAEQEAARQRQLAAEEEQrrreaeervqrsLAAEEEAARQRKVALEEVERLKAKVEEAR 2011
Cdd:COG1196 341 ELEEEL--EEAEEELEEAEAELAEAEEALLEAEAELAEA------------EEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2012 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAER 2091
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2092 EAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE--MEKHKKFAEQTLRQ 2169
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2170 KAQVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2249
Cdd:COG1196 567 KAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2250 NTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2329
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2330 EQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgek 2405
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL--- 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 40849888 2406 lhrtelaTQEKVTLVQTLeiqrqqsdqdaERLREAIAELEREKEKLKQEA 2455
Cdd:COG1196 801 -------SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
883-960 |
1.76e-29 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 113.85 E-value: 1.76e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 883 LAWQSLNRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQS 960
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1388-2177 |
2.77e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 130.26 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1388 EEVTrrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQAL 1467
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1468 RARAEEA----EAQKRQaqEEAERLRRQVQDESQRK----RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAER 1539
Cdd:PTZ00121 1108 TGKAEEArkaeEAKKKA--EDARKAEEARKAEDARKaeeaRKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1540 RLRQAE----AERARQVQVAletaqRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREE 1615
Cdd:PTZ00121 1186 EVRKAEelrkAEDARKAEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1616 AERELERWQ--LKANEALR---LRlQAEEVAQQKSLAQADaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1690
Cdd:PTZ00121 1261 RMAHFARRQaaIKAEEARKadeLK-KAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1691 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL-EAELAKVRAEMEVLLASKARAEEESRS 1769
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1770 TSEKSKQRLEA-----EAGRFRELAEEAARLRALAEEAKRQRQL---AEE----DAARQRAEAERVLTEKLAAISEATRL 1837
Cdd:PTZ00121 1419 KADEAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1838 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ---HKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEE 1914
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1915 EIMALKASFEKAAAGKAELELELGRIRSnaEDTMRSKELAEQEAARQRqlaaeeeqrrreaeervQRSLAAEEEaarQRK 1994
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIK-----------------AEELKKAEE---EKK 1633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1995 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEA 2074
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2075 ARRAAEEAEEAREQAEREAAQSRKQVEEAERlkqsaeeqaqaqaqaqaAAEKLRKEAEqeaarraqaeqaalKQKQAADA 2154
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKK-----------------KAEEAKKDEE--------------EKKKIAHL 1762
|
810 820
....*....|....*....|...
gi 40849888 2155 EMEKHKKFAEQTLRQKAQVEQEL 2177
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1303-2019 |
4.11e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.02 E-value: 4.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQ-AKAQAEL-E 1378
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSELEEEiEELQKELyA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1379 ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE---AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTER 1455
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1456 QRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD-ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQA 1534
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1535 EEAERRLRQAEaERARQVQVALETAQRSAEVELQSKRASFAektaqLERTLQEEHVTVTQLREEAERRAQQQAEAERARE 1614
Cdd:TIGR02168 453 QEELERLEEAL-EELREELEEAEQALDAAERELAQLQARLD-----SLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1615 EAERELERWQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR---- 1687
Cdd:TIGR02168 527 ELISVDEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvakd 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1688 -----------------------QLAEGTAQQRLAAEQELI---------------RLRAETEQGEQQRQL----LEEEL 1725
Cdd:TIGR02168 607 lvkfdpklrkalsyllggvlvvdDLDNALELAKKLRPGYRIvtldgdlvrpggvitGGSAKTNSSILERRReieeLEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1726 ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAE--EAARLRALAEEAK 1803
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL-RKDLARLEAEVEQLEERIAqlSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1804 RQRQLAEEDAARQRAEAERVLTEKLAAisEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1883
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIE--QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1884 LAQLRKASEsELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELgrirSNAEDTMRSKELAEQEAARQRQ 1963
Cdd:TIGR02168 844 EEQIEELSE-DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL----EELSEELRELESKRSELRRELE 918
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1964 LAAEEEQRRREAEERVQRSLAAEEEAARQR-KVALEEVERLKAKVE-EARRLRERAEQ 2019
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEdDEEEARRRLKR 976
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1711-2558 |
4.94e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.11 E-value: 4.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1711 TEQGEQQRQLLEEELARLQHEATAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1788
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1789 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlTEKLAAISEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1866
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1867 RRLEEQaaqHKADIEERLAQLRKASESelerqkglvedtlrqrRQVEEeimalkasfekaaAGKAELELELGRIRsNAED 1946
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1947 TMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERlkaKVEEARRLRERAEQESARQLQ 2026
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2027 LAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERL 2106
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2107 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2186
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2187 TDHQksildEELQRLKAEVTEAARQRSQVEEelfsvRVQMEELGKlkaRIEAENRALILRDKDNTQRFLEE---EAEKMK 2263
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEAK 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2264 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2339
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2340 eQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVTL 2419
Cdd:PTZ00121 1577 -NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2420 VQTL-------EIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ-----EQILQETQALQKSFLSE 2487
Cdd:PTZ00121 1649 AEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEEEN 1728
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 2488 KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRK 2558
Cdd:PTZ00121 1729 KIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
153-252 |
2.73e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.61 E-value: 2.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 231
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 40849888 232 VDVPQPDEKSIITYVSSLYDA 252
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
137-261 |
5.66e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 137 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 216
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 40849888 217 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQD 261
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF---SGAQK 119
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1683-2495 |
1.39e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.48 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1683 LEKQRQLAEGTAQQRLAAEQELIRLRAE------TEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmEVL 1756
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDgnhegkAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAE-EAK 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1757 LASKARAEEESRStsEKSKQRLEaEAGRFREL--AEEAARlralAEEAKRQRQLAEEDAARQRAEAERVlteKLAAISEA 1834
Cdd:PTZ00121 1105 KTETGKAEEARKA--EEAKKKAE-DARKAEEArkAEDARK----AEEARKAEDAKRVEIARKAEDARKA---EEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1835 TRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRRRLEEQAaqHKADIEERLAQLRKASES---ELERQKGLVEDTLR 1907
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEElrkaEDARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAkkdAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1908 QRRQVEEEIMALKAsfEKAAAGKAELELELGRIRSnAEDTMRSKELAEQEAARQrqlaaeeeqrrreaeervQRSLAAEE 1987
Cdd:PTZ00121 1253 EIRKFEEARMAHFA--RRQAAIKAEEARKADELKK-AEEKKKADEAKKAEEKKK------------------ADEAKKKA 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1988 EAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAfvvqqreeelqqtlqqeqnmLER 2067
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA--------------------AEK 1371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2068 LRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALK 2147
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAK 1450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2148 QKQAADAEMEKHKKFAEQT-----LRQKAQVEQELTTLRLQLEETDHQKsildEELQRlKAEVTEAARQRSQVEEelfsv 2222
Cdd:PTZ00121 1451 KKAEEAKKAEEAKKKAEEAkkadeAKKKAEEAKKADEAKKKAEEAKKKA----DEAKK-AAEAKKKADEAKKAEE----- 1520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2223 RVQMEELGKLKARIEAEN--RALILRDKDNTQRFLE----EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2296
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEakKAEEKKKADELKKAEElkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2297 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ--EQARRLQEDKEQMAQQL--VEETQGFQRTLEA----ERQRQLEMS 2368
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKkvEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAkkaeEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2369 AEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHRTELATQEKVTLVQTLEIQRQQsDQDAERLREAIAElEREK 2448
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEA-EEDKKKAEEAKKD-EEEK 1756
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 40849888 2449 EKLKQEAKLLQLKSEEmqtvqqeqILQETQALQKSFLSEKDSLLQRE 2495
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEE--------IRKEKEAVIEEELDEEDEKRRME 1795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1621-2212 |
1.93e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.12 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1621 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1700
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE----LELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1701 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRLEA 1780
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1781 EAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1860
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1861 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFE-KAAAGKAELELELGR 1939
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyEAALEAALAAALQNI 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1940 IRSNAEDTMRSKELAEQEAARQR---QLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2016
Cdd:COG1196 552 VVEDDEVAAAAIEYLKAAKAGRAtflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2017 AEQESARQLQLAQEAAQKRLQAEEkahafvvqqREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQS 2096
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEG---------GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2097 RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQ---- 2172
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpv 782
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 40849888 2173 ---VEQELTTLRLQLEETDHQKSILDEELQRLK---AEVTEAARQR 2212
Cdd:COG1196 783 nllAIEEYEELEERYDFLSEQREDLEEARETLEeaiEEIDRETRER 828
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
33-135 |
3.94e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.34 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1331-2375 |
8.76e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.47 E-value: 8.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAELEARELQRRMQEEVTRR-EEAAVDAQQQKRSIQ 1408
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIARLvGEATKEAEALKAEAE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1409 EELQhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVvrlQLETTERQrggAEDelqALRARAEEAEAQKRQAQEEAERL 1488
Cdd:NF041483 334 QALA------DARAEAEKLVAEAAEKARTVAAEDTAA---QLAKAART---AEE---VLTKASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1489 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELKLQaEEAeRRLRqAEAERARQVQVA----LETAQRSAE 1564
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLRAEAVAegerIRGEARREA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1565 VELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerAREEAERELERWQLKANE-ALRLRLQAEEVAQQ 1643
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADE-----------------------LRSTATAESERVRTEAIErATTLRRQAEETLER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1644 kslAQADAEKQKeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAEteqGEQQRQLLE 1722
Cdd:NF041483 529 ---TRAEAERLR----------AEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTE---AEERLTAAE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1723 EELARLQHEataATQKRQELEAELAKVRAEM-EVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEEAA-RLRA-LA 1799
Cdd:NF041483 593 EALADARAE---AERIRREAAEETERLRTEAaERIRTLQAQAEQE----AERLRTEAAADASAARAEGENVAvRLRSeAA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1800 EEAKRQRQLAEEDAARQRAE----AERVLTEKL----AAISEATRLKTEAEIALKEKEAENERLRRLAEDE-----AFQR 1866
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEaaaaAERVGTEAAealaAAQEEAARRRREAEETLGSARAEADQERERAREQseellASAR 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1867 RRLEEQAAQHKADIEE---RLAQLRKASESELERQKGLVEDTlrqRRQVEEEIMALKASFEKAAA-GKAELELELGRIRS 1942
Cdd:NF041483 746 KRVEEAQAEAQRLVEEadrRATELVSAAEQTAQQVRDSVAGL---QEQAEEEIAGLRSAAEHAAErTRTEAQEEADRVRS 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1943 naeDTMRSKELAEQEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEE-ARRLRERA---- 2017
Cdd:NF041483 823 ---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEAsdtl 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2018 ---EQESARQLQLAQEAAQK-RLQAEEKAHAFVVQQREEELQQTLQQEQNMlERLRSEAEAARRAAEEAEEAREQAEREA 2093
Cdd:NF041483 887 asaEQDAARTRADAREDANRiRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQLIAE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2094 AQS---RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA------------ADAEMEK 2158
Cdd:NF041483 966 ATGeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankrrseaaeqADTLITE 1045
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2159 HKKFAEQtLRQKAQVEQELTTLRLQlEETDHQKSILDEELQRLKAEVT-----EAARQRSQVEEELFSVRVQM----EEL 2229
Cdd:NF041483 1046 AAAEADQ-LTAKAQEEALRTTTEAE-AQADTMVGAARKEAERIVAEATvegnsLVEKARTDADELLVGARRDAtairERA 1123
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2230 GKLKARIEAENRALilrdkdnTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlrQLAEEDLAQQRALAE---KMLKEKMQ 2306
Cdd:NF041483 1124 EELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE-----QLAEAEAKAKELVSDansEASKVRIA 1191
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 2307 AVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAEAERLK 2375
Cdd:NF041483 1192 AVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
137-252 |
9.18e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.89 E-value: 9.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 137 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 216
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 217 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1473-2455 |
1.24e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.09 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1473 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELKLQAE-EAERRLR 1542
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1543 QAEAERARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtqlreEAERRAQQQAEAERAREEAERE 1619
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE---------AESARAEAEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1620 LERWQLKANEALRlrlQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQRLA 1699
Cdd:NF041483 224 LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAKEAAAKQLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1700 AeqelirlrAETeQGEQQRQLLEEELARLQHEATA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSK 1775
Cdd:NF041483 298 S--------AES-ANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1776 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI---------------SEATRLKTE 1840
Cdd:NF041483 369 AARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1841 AEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIEErlaqLRKASESELERQKG-LVEDTLRQRRQVEE 1914
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE----LRSTATAESERVRTeAIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1915 eimALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLA------AEEE 1988
Cdd:NF041483 525 ---TLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAeealadARAE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1989 AARQRKVALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqNMLE 2066
Cdd:NF041483 602 AERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGE-----------------------NVAV 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2067 RLRSEAEaarraaeeaeeareqaereaaqsrkqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2146
Cdd:NF041483 659 RLRSEAA---------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 kqkQAADAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2214
Cdd:NF041483 702 ---AAAQEEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2215 -VEEELFSVRVQM-EELGKLkaRIEAENRAlilrdkDNTQRFLEEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDLAQ 2292
Cdd:NF041483 779 qVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEA 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2293 QRALAEKMLKEkmqAVQEATRLKAEAELLQQQ-------------------KELAQEQARRLQEDKEQMAQQLVEETQGF 2353
Cdd:NF041483 849 AKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAQADRLIGEATSE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2354 QRTLEAE-----RQRQLEMSAEAERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIgeklhrTELATQEKVTLVQTLEIQR 2427
Cdd:NF041483 926 AERLTAEaraeaERLRDEARAEAERVRADAAAQAeQLIAEATGEAERLRAEAAET------VGSAQQHAERIRTEAERVK 999
|
1050 1060
....*....|....*....|....*....
gi 40849888 2428 QQSDQDAERLR-EAIAELEREKEKLKQEA 2455
Cdd:NF041483 1000 AEAAAEAERLRtEAREEADRTLDEARKDA 1028
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
33-138 |
2.03e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1330-2020 |
2.41e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1330 LRRMEEEERLAEQQRaEERERLAEVEAAL------EKQRQLAEAHAQAKAqAELEARELQRRMQEEVTRREEAaVDAQQQ 1403
Cdd:TIGR02168 202 LKSLERQAEKAERYK-ELKAELRELELALlvlrleELREELEELQEELKE-AEEELEELTAELQELEEKLEEL-RLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1404 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1483
Cdd:TIGR02168 279 LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1484 EAERLRRQVQDESQRKRQAEAELaLRVKAEAEAAREKQRALQAldelklQAEEAERRLRQAEAERARQVQVALETAQRSA 1563
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQL-ETLRSKVAQLELQIASLNN------EIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1564 EVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAEREL----------------------- 1620
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsegvkal 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1621 ---------------------ERWQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR 1676
Cdd:TIGR02168 512 lknqsglsgilgvlselisvdEGYEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1677 ELAEQE-------------------------------------LEKQRQL-----------------------AEGTAQQ 1696
Cdd:TIGR02168 592 EILKNIegflgvakdlvkfdpklrkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1697 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK--- 1773
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaq 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1774 -SKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAeialKEKEAEN 1852
Cdd:TIGR02168 752 lSKELTELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1853 ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKASFEKAAAGKAE 1932
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1933 LELELGRIRSNAEDTMRSKE-----LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKV 2007
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAqlelrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKI 981
|
810
....*....|...
gi 40849888 2008 EEARRLRERAEQE 2020
Cdd:TIGR02168 982 KELGPVNLAAIEE 994
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1327-2043 |
4.07e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.16 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1327 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAELEARELQRRMQEEVTR-REEA 1396
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1397 AVDAQQQKRSIQEELQHLRqsSEAEiQAKAQQVEAAERSRMRIEEEIRVVRLQLE-TTERQRGGAEDELQALRARAEE-- 1473
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1474 --AEAQKRQAQEEAERLRRQVQDESQRKRqaeaelalrvkaeAEAArEKQRALQAldelklQAEEAERRLRQAEAERARQ 1551
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLR-------------TEAA-ERIRTLQA------QAEQEAERLRTEAAADASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1552 VQVALEtaqrSAEVELQSKrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeaerelerwqlKANEAL 1631
Cdd:NF041483 649 ARAEGE----NVAVRLRSE-------------------------------------------------------AAAEAE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1632 RLRLQAEEVAQQ-KSLAQADAEKqkeEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI---RL 1707
Cdd:NF041483 670 RLKSEAQESADRvRAEAAAAAER---VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1708 RAETEQGEQQRqLLEEELARLQHEATAATQKRQELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAG 1783
Cdd:NF041483 747 RVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAY 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1784 RFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED 1861
Cdd:NF041483 826 AERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADARE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1862 EAFQRRrlEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAElelelgRIR 1941
Cdd:NF041483 903 DANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLR 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1942 SNAEDTMRSkelAEQEAARQRQLAAEEEQRrreaeervqrslaAEEEAARQRKVALEEVERL--KAKVEEARRLRERAEQ 2019
Cdd:NF041483 975 AEAAETVGS---AQQHAERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQ 1038
|
730 740
....*....|....*....|....
gi 40849888 2020 ESARQLQLAQEAAQKRLQAEEKAH 2043
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
18-137 |
4.98e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 106.00 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 18 QAYEEVR-EKYKDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQN 93
Cdd:cd21247 3 TEYEKGHiRKLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLEN 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 40849888 94 VQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21247 83 NSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
37-134 |
2.18e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 37 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 112
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 40849888 113 NDDIADGnPKLTLGLIWTIILH 134
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
137-252 |
2.48e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 104.00 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 137 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 216
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 217 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
155-250 |
2.62e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.00 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 155 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 233
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 40849888 234 VPQPDEKSIITYVSSLY 250
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
149-255 |
7.44e-25 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 101.98 E-value: 7.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 149 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 225
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 40849888 226 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 255
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1670-2508 |
2.27e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 113.61 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1670 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1749
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1750 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKla 1829
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1830 aiseatrlkTEAEIALKEKEAENERLRRLAEDeafqrrrLEEQAAQHKADIEERLAQLRKASeSELERQKGLVEDTLRQR 1909
Cdd:TIGR02168 354 ---------ESLEAELEELEAELEELESRLEE-------LEEQLETLRSKVAQLELQIASLN-NEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1910 RQVEEEIMALKASFEKAAagKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRReaeervqrSLAAEEEA 1989
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD--------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1990 ARQRKVALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQAEEKAHAFVVQQREEELQ 2055
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2056 QTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEA 2135
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2136 ARRAQAEQAALKQKQAAdaemeKHKKFAEQTLRQKaqveQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV 2215
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITG-----GSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2216 EEELFSVRVQMEELGKLKARIEAENRALiLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA 2295
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2296 LAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLVEETQgfqrtleaerqrqlEMSAEAERL 2374
Cdd:TIGR02168 797 ELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------------ELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2375 KLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQE 2454
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2455 -AKLLQLKSEEMQTVQQEqilqetqALQKSFLSEKDSLLQRERfIEQEKAKLEQL 2508
Cdd:TIGR02168 938 iDNLQERLSEEYSLTLEE-------AEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
34-137 |
3.19e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.05 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 109
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
151-250 |
4.58e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 99.56 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 151 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 230
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 40849888 231 D-VDVPQPDEKSIITYVSSLY 250
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1340-2596 |
7.34e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 111.84 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAELEARELQRRM---QEEVTRRE--EAAVD-----AQQQKRSIQ 1408
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAELHTEAVQRRQqldQELAERRQtvESHVNenvawAEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1409 EELQHLRQSSEAEiqakAQQVEAAERSRM-RIEEEirvvrlqlettERQRGGAEDElqalRARAEeAEAQKRQAQEEAER 1487
Cdd:NF041483 163 SQARRLLDESRAE----AEQALAAARAEAeRLAEE-----------ARQRLGSEAE----SARAE-AEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1488 LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQaeEAERRLRQAEAERARQVQVALETAqrsaevel 1567
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA-------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1568 qSKRASFAEKT-AQLERTLQEEHVTVTQlrEEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1646
Cdd:NF041483 293 -AKQLASAESAnEQRTRTAKEEIARLVG--EATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1647 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEEL 1725
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1726 ARLQHEATaatQKRQELEAELAKVRAEmevllaskARAE-----EESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALA 1799
Cdd:NF041483 443 RRLRGEAE---QLRAEAVAEGERIRGE--------ARREavqqiEEAARTAEELLTKAKADADELRSTATaESERVRTEA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1800 -EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRLEEQAAQHK 1877
Cdd:NF041483 512 iERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQAEAAEElTRLHTEAEERL 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1878 ADIEERLAQLRkaSESELERQKGlVEDTLRQRRQVEEEIMALKAsfekaaagKAELELElgRIRSNA-EDTMRSKELAEQ 1956
Cdd:NF041483 589 TAAEEALADAR--AEAERIRREA-AEETERLRTEAAERIRTLQA--------QAEQEAE--RLRTEAaADASAARAEGEN 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1957 EAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkVALEEVERLKAKVEEARRLRERAEQ--ESARQlqlaqEAAQK 2034
Cdd:NF041483 656 VAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAER-VGTEAAEALAAAQEEAARRRREAEEtlGSARA-----EADQE 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2035 RLQAEEKAHAFVVQQREEELQQTLQQEqnmleRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQA 2114
Cdd:NF041483 730 RERAREQSEELLASARKRVEEAQAEAQ-----RLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEH 804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2115 QAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQkAQVEQElttlRLQLEETDHQKSIL 2194
Cdd:NF041483 805 AAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE-AIAEAE----RLRSDASEYAQRVR 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2195 DEELQRLKAEVTEAARQRSQVEEELFSVR----VQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAA 2270
Cdd:NF041483 880 TEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQA 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2271 R--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKE----KMQAVQEATRLKAEA--ELLQQQKELAQEQARRLQEDKEQM 2342
Cdd:NF041483 960 EqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEaervKAEAAAEAERLRTEAreEADRTLDEARKDANKRRSEAAEQA 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2343 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeedaqrfRKQAEEIGEKLHRTELATQEKVTLvqt 2422
Cdd:NF041483 1040 DTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAE--------RIVAEATVEGNSLVEKARTDADEL--- 1108
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2423 LEIQRQQSDQDAERLREAIAELEREKEKLKQEAKllQLKSEEMQTVQQ---------EQILQETQALQKSFLSEKDSLLQ 2493
Cdd:NF041483 1109 LVGARRDATAIRERAEELRDRITGEIEELHERAR--RESAEQMKSAGErcdalvkaaEEQLAEAEAKAKELVSDANSEAS 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2494 RERFIEQEKAklEQLFQDEVAKAKQLqeeqqrqqqqmeqekqelvasMEEARRRQREAEEGVRRkqeelqrleqqrqqqe 2573
Cdd:NF041483 1187 KVRIAAVKKA--EGLLKEAEQKKAEL---------------------VREAEKIKAEAEAEAKR---------------- 1227
|
1290 1300
....*....|....*....|...
gi 40849888 2574 klLAEENQRLRERLQRLEEEHRA 2596
Cdd:NF041483 1228 --TVEEGKRELDVLVRRREDINA 1248
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
150-250 |
1.14e-23 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 98.27 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 229
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 40849888 230 EDVDVPQ-PDEKSIITYVSSLY 250
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
153-253 |
1.45e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 97.92 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 232
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 40849888 233 DVPQPDEKSIITYVSSLYDAM 253
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1340-2044 |
3.31e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 109.76 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQA-KAQAELEARELQRRMQEEV-TRREEAAVDAQQQKRSIQEELQHLRQ 1416
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAeKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1417 SSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRR------ 1490
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEE--------------LQKELYALANEISRLEQQKQILRERLANLERqleele 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1491 -QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLR--QAEAERARQVQVALETAQRSAEVEL 1567
Cdd:TIGR02168 323 aQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1568 QSKRASFAEKTAQLERTLQEehvtvtqlreEAERRAQQQAEAERAREEAERELERWQLKANEALRlRLQAEEVAQQKSLA 1647
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1648 QADAEKQKEeaerearrrgKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQ---------ELIRLRAETEQG--- 1714
Cdd:TIGR02168 472 EAEQALDAA----------ERELAQLQARlDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1715 --------------EQQRQ----LLEEELARL----------------QHEATAATQKRQELEAELAKVRAEMEVLLA-- 1758
Cdd:TIGR02168 542 alggrlqavvvenlNAAKKaiafLKQNELGRVtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1759 --------SKARAEEESRSTSEK-----------------SKQRLEAEAGRF---RELAEEAARLRALAEEAKRQRQlAE 1810
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-AL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1811 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKA 1890
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1891 SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQlaaeeeq 1970
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------- 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1971 rrreAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2044
Cdd:TIGR02168 853 ----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1845-2595 |
6.84e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.08 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1845 LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE-LERQKGLVEDTLRQRRQVEEEimalkASF 1923
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEAKKTETGKAEE-----ARK 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1924 EKAAAGKAELELELGRIRsNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV-------A 1996
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEAR-KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrkaeelrK 1195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1997 LEEVERLKA--KVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEA 2074
Cdd:PTZ00121 1196 AEDARKAEAarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2075 ARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAeqaalKQKQAADA 2154
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAK-----KAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2155 EMEKHKKFAEQTLRQKAQVEQElttlrlqlEETDHQKSildEELQRLKAEVTEAARQRSQVEEElfsvRVQMEELgklKA 2234
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKK--------KEEAKKKA---DAAKKKAEEKKKADEAKKKAEED----KKKADEL---KK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2235 RIEAENRALILRDKDNTQRfleeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRL 2314
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2315 KAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAErlKLRMAEMSRaqaRAEEdaqr 2394
Cdd:PTZ00121 1489 KKKAE---EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE--EKKKADELK---KAEE---- 1556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2395 fRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQqsdqdAERLR-EAIAELEREKEKLKQEakllQLKSEEMQTVQQEQI 2473
Cdd:PTZ00121 1557 -LKKAEEK-KKAEEAKKAEEDKNMALRKAEEAKK-----AEEARiEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2474 LQETQalqksflsEKDSLLQRERFIEQEKAKLEQlfqdeVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEE 2553
Cdd:PTZ00121 1626 KKAEE--------EKKKVEQLKKKEAEEKKKAEE-----LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 40849888 2554 GVRRKQEELQRLEQQRQQQekllaEENQRLRERLQRLEEEHR 2595
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKE-----AEEKKKAEELKKAEEENK 1729
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
150-254 |
7.93e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 96.01 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 40849888 230 EDVDVPQPDEKSIITYVSSLYDAMP 254
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
150-248 |
2.43e-22 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 94.61 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 40849888 229 PEDVDVPQPDEKSIITYVSS 248
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1530-2409 |
4.42e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.91 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1530 LKLQAEEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVTVTQLREEAERRAQQQA 1607
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1608 eaerareeaerelerwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAE-----QE 1682
Cdd:TIGR02168 247 ----------------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1683 LEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskar 1762
Cdd:TIGR02168 300 LEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1763 aeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-LAAISEATRLKTEA 1841
Cdd:TIGR02168 369 ---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1842 EIALKEKEAENERLRRLAEdEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT---LRQRRQVEEEIMA 1918
Cdd:TIGR02168 446 EEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkalLKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1919 LKASFEKAAAGKAELELELGRIRSNAedTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALE 1998
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1999 EVERLKAKVEEARRL----------RERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL 2068
Cdd:TIGR02168 603 VAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2069 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2148
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2149 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEE 2228
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2229 LGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAV 2308
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2309 QEATRLKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEMS------------AEAE 2372
Cdd:TIGR02168 918 EELREKLAQLELrlegLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENKikelgpvnlaaiEEYE 996
|
890 900 910
....*....|....*....|....*....|....*..
gi 40849888 2373 RLKLRMAEMSRAQaraeEDAQRFRKQAEEIGEKLHRT 2409
Cdd:TIGR02168 997 ELKERYDFLTAQK----EDLTEAKETLEEAIEEIDRE 1029
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
33-138 |
7.33e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
33-138 |
7.89e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.00 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 33 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1427-2243 |
8.32e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.14 E-value: 8.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1427 QQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAED-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1495
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1496 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR--QVQVALETAQRSAEVELQSKRAS 1573
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1574 FAEKTAQLERtLQEEHvtvtqlreeaerraqqqaeaerarEEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEK 1653
Cdd:TIGR02168 339 LAELEEKLEE-LKEEL------------------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1654 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1733
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1734 AATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA-- 1809
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvv 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1810 --EEDAARQRAEAERVLTEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQR--RRLEEQAAQHKADIEERLA 1885
Cdd:TIGR02168 552 veNLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1886 QLRKASEselerqkglVEDTLRQRRQVEEEIMALKASFEKAAAG----KAELELELGRI--RSNAEDTMRSKELAEQEAA 1959
Cdd:TIGR02168 624 GVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILerRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1960 RQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAE 2039
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2040 EKAHAfvVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQ 2119
Cdd:TIGR02168 775 EELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2120 AQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQ 2199
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 40849888 2200 RLKAEVteaARQRSQVEEElfsVRVQMEELGKLKARIEAENRAL 2243
Cdd:TIGR02168 933 GLEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1005-1550 |
1.33e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1005 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1084
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1085 RSTQGAEEVLKTHEEHLKEAQAvpATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1164
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1165 RWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALL 1244
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1245 EEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRyseLTTLTSQYIK 1324
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA---LAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1325 FISETLRRMEEEERLAEQQRAEER--ERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQ 1402
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1403 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggAEDELQALRARAEEAEAQKRQAQ 1482
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER---LAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1483 EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR 1550
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1090-1890 |
8.62e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.67 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1090 AEEVLKTHEEHLKEAQAvpatlqELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1169
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1170 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIER 1249
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1250 hgekveecqkfAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISET 1329
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1330 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE------------LEARE---------LQRRMQE 1388
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselISVDEgyeaaieaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1389 EVTRREEAAVDAQqqkrSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALR 1468
Cdd:TIGR02168 550 VVVENLNAAKKAI----AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1469 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAeaeLALRVKAEAEAAREKQRalQALDELKLQAEEAERRLRQAEAE- 1547
Cdd:TIGR02168 626 LVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAl 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1548 -RARQVQVALETAQRSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERwQLK 1626
Cdd:TIGR02168 701 aELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELA 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1627 ANEALRLRLQAeEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIR 1706
Cdd:TIGR02168 779 EAEAEIEELEA-QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIES 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1707 LRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEAG 1783
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEV 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1784 RFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLTEKLAAISEATRLkteaeiALKEKEAENERLRRLaede 1862
Cdd:TIGR02168 937 RIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL---- 1005
|
810 820
....*....|....*....|....*...
gi 40849888 1863 afqrrrleeqaAQHKADIEERLAQLRKA 1890
Cdd:TIGR02168 1006 -----------TAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1865-2454 |
9.15e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 9.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1865 QRRRLEEQAA---QHKADIEERLAQLRKASE---------SELERQKGLVEdtlRQRRQVEE-----------EIMALKA 1921
Cdd:COG1196 156 ERRAIIEEAAgisKYKERKEEAERKLEATEEnlerledilGELERQLEPLE---RQAEKAERyrelkeelkelEAELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1922 SFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVE 2001
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2002 RLKakvEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvvQQREEELQQTLQQEQNMLERLRSEAEAARRAAEE 2081
Cdd:COG1196 313 ELE---ERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2082 AEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKK 2161
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2162 FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENR 2241
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2242 AL-----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKA 2316
Cdd:COG1196 544 LAaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2317 EAELLQQQKELAQEQARRLQEDKE------QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEE 2390
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLRevtlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2391 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREA--------IAELEREKEKLKQE 2454
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELERELERLERE 775
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
782-848 |
1.08e-20 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.47 E-value: 1.08e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 782 QLKPRNpaHPVRGHVPLLAVCDYKQVEVTVHKGDQCQLVGPAQPFHWKVLGGSSSEAAVPSVCFLVP 848
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
154-251 |
1.14e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 90.10 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 154 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 232
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 40849888 233 DVPQPDEKSIITYVSSLYD 251
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1679-2556 |
2.59e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 100.29 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1679 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-TAATQKRQELEAELAKVRAEMEV 1755
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1756 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLtekLAAISE 1833
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1834 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAAQHKADIEERLAQLRKASESELE-------RQKGLV 1902
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1903 EDTLRQR-RQVEEEIMALKASFEK-AAAGKAELELELG-------RIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRR 1973
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALAdaraeaeKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1974 EAEERVQRSLAAEEEAARQRKVALEEVERLKAKV--------------------------EEARRLRERAEQ-------- 2019
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQlraeavae 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2020 ------ESARQ-LQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERL----RSEAEAARRAAEEAEEAREQ 2088
Cdd:NF041483 460 gerirgEARREaVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERAttlrRQAEETLERTRAEAERLRAE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2089 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlkqkqAADAEMEK-HKKFAEQTL 2167
Cdd:NF041483 540 AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA-----DARAEAERiRREAAEETE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2168 RQKAQVEQELTTLRLQLEetdhqksildEELQRLKaevTEAARQRSQVEEELFSVRVqmeelgKLKARIEAENRALILRD 2247
Cdd:NF041483 615 RLRTEAAERIRTLQAQAE----------QEAERLR---TEAAADASAARAEGENVAV------RLRSEAAAEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2248 KDNTQRFLEEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEkmlKEKMQAVQEATRLKAEAellQQQKE 2326
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVE 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2327 LAQEQARRLQED-----------KEQMAQQLVEETQGFQRTLE-------------AERQRQlEMSAEAERLKlrmAEMS 2382
Cdd:NF041483 750 EAQAEAQRLVEEadrratelvsaAEQTAQQVRDSVAGLQEQAEeeiaglrsaaehaAERTRT-EAQEEADRVR---SDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2383 RAQARAEEDAQRFRKQAEEIGEKLHrtELATQEKVTLVQTLEIQRQQSDQDAERLR----EAIAELEREKEKLKQEAKLL 2458
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAK--ALAERTVSEAIAEAERLRSDASEYAQRVRteasDTLASAEQDAARTRADARED 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2459 QLKSEEMQTVQQEQILQEtqALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELV 2538
Cdd:NF041483 904 ANRIRSDAAAQADRLIGE--ATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETV 981
|
970
....*....|....*...
gi 40849888 2539 ASMEEARRRQREAEEGVR 2556
Cdd:NF041483 982 GSAQQHAERIRTEAERVK 999
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1468-2356 |
3.91e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 99.66 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1468 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA 1546
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1547 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvtvtqlreeaeRRAQQQAEAERAREEAERELERWQLK 1626
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----------AKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1627 ANEALRLRLQAEEVAQQKSLAQAdaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIR 1706
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1707 LRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrFR 1786
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS---ED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER--------VLTEKLAAISEATRLKTEAEIALKEKEAEN---ERL 1855
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvllaliKDGVGGRIISAHGRLGDLGVAVENYKVAIStavIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1856 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRqrrqveeEIMALKASFEKAAAGKAELEL 1935
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN-------LAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1936 ELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEverlkAKVEEARRLRE 2015
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL-----AKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2016 RAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQ 2095
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2096 SRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2175
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2176 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFL 2255
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2256 EEEAEKMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2335
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|.
gi 40849888 2336 QEDKEQMAQQLVEETQGFQRT 2356
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSI 1029
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
150-249 |
4.44e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 229
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 40849888 230 ED-VDVPQPDEKSIITYVSSL 249
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1332-2070 |
8.23e-20 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 98.74 E-value: 8.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1332 RMEEEERlAEQQRAEERERLAEVEAALEKQRQLAEAHAQA-KAQAELEARELqrrmqeevtrREEAAVDAQQQKRSIQEE 1410
Cdd:NF041483 508 RTEAIER-ATTLRRQAEETLERTRAEAERLRAEAEEQAEEvRAAAERAAREL----------REETERAIAARQAEAAEE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1411 LQHLRQSSEAEIQAKAQQVEAA--ERSRMRIEEEIRVVRLQLETTERQR---GGAEDELQALRARA-EEAEAQKRQAQEE 1484
Cdd:NF041483 577 LTRLHTEAEERLTAAEEALADAraEAERIRREAAEETERLRTEAAERIRtlqAQAEQEAERLRTEAaADASAARAEGENV 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1485 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQrALQALDELKLQAEEAERRLRQAE----AERARQVQvALETAQ 1560
Cdd:NF041483 657 AVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERV-GTEAAEALAAAQEEAARRRREAEetlgSARAEADQ-ERERAR 734
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1561 RSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERElerwqlkanEALRLRLQAEEV 1640
Cdd:NF041483 735 EQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEE---------EIAGLRSAAEHA 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1641 AQQ-KSLAQADAEKQKEEAEREARrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRLRAETeqGEQQRQ 1719
Cdd:NF041483 806 AERtRTEAQEEADRVRSDAYAERE---RASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDA--SEYAQR 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1720 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRAL 1798
Cdd:NF041483 878 VRTEASDTLASAEQDAARTRADAREDANRIRSDAA---AQADRLIGEATSEAERLTAEARAEAERLRdEARAEAERVRAD 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1799 A-EEAKRQRQLAEEDAARQRAEAERVLTeklAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ---------RRR 1868
Cdd:NF041483 955 AaAQAEQLIAEATGEAERLRAEAAETVG---SAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRtldearkdaNKR 1031
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1869 LEEQAAQHKADIEERLAQ----LRKASE------SELERQKGLVEDTLRQR--RQVEEEIMALKASFEKAAAGKAELELE 1936
Cdd:NF041483 1032 RSEAAEQADTLITEAAAEadqlTAKAQEealrttTEAEAQADTMVGAARKEaeRIVAEATVEGNSLVEKARTDADELLVG 1111
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1937 LGR----IRSNAEDtMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLK-------- 2004
Cdd:NF041483 1112 ARRdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANseaskvri 1190
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2005 AKVEEARRLRERAEQESARQLQLAQ------EAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRS 2070
Cdd:NF041483 1191 AAVKKAEGLLKEAEQKKAELVREAEkikaeaEAEAKRTVEEGKRELDVLVRRREDINAEISRVQDVLEALES 1262
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
150-250 |
1.44e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 86.63 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 229
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 40849888 230 EDVDV--PQPDEKSIITYVSSLY 250
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1326-1957 |
1.66e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.45 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1326 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAELEARELQRRMqEEVTRREEAAVDAQQQKR 1405
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 SIQEELQHLRQSSEAEIQAKAQQVEAaersrmrIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR------ 1479
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1480 --------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEAER-- 1548
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1549 ARQVQVALETAQRSAEVELQSKRA--SFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREeaerelERWQLK 1626
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG------ERYATA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1627 ANEALRLRLQA-----EEVAQQ--KSLAQADAE----------KQKEEAEREARRRG------------KAEEQAVR--- 1674
Cdd:TIGR02169 541 IEVAAGNRLNNvvvedDAVAKEaiELLKRRKAGratflplnkmRDERRDLSILSEDGvigfavdlvefdPKYEPAFKyvf 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1675 QRELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1728
Cdd:TIGR02169 621 GDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1729 QHEATAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALaEEAKR 1804
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELKELEARIEEL-EEDLH 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1805 QRQLAEEDAARQRAEAE--------RVLTEKLAAISEATRlktEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQH 1876
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1877 KADIEERLAQLRKAsESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQ 1956
Cdd:TIGR02169 853 EKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
.
gi 40849888 1957 E 1957
Cdd:TIGR02169 932 E 932
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1303-1897 |
1.97e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 97.29 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEL 1377
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1378 EARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1457
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1458 GGAEDELQALRARA---EEAEAQKRQAQEEAERLRR----------QVQDESQRKRQAeAELALR-------VKAEAEAA 1517
Cdd:COG4913 422 RELEAEIASLERRKsniPARLLALRDALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLGgfaltllVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1518 rekqrALQALDELK----LQAEEAERRLRQAEAER------ARQVQVALETAQRSAEVELQsKRASFA--EKTAQLERTl 1585
Cdd:COG4913 501 -----ALRWVNRLHlrgrLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPEELRRH- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1586 qEEHVTVTQLREEAERRAQQQAEAERAreeaerelERWQL-KANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearr 1664
Cdd:COG4913 574 -PRAITRAGQVKGNGTRHEKDDRRRIR--------SRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1665 rgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQE 1741
Cdd:COG4913 637 --EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1742 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1821
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1822 RVLTE-KLAAISEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELER 1897
Cdd:COG4913 791 RAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
146-251 |
3.35e-19 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 85.77 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 146 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 225
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 40849888 226 LLDPEDV-DVPQPDEKSIITYVSSLYD 251
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
153-249 |
3.75e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 85.45 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 153 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 228
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 40849888 229 PEDVDVPQPDEKSIITYVSSL 249
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1931-2594 |
5.75e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1931 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQrslAAEEEAARQRKVALEEVERLKAKVEEA 2010
Cdd:COG1196 196 GELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELE---AELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2011 RRLRERAEQEsARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQtlqqeqnmLERLRseaeaarraaeeaeeareqae 2090
Cdd:COG1196 273 RLELEELELE-LEEAQAEEYELLAELARLEQDIARLEERRRELEER--------LEELE--------------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2091 reaaqsrkqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKhkkfAEQTLRQK 2170
Cdd:COG1196 323 ----------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE----LEELAEEL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2171 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDN 2250
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2251 TQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELA-- 2328
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAal 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2329 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHR 2408
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2409 TELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEK 2488
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2489 DS-LLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelqrleq 2567
Cdd:COG1196 709 LAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpv------ 782
|
650 660
....*....|....*....|....*..
gi 40849888 2568 qrqqqekllAEENQRLRERLQRLEEEH 2594
Cdd:COG1196 783 -----nllaIEEYEELEERYDFLSEQR 804
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1320-2251 |
8.51e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 95.04 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1320 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAELEARELQRRMQEEVTRREEAAVD 1399
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1400 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELqalraraEEAEAQKR 1479
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE-------EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1480 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETA 1559
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1560 QRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwqLKANEALRLRLQAEE 1639
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL-----------------EILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1640 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1719
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1720 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL--EAEAGRFRELAEEAARLRA 1797
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1798 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaQHK 1877
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--ELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1878 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 1957
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1958 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQ 2037
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2038 AEEKahaFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQ 2117
Cdd:pfam02463 840 LELK---EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2118 AQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2197
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2198 LQRLKAEVTEAARQRSQVEEELF------SVRVQMEELGKLKARIEAENRALILRDKDNT 2251
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLkeflelFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
35-135 |
1.47e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.79 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 35 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 110
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 40849888 111 IRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1052-1826 |
1.97e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.97 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1052 LRSELELTLGKLEQVRSLSaiylEKLKTISLVIRSTQGAEEVLKTHEEHlKEAQAVPATLQELEVTKASLKKLRAQAEAQ 1131
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKA----ERYKELKAELRELELALLVLRLEELR-EELEELQEELKEAEEELEELTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1132 qpvFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSW 1211
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1212 LQDAKSRQEQIQA--------VPIANS--QAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQ 1281
Cdd:TIGR02168 346 LEELKEELESLEAeleeleaeLEELESrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1282 LEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ 1361
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1362 RQLAEAHAQAKAQAE------------LEARE---------LQRRMQEEVTRREEAAVDAQQ---QKRSIQEELQHLRQS 1417
Cdd:TIGR02168 502 EGFSEGVKALLKNQSglsgilgvlselISVDEgyeaaieaaLGGRLQAVVVENLNAAKKAIAflkQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1418 SEAEIQAKAQQVEAAERSRMRI-------EEEIRVV------------------RLQLETTERQR--------------- 1457
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVakdlvkfDPKLRKAlsyllggvlvvddldnalELAKKLRPGYRivtldgdlvrpggvi 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1458 -GGAEDE---LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQ 1533
Cdd:TIGR02168 662 tGGSAKTnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1534 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAR 1613
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA--EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1614 EEAERELERWQlkaNEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGT 1693
Cdd:TIGR02168 820 ANLRERLESLE---RRIAATERRLEDLEEQIEELSEDIESLA-----------AEIEELEELIEELESELEALLNERASL 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1694 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA--------KVRAEMEVLLASKARAEE 1765
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerlseEYSLTLEEAEALENKIED 965
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1766 ESRSTSEKSKQ--RLEAEAGRFRELAEEAARlralaEEAKRQRQLAE--EDAARQRAEAERVLTE 1826
Cdd:TIGR02168 966 DEEEARRRLKRleNKIKELGPVNLAAIEEYE-----ELKERYDFLTAqkEDLTEAKETLEEAIEE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2164-2508 |
4.49e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 4.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2164 EQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVtEAARQRSQVEEELFsvrvqmeelgklkariEAENRAL 2243
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGE-------LERQLEPLERQA-EKAERYRELKEELK----------------ELEAELL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2244 ILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQ 2323
Cdd:COG1196 231 LLKLRE-----LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE---LLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2324 QKELAQEQARRLQEDKEQMAQQLVEETQ---GFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2400
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2401 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQAL 2480
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE-EEAELEEEEEAL 461
|
330 340
....*....|....*....|....*...
gi 40849888 2481 QKSFLSEKDSLLQRERFIEQEKAKLEQL 2508
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEA 489
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
36-133 |
5.68e-18 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 82.00 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 36 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 111
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 40849888 112 RNDDI-ADGNPKLTLGLIWTIIL 133
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1328-1942 |
6.82e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.03 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1328 ETLRRMEEEERLA-EQQRAEERERLAEVEAALEkQRQLAEAHAQ--------AKAQAELEARELQRRMQEEvtrREEAAV 1398
Cdd:PRK02224 165 EEYRERASDARLGvERVLSDQRGSLDQLKAQIE-EKEEKDLHERlngleselAELDEEIERYEEQREQARE---TRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1399 DAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQK 1478
Cdd:PRK02224 241 EVLEEHEERREELETL----EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1479 RQAQEEAERLRRQVQDESQRKRQAEaelalrvkAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEAERARQvqvalE 1557
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHN--------EEAESLREDADDLEErAEELREEAAELESELEEAREAVEDR-----R 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1558 TAQRSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQlreeaerraqqqaeaerareeaerelERWQLKANEA-LRLRLQ 1636
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGN-AEDFLEELRE--------------------------ERDELREREAeLEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1637 AEEVAQQKSLAQADAEK-----QKEEAEREARRRGKAEEqavrQRELAEQELEKQRqLAEGTAQQRLAAEQELIRLRAET 1711
Cdd:PRK02224 437 TARERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRE----RVEELEAELEDLE-EEVEEVEERLERAEDLVEAEDRI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1712 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEE 1791
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1792 AARLRALAEeakrqrQLAEEDAARQRAEAERvltEKLAAISEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRRRLEE 1871
Cdd:PRK02224 588 IESLERIRT------LLAAIADAEDEIERLR---EKREALAE---LNDERRERLAEK---RERKRELEAE--FDEARIEE 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1872 ------QAAQHKADIEERLAQLRkASESELERQKGLVE------DTLRQRR-QVEEEIMALKASFEKAaagkAELELELG 1938
Cdd:PRK02224 651 aredkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELESMYG 725
|
....
gi 40849888 1939 RIRS 1942
Cdd:PRK02224 726 DLRA 729
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
150-249 |
8.82e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 81.82 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 229
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 40849888 230 ED-VDVPQPDEKSIITYVSSL 249
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1715-2604 |
1.82e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.80 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1715 EQQRQLLEEELARLQH-----EATAAT-QKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRF-RE 1787
Cdd:pfam02463 152 PERRLEIEEEAAGSRLkrkkkEALKKLiEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYlDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1788 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRR 1867
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1868 RLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRirsNAEDT 1947
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL---ESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1948 MRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLREraEQESARQLQL 2027
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE--KQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2028 AQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLK 2107
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2108 QSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQL 2184
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqlDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2185 EETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEelgklkarieaenralilrDKDNTQRFLEEEAEKMKQ 2264
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKAS-------------------LSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2265 VAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKELAQEQARRLQEDKEQMA 2343
Cdd:pfam02463 686 ESELAkEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQD--KINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2344 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAE--EDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2421
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEElkEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2422 TLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKS----EEMQTVQQEQILQETQALQKSFLSEKDSllQRERF 2497
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLkdelESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2498 IEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelqrleqqrqqQEKLLA 2577
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE--------------EFEEKE 987
|
890 900
....*....|....*....|....*..
gi 40849888 2578 EENQRLRERLQRLEEEHRAALAHSEEI 2604
Cdd:pfam02463 988 ERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
154-251 |
5.59e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.54 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 154 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 232
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 40849888 233 DVPQPDEKSIITYVSSLYD 251
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1778-2633 |
1.49e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLTEKLAAISEATRlKTEAE 1842
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1843 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMAL 1919
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1920 KASFEKAAAGKAELELELGRIRSnaedtmRSKELAEQEAARQRQLAAEEEQRRreaeervqrSLAAEEEAARqrkvalEE 1999
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELES------KLDELAEELAELEEKLEELKEELE---------SLEAELEELE------AE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2000 VERLKAKVEEARRLRERAEQESArQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRA 2078
Cdd:TIGR02168 367 LEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2079 AEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADaemek 2158
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG----- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2159 hkkfAEQTLRQKAQVEQElttLRLQLEETdhqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEA 2238
Cdd:TIGR02168 521 ----ILGVLSELISVDEG---YEAAIEAA------LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2239 ENRALILRDKDNTQRF---LEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED------------------LAQQRAL 2296
Cdd:TIGR02168 588 GNDREILKNIEGFLGVakdLVKFDPKLRKALSYLlGGVLVVDDLDNALELAKKLRpgyrivtldgdlvrpggvITGGSAK 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2297 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKL 2376
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2377 RMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2456
Cdd:TIGR02168 748 RIAQLSKELTELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2457 LLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQE 2536
Cdd:TIGR02168 821 NLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2537 LVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEhraALAHSEEIATSQAAA---TK 2613
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEArrrLK 975
|
890 900
....*....|....*....|
gi 40849888 2614 ALPNGRDALDGPSMEAEPEY 2633
Cdd:TIGR02168 976 RLENKIKELGPVNLAAIEEY 995
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1810-2620 |
2.53e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.95 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1810 EEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhkadiEERLAQLRK 1889
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-----ALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1890 ASESELERQKGLVEDTLRQRRQVEEEimalkasfEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEE 1969
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQ--------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1970 QRRREAEERVQRSLAAEeeaaRQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafVVQQ 2049
Cdd:pfam02463 290 LLAKEEEELKSELLKLE----RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE----EEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2050 REEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQveEAERLKQSAEEQAQAQAQAQAAAEKLRK 2129
Cdd:pfam02463 362 EKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL--ELARQLEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2130 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELqrlkaEVTEAA 2209
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG-----LKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2210 RQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAE------EAARLSVAAQEAARLR 2283
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarKLRLLIPKLKLPLKSI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2284 QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2363
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2364 QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAE 2443
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2444 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQ 2523
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2524 QRQQQQMEQEKQELVASMEEARRRQRE---AEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAH 2600
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEeitKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
810 820
....*....|....*....|
gi 40849888 2601 SEEIATSQAAATKALPNGRD 2620
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYE 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2147-2615 |
3.01e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2226
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkmLKEKMQ 2306
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEE---LEELEEALAELEEEEEEEEEALEEAAEEEAELEEE--EEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2307 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMS-------AEAERLKLRMA 2379
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligvEAAYEAALEAA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2380 EMSRAQARAEEDAQRFRKQAEEigEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2459
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2460 LKSEEMQTVQQEQ---ILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQlfqdEVAKAKQLQEEQQRQQQQMEQEKQE 2536
Cdd:COG1196 622 LLGRTLVAARLEAalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA----ALLEAEAELEELAERLAEEELELEE 697
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 2537 LVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKAL 2615
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
152-250 |
7.00e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 76.57 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 40849888 232 -VDVPQPDEKSIITYVSSLY 250
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
910-1587 |
7.35e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 7.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 910 EQRQALRNLELHYQA----FLRDSQDAGgfgPEDRLVAEREYGSCSRHYQQLLQSLEQGEQE----ESRCQRCISELKDI 981
Cdd:TIGR02168 217 ELKAELRELELALLVlrleELREELEEL---QEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 982 RLQLEACETRTVH---RLRlPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELEL 1058
Cdd:TIGR02168 294 ANEISRLEQQKQIlreRLA-NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1059 TLGKL-EQVRSLSAIYLEKLKTISLvIRSTQgaeEVLKTHEEHLKEAQAVpatlQELEVTKASLKKLRAQAEAQQPVFNT 1137
Cdd:TIGR02168 373 RLEELeEQLETLRSKVAQLELQIAS-LNNEI---ERLEARLERLEDRRER----LQQEIEELLKKLEEAELKELQAELEE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1138 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQL---LERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQD 1214
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1215 AKSR---------------QEQIQAVPIANSQAAR---EQLRQEK----ALLEEIERHGEKVEECQKFAKQYINAIKDYE 1272
Cdd:TIGR02168 525 LSELisvdegyeaaieaalGGRLQAVVVENLNAAKkaiAFLKQNElgrvTFLPLDSIKGTEIQGNDREILKNIEGFLGVA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1273 LQLITYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTRYS--------ELTTL-TSQYIKFISE 1328
Cdd:TIGR02168 605 KDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRRREIEELEE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1329 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQ 1408
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1409 EELQHLRQSSEAEIQAKAQQVEAaersrmriEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERL 1488
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEEL--------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1489 RRQVQDESQRKRQAE---AELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRsaev 1565
Cdd:TIGR02168 837 ERRLEDLEEQIEELSediESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE---- 912
|
730 740
....*....|....*....|..
gi 40849888 1566 elqskrasfaektaqLERTLQE 1587
Cdd:TIGR02168 913 ---------------LRRELEE 919
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1402-2345 |
1.12e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1402 QQKRSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEA----- 1476
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1477 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE-KQRALQALDELKLQAEEAERRLRQAEAERA---RQV 1552
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEEQLRVKEKIGELEAEIAsleRSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1553 QVALETAQRSAE--VELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQaeaerareeaerelerwqlkanEA 1630
Cdd:TIGR02169 311 AEKERELEDAEErlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------ED 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1631 LRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRA 1709
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1710 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAGRFR 1786
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 ELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLTEKLAAiseatrlktEAEIALKEKEAENER---LRRLAEDEA 1863
Cdd:TIGR02169 529 QLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1864 FQRRRLEEQAAQHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQVEEEIMALKAS--FEKAAAGKAELELELGRIR 1941
Cdd:TIGR02169 589 DLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGAMTGGSRAPRGGIL 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1942 SNAEDTMRSKELAEQEaarqrqlaaeeeqrrreaeervqrslaaeEEAARQRKVALEEVERLKAKVEEARRLRERAEQE- 2020
Cdd:TIGR02169 668 FSRSEPAELQRLRERL-----------------------------EGLKRELSSLQSELRRIENRLDELSQELSDASRKi 718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2021 ---SARQLQLAQEAAQKRLQAEEkahafvVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSR 2097
Cdd:TIGR02169 719 geiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2098 KQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2177
Cdd:TIGR02169 793 IPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2178 TTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENraliLRDKDNTQRfLEE 2257
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK-LEA 928
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2258 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2337
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*...
gi 40849888 2338 DKEQMAQQ 2345
Cdd:TIGR02169 1008 RIEEYEKK 1015
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1157-1919 |
1.62e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.35 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1157 GERDVEVERWRE---RVTQLLERWQAVLAQTdvrqreLEQLGRqLRYYRESADPLsswlQDAKSRQEQIQAVPIANS-QA 1232
Cdd:TIGR02169 166 AEFDRKKEKALEeleEVEENIERLDLIIDEK------RQQLER-LRREREKAERY----QALLKEKREYEGYELLKEkEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1233 AREQLRQEKALLEEIERHGEKVEEcqkfakqyinAIKDYELQLITYKAQLEPVASPAKKpkvqSGSESVIQEYVDLRTRY 1312
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTE----------EISELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1313 SELTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR 1392
Cdd:TIGR02169 301 AEIASLERS-IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1393 REEAaVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAE 1472
Cdd:TIGR02169 380 FAET-RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1473 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALDELKLQAEEAE----RRLRQAEAER 1548
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVhgtvAQLGSVGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1549 ARQVQVAL------------ETAQRSAEV--ELQSKRASFA--EKTAQLERTLQEEH----------------------- 1589
Cdd:TIGR02169 538 ATAIEVAAgnrlnnvvveddAVAKEAIELlkRRKAGRATFLplNKMRDERRDLSILSedgvigfavdlvefdpkyepafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1590 ------VTVTQLREEAERRAQQQAEAER-------------AREEAERELERWQLKAnEALRLRLQAEEVAQQKSLAQAD 1650
Cdd:TIGR02169 618 yvfgdtLVVEDIEAARRLMGKYRMVTLEgelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1651 AEKQKEEAEREARRRGKAEEQAV---RQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQL 1720
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHK 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1721 LEEELARLqhEATAATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALA 1799
Cdd:TIGR02169 777 LEEALNDL--EARLSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1800 EEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1879
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 40849888 1880 IE---ERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEIMAL 1919
Cdd:TIGR02169 926 LEaleEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3453-3491 |
1.85e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 72.75 E-value: 1.85e-15
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3453 LLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3491
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
155-250 |
1.88e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.09 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 155 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 233
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 40849888 234 VPQPDEKSIITYVSSLY 250
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
953-1710 |
2.04e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 83.95 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 953 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkdpaRECAQRIAEQQK----AQAEVEGLGK 1027
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1028 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTH-----EEHL 1101
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeleEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1102 KEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQ-QRHGERDVEVERWRERVTQLLERWQAV 1180
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1181 LAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAvPIANSQAAREQLRQEKALLEEIERHGEKVEEC--- 1257
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1258 -------------QKFAKQYINAIKDYELQLITYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTL 1318
Cdd:TIGR02168 542 alggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1319 TSQYikFISETLrrmEEEERLAEQQRAEER-----ERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRR 1393
Cdd:TIGR02168 622 LGGV--LVVDDL---DNALELAKKLRPGYRivtldGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1394 EEAAVDAQQQKRSIQEELQHLR---QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRAR 1470
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1471 AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAr 1550
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE- 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1551 qvqvaletaqrSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwQLKANEA 1630
Cdd:TIGR02168 856 -----------SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE----------------ELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1631 LRLRLQAEEVAQQKSLAQADAEKQKeeaerearRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1710
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEG--------LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
152-251 |
2.12e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 40849888 232 VDV--PQPDEKSIITYVSSLYD 251
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1624-2484 |
2.34e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.96 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1624 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1699
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1700 --AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1777
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLTEKLAAISEatrlKTEAEIALKEKEAENERLRR 1857
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEE----KEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1858 LAEDEAFQRRRLEEQAAQhkadIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEImalkasfEKAAAGKAELELEL 1937
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDR----VEKELSKLQR-ELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1938 GRIRsnaedtmRSKELAEQEAARQRqlaaeeeqrrreaeervQRSLAAEEEAarqrkVALEEVERLKA------------ 2005
Cdd:TIGR02169 531 GSVG-------ERYATAIEVAAGNR-----------------LNNVVVEDDA-----VAKEAIELLKRrkagratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2006 KVEEARRLRERAEQESARQLQLAQEAAQKRLqaeEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEA 2085
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2086 REQAEREAAQSRKQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2162
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2163 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2242
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2243 L--ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAEL 2320
Cdd:TIGR02169 817 IeqKLNRLTLEKEYLEKEIQELQEQRIDL-----KEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2321 LQQQKELAQEQARRLQEDKEQMAQQlVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2400
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2401 EIgeklhrtelatqekvtlvQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2480
Cdd:TIGR02169 966 EI------------------RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....
gi 40849888 2481 QKSF 2484
Cdd:TIGR02169 1028 NENF 1031
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
152-255 |
3.18e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 74.70 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 40849888 232 VDV--PQPDEKSIITYVSSLYDAMPR 255
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4031-4069 |
3.25e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.25e-15
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 4031 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4069
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
32-131 |
3.76e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.49 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 32 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 106
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 40849888 107 KLVNIRNDDIADGNPKLTLGLIWTI 131
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1131-2009 |
4.19e-15 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 82.92 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1131 QQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1200
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1201 YRESADPLSSWLQDAKSR-QEQIQAVP--IANSQAAREQLRQEKALLE-EIERHGEKVEECQKFAKQYINAIKDYELQLI 1276
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKmQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1277 TYKAQLEPVASPAKK-PKVQSGSESVIQEyVDLRTRYSELTTLTSQYIKfisetlRRMEEEERLAEQQRAEERERLAEVE 1355
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEEKGRQELEKAK------RKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1356 AAL-EKQRQLAEAHAQ------AKAQAELEARELQRR---MQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAK 1425
Cdd:pfam01576 236 AQLaKKEEELQAALARleeetaQKNNALKKIRELEAQiseLQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1426 AQQVEAaersRMRIEEEIRVVRLQLETTERQRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1505
Cdd:pfam01576 316 AAQQEL----RSKREQEVTELKKALEEETRSH---EAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1506 LALRVK----AEAEAAREKQRALQALDELKLQAEEAErRLRQAEAERARQVQVALETAQRSAEvELQSKRASFAEKTAQL 1581
Cdd:pfam01576 389 LQAELRtlqqAKQDSEHKRKKLEGQLQELQARLSESE-RQRAELAEKLSKLQSELESVSSLLN-EAEGKNIKLSKDVSSL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1582 ERTLQE----------EHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL-RLRLQAEEVA-------QQ 1643
Cdd:pfam01576 467 ESQLQDtqellqeetrQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLsDMKKKLEEDAgtlealeEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1644 KSLAQADAEKQKEEAEREARRRGKAEEQAVR-QRELAEQ--ELEKQRQLAEGTAQQ-----RLAAEQELIRLRAETEQGE 1715
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAAYDKLEKTKNRlQQELDDLlvDLDHQRQLVSNLEKKqkkfdQMLAEEKAISARYAEERDR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1716 QQRQLLEEE--LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEAGRFRELAEEA- 1792
Cdd:pfam01576 627 AEAEAREKEtrALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRALEQQVEEMKTQLEELe 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1793 --------ARLR------ALAEEAKRQRQLAEEDA-------ARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1851
Cdd:pfam01576 706 delqatedAKLRlevnmqALKAQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1852 NERLRRLAEDEAFQRRRLEEQAAQHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEIM 1917
Cdd:pfam01576 786 IDAANKGREEAVKQLKKLQAQMKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERD 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1918 ALKASFEKAAAGKAELELELGRIrsnaEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL 1997
Cdd:pfam01576 865 ELADEIASGASGKSALQDEKRRL----EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR 940
|
970
....*....|....*.
gi 40849888 1998 EEVER----LKAKVEE 2009
Cdd:pfam01576 941 QQLERqnkeLKAKLQE 956
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2794-2832 |
4.23e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.23e-15
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 2794 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEMNRVL 2832
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2321-2615 |
5.33e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.68 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2321 LQQQKELAqEQARRLQEDKEQM-AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2399
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2400 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2479
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2480 LQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQ 2559
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 2560 EELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKAL 2615
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1303-1812 |
5.44e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.12 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERL---AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEL-- 1377
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1378 EARELQRRMQEEVTRREEAavdaQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1457
Cdd:COG4717 133 ELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1458 GGAEDELQALRARAEEAEAQKRQAQEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAE 1535
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1536 EAERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaekTAQLERTLQEEHVtvtqlreeaeRRAQQQAEAERAREE 1615
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELE-------------EEELEELLAALGL----------PPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1616 AERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEkqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtAQ 1695
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVE---------------DEEELRAALEQAEEYQELKEELEE--LE 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1696 QRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSK 1775
Cdd:COG4717 409 EQLEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELL 475
|
490 500 510
....*....|....*....|....*....|....*..
gi 40849888 1776 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1812
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1090-1588 |
7.00e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 7.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1090 AEEVLKTHEEhlkeaqavpaTLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1169
Cdd:PRK02224 239 ADEVLEEHEE----------RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1170 VTQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLSSWLQDAKSRQEQIQavpiANSQAAREQLRQEKA 1242
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1243 LLEEIERHGEKVEECQKFAkqyinaikdyelqlitykaqlepvasPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqy 1322
Cdd:PRK02224 385 EIEELEEEIEELRERFGDA--------------------------PVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1323 ikfISETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEAR- 1380
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEDLVEAEDRi 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1381 ----ELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvRLQLETTERQ 1456
Cdd:PRK02224 512 erleERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1457 RGGAEDELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALDEL- 1530
Cdd:PRK02224 590 SLERIRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYLEQVe 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1531 -KLQAEEAERRLRQAEAERARQVQVALEtaqrsaevELQSKRASFAEKTAQLErTLQEE 1588
Cdd:PRK02224 667 eKLDELREERDDLQAEIGAVENELEELE--------ELRERREALENRVEALE-ALYDE 716
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
29-134 |
1.26e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 72.70 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 98
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 40849888 99 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 134
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3712-3750 |
1.27e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.27e-14
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3712 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3750
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1377-1890 |
1.98e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.73 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1377 LEARELQ---RRMQEEVT---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQL 1450
Cdd:COG4913 218 LEEPDTFeaaDALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1451 ETTERQRggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALDE 1529
Cdd:COG4913 293 LEAELEE--LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1530 LKLQAEEAERRLrQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvtvtqlreeaerraqqqaea 1609
Cdd:COG4913 371 LGLPLPASAEEF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL------------------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1610 erareeaERELERwqLKAN--------EALRLRLQAE---------------EVAQ-----------------------Q 1643
Cdd:COG4913 425 -------EAEIAS--LERRksniparlLALRDALAEAlgldeaelpfvgeliEVRPeeerwrgaiervlggfaltllvpP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1644 KSLAQA----DAEKQKEEAEREARRRGKAEEQAVR--QRELAEqELEKQRQLAEGTAQQRLAA---------EQELIRL- 1707
Cdd:COG4913 496 EHYAAAlrwvNRLHLRGRLVYERVRTGLPDPERPRldPDSLAG-KLDFKPHPFRAWLEAELGRrfdyvcvdsPEELRRHp 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1708 RAETEQG---------------------------EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1760
Cdd:COG4913 575 RAITRAGqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1761 ARAEEESRSTS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLTEKLA 1829
Cdd:COG4913 655 EYSWDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1830 AISEATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1890
Cdd:COG4913 735 RLEAAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
607-785 |
2.48e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 75.17 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 607 LHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQ 686
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 687 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDrsiTVTRLEDLLQDAQDEKEQLNEY 766
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 40849888 767 KGHLSGLAKRAKAIVQLKP 785
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
35-135 |
2.55e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.95 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 35 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 106
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 40849888 107 KLVNIRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
152-253 |
5.70e-14 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 71.27 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 40849888 232 -VDVPQPDEKSIITYVSSLYDAM 253
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
150-247 |
7.45e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 225
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 40849888 226 LLDPEDVDVPQPDEKSIITYVS 247
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
150-250 |
7.80e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 70.87 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 229
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 40849888 230 ED-VDVPQPDEKSIITYVSSLY 250
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1121-1570 |
1.29e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.50 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1121 LKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWR--ERVTQLLERWQAVLAQTDVRQRELEQLGRQL 1198
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1199 RYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQekaLLEEIERHGEKVEECQKFAKQYINAIKDYELQLITY 1278
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1279 KAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEE 1347
Cdd:COG4717 233 ENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1348 RERL--AEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKrsIQEELQHLRQSSEAEIQAK 1425
Cdd:COG4717 313 LEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1426 AQQVEAAErsrmRIEEEIRVVRLQLettERQRGGAEDELQALraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1505
Cdd:COG4717 391 LEQAEEYQ----ELKEELEELEEQL---EELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1506 LalrvkAEAEAAREKQRALQALDELKLQAEEAERRLRqaeaeRARQVQVALETAQRSAEVELQSK 1570
Cdd:COG4717 462 L-----EQLEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREERLPP 516
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3046-3084 |
1.71e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 1.71e-13
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3046 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEMHEKL 3084
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
955-1864 |
1.83e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.80 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 955 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKDPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1032
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1033 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLKTHEEHLKE 1103
Cdd:TIGR02169 250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1104 AQAVPATLQ-ELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1182
Cdd:TIGR02169 320 AEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1183 qtdvRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAvpiansqaareqlrqekalleEIERHGEKVEECQKFAK 1262
Cdd:TIGR02169 390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1263 QYINAIKDYELQLITYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ 1342
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1343 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEArelQRRMQEEVTRREEAAVDAQQQKRS-------------IQE 1409
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAA---GNRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ELQHLRQSSEAEIQAKA-------QQVEAAER-------------SRMRIEEEIRVVRLQLETTERQ---RGGAEDEL-Q 1465
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAvdlvefdPKYEPAFKyvfgdtlvvedieAARRLMGKYRMVTLEGELFEKSgamTGGSRAPRgG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1466 ALRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDElklqaeeaerrlrqa 1544
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--------------- 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1545 EAERARQVQVALETAQRSAEVELQSKRASFAE---KTAQLERTLQEEHVTVTQLREEAERraqqqaeaerareeaerelE 1621
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKEleaRIEELEEDLHKLEEALNDLEARLSH-------------------S 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 RWQLKANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEGTAQQRlAAE 1701
Cdd:TIGR02169 792 RIPEIQAELSKLE--EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1702 QELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE-- 1779
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEip 947
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1780 AEAGRFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLTEKLAaiseatRLKTEAEiALKEKEAENERL 1855
Cdd:TIGR02169 948 EEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEKK 1015
|
....*....
gi 40849888 1856 RRLAEDEAF 1864
Cdd:TIGR02169 1016 KREVFMEAF 1024
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1314-1733 |
2.67e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.70 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1314 ELTTLTSQYI-----------KFISETLRRMEEEERLAEQQRAEERERLAEveaalEKQRQlaeahaqakaQAELEAREL 1382
Cdd:pfam17380 248 DVTTMTPEYTvryngqtmtenEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-----ERLRQ----------EKEEKAREV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1383 QRRMQ-EEVTRREEAAVDAQqqkrsiqeelqhlrqsseAEIQakaqqveaAERSRMRIEEEIRVVRLQLEttERQRggae 1461
Cdd:pfam17380 313 ERRRKlEEAEKARQAEMDRQ------------------AAIY--------AEQERMAMERERELERIRQE--ERKR---- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1462 dELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEAEAAREKQRALQALDELKLQAEEA-ER 1539
Cdd:pfam17380 361 -ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEEERQRKIQQQKVEMEQIRAEQEEArQR 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1540 RLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaEAERAREEAERE 1619
Cdd:pfam17380 436 EVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE-------------------EERKRKKLELEK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1620 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQavrQRELAEQELEKQRQLAE--GTAQQR 1697
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE---RRREAEEERRKQQEMEErrRIQEQM 558
|
410 420 430
....*....|....*....|....*....|....*.
gi 40849888 1698 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1733
Cdd:pfam17380 559 RKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
986-1541 |
3.60e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 986 EACETRTVHRLRLPLDKDPARECAQRIAEQQKA---QAEVEGLGKGVARLSAEAEkvlalpEPSPAAPTLRSELELTLGK 1062
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeaKKKAEEAKKKADAAKKKAE------EAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1063 LEQVRslsaiylEKLKTISLVIRSTQGAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKlRAQAEAQQPVFNTLRDEL 1142
Cdd:PTZ00121 1359 AEAAE-------EKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEK 1430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1143 RGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQlgrqlryyRESADPLSSWLQDAKSRQEQI 1222
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE--------AKKADEAKKKAEEAKKKADEA 1502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1223 QAVPIANSQAAREQLRQEKALLEEIERHGE--KVEECQKFAKQYinaiKDYELQLITYKAQLEPVASPAKKPKVQSGSES 1300
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEakKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1301 VIQEYVDLR----TRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaalEKQRQLAEAHAQAKAQAE 1376
Cdd:PTZ00121 1579 ALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK--------KKVEQLKKKEAEEKKKAE 1650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1377 learELQRRMQEEVTRREEAAVDAQQQKRSIQEelqhLRQSSEAEIQAKAQQVEAAERSRMriEEEIRvvrlqlETTERQ 1456
Cdd:PTZ00121 1651 ----ELKKAEEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAEEAKK--AEELK------KKEAEE 1714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1457 RGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQRALQALDELKLQAEE 1536
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK-----KEEEKKAEEIRKEKEAVIEEELDEED 1789
|
....*
gi 40849888 1537 AERRL 1541
Cdd:PTZ00121 1790 EKRRM 1794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1857-2677 |
3.73e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1857 RLAEDEAFQRRRLEEQAA---QHKADIEERLAQLRKASESeLERqkglVEDTLRqrrqveeeimalkasfekaaagkaEL 1933
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREN-LDR----LEDILN------------------------EL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1934 ELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAA----EEEAARQRKVALEEVERLKAKVEE 2009
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEaeeeLEELTAELQELEEKLEELRLEVSE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2010 arrLRERAEQESARQLQLAQEaaQKRLQAEEKAHafvvQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQA 2089
Cdd:TIGR02168 279 ---LEEEIEELQKELYALANE--ISRLEQQKQIL----RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2090 EREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKkfAEQTLRQ 2169
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ--QEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2170 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALilRDKD 2249
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENL--EGFS 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2250 NTQRFLEEEAEKMKQV---------AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQ--------AVQEAT 2312
Cdd:TIGR02168 506 EGVKALLKNQSGLSGIlgvlselisVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGrvtflpldSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2313 RLKAEAELLQQQKELAQEQARRLQEDKE------------------QMAQQLVEETQGFQR--TLEAE------------ 2360
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddlDNALELAKKLRPGYRivTLDGDlvrpggvitggs 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2361 ---RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERL 2437
Cdd:TIGR02168 666 aktNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2438 REAIAELEREKEKLKQEAKLLQLK-----------SEEMQTVQQ--EQILQETQALQKSFLSEKDSLLQRERFIEQEKAK 2504
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERleeaeeelaeaEAEIEELEAqiEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2505 LEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQ---EELQRLEQQRQQQEKLLAEENQ 2581
Cdd:TIGR02168 826 LESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEELR 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2582 RLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDAL---------DGPSMEAEPEYTFEGLRQKVPA--QQLQEA 2650
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltleEAEALENKIEDDEEEARRRLKRleNKIKEL 984
|
890 900 910
....*....|....*....|....*....|
gi 40849888 2651 G---ILSMEELQRLTQGHTTVAEltQREDV 2677
Cdd:TIGR02168 985 GpvnLAAIEEYEELKERYDFLTA--QKEDL 1012
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
20-138 |
4.62e-13 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 68.42 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 20 YEEVREKykderdrvqkKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQ 92
Cdd:cd21298 2 IEETREE----------KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIE 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 40849888 93 NVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21298 70 NCNYAVELGKKLKFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1098-1821 |
4.82e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 76.53 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1098 EEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVfntlrdeLRGAQEVGERLQQRHGERDVEVERWRervTQLLERW 1177
Cdd:COG3096 333 SDHLNLVQTALRQQEKIERYQEDLEELTERLEEQEEV-------VEEAAEQLAEAEARLEAAEEEVDSLK---SQLADYQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1178 QAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIAN------SQAAREQLRQEK 1241
Cdd:COG3096 403 QAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELeqklsvADAARRQFEKAY 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1242 ALLEEIERHGEKVEECQKfAKQYINAIKDYELQLitykAQLEPVAspakkpkvqsgsesviQEYVDLRTRYS---ELTTL 1318
Cdd:COG3096 479 ELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRLRqqqNAERL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1319 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ-AELEARELQ-RRMQEEVTRREEA 1396
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARiKELAARAPAwLAAQDALERLREQ 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1397 AVDAQQQKRSIQEELQHLrqsSEAEIQAKAQQVEAAERsRMRIEEEIRvvRLQletterQRGGAED-ELQALRAR----- 1470
Cdd:COG3096 618 SGEALADSQEVTAAMQQL---LEREREATVERDELAAR-KQALESQIE--RLS------QPGGAEDpRLLALAERlggvl 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1471 ------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQRKRQaEAELALRVKAE- 1513
Cdd:COG3096 686 lseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVVKLSd 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1514 --------------AEAAREKQralqaLDELKLQAEE-----AERRLRQAEAER---------ARQVQVALETaqrSAEV 1565
Cdd:COG3096 765 rqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVAFAP---DPEA 836
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1566 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRA-------QQQAEAERAREEAERELERWQLKANEALR-LRLQA 1637
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQEAQAfIQQHG 916
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1638 EEVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLAAEQELI-RLRAETEQG 1714
Cdd:COG3096 917 KALAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQA 996
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1715 EQQRQLLEEELARLQHEATAATQKRQELEA-------ELAKVRAEMEVL-LASKARAEEESRSTSEKSKQRLEAEAGRFR 1786
Cdd:COG3096 997 EEARREAREQLRQAQAQYSQYNQVLASLKSsrdakqqTLQELEQELEELgVQADAEAEERARIRRDELHEELSQNRSRRS 1076
|
810 820 830
....*....|....*....|....*....|....*
gi 40849888 1787 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1821
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
53-132 |
5.60e-13 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 68.00 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 53 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 124
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 40849888 125 LGLIWTII 132
Cdd:cd21223 105 LALLWRII 112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1402-2043 |
5.95e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.78 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1402 QQKRSIQEELQHLRQSSEAEIQAKAQQVEAaersrmRIEEEIRVVRLQLET--TERQRGGAEDELQALRARAEEAEAQKR 1479
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSL------HGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1480 QAQEEAERLRRQvqDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA-ERARQVQVALET 1558
Cdd:TIGR00618 237 QTQQSHAYLTQK--REAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1559 AQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1638
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1639 EVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-EGTAQQRLAAEQELIRLR---AETEQG 1714
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAqslKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1715 EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskarAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1794
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN--------PARQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1795 LRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA- 1873
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQd 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1874 ----AQHKADIEERLAQLRKASES-ELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTM 1948
Cdd:TIGR00618 627 lqdvRLHLQQCSQELALKLTALHAlQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1949 RSKELAEQEAARQRQlaaeeeqRRREAEERVQRSLAAEEEAARQRKVALEEVER--LKAKVEEARRLRERA---EQESAR 2023
Cdd:TIGR00618 707 RELETHIEEYDREFN-------EIENASSSLGSDLAAREDALNQSLKELMHQARtvLKARTEAHFNNNEEVtaaLQTGAE 779
|
650 660
....*....|....*....|
gi 40849888 2024 QLQLAQEAAQKRLQAEEKAH 2043
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTH 799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1137-1964 |
6.86e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 75.76 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1137 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQRelEQLGRqlryYRESADPLSSW 1211
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQ--EKIER----YQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1212 LqdaksrQEQIQAVPIANSQAAREQLRQEKAlLEEIER-------HGEKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1283
Cdd:PRK04863 364 L------EEQNEVVEEADEQQEENEARAEAA-EEEVDElksqladYQQALDVQQTRAIQYQQAVQALErAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1284 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaALEKQRQ 1363
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR------RLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1364 LAEAHAQAKAQ-AELEARELQRRMQEevtRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1442
Cdd:PRK04863 511 LAEQLQQLRMRlSELEQRLRQQQRAE---RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1443 IrvvrlqletterqrggaeDELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--------SQRKRQAEAELALRVkAEA 1514
Cdd:PRK04863 588 L------------------EQLQARIQRLAARAPAWLAAQDALARLREQSGEEfedsqdvtEYMQQLLERERELTV-ERD 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1515 EAAREKQRALQALDELkLQAEEAERRLRQAEAERARQV-------QVALETA---------QRSAEVELQSKRAsfAEKT 1578
Cdd:PRK04863 649 ELAARKQALDEEIERL-SQPGGSEDPRLNALAERFGGVllseiydDVSLEDApyfsalygpARHAIVVPDLSDA--AEQL 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1579 AQLERTLQEEHVT---VTQLREEAERRAQQQAEAERAREEAERELERWQL------KANEAL--RLRLQAEEVAQQksLA 1647
Cdd:PRK04863 726 AGLEDCPEDLYLIegdPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgrAAREKRieQLRAEREELAER--YA 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1648 QADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1727
Cdd:PRK04863 804 TLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLN-------RRRVELERALADHESQEQQQRSQLEQAKEGLSA 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1728 L-QHEATAATQKRQELEAELAKVRAEMEvllaskaRAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEAKR 1804
Cdd:PRK04863 877 LnRLLPRLNLLADETLADRVEEIREQLD-------EAEEAKRFVQQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQAQQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1805 QRQlaeedAARQRAEAervLTEklaAISEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAfQRRRLEEQAAQHKADIEE 1882
Cdd:PRK04863 950 TQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAQLAQ 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1883 -------------RLAQLRKASESELE----RQKGLVEDTLRQRRqvEEEIMALKASFEKaaagKAELELELGRIRSNAE 1945
Cdd:PRK04863 1018 ynqvlaslkssydAKRQMLQELKQELQdlgvPADSGAEERARARR--DELHARLSANRSR----RNQLEKQLTFCEAEMD 1091
|
890
....*....|....*....
gi 40849888 1946 DTMRSKELAEQEAARQRQL 1964
Cdd:PRK04863 1092 NLTKKLRKLERDYHEMREQ 1110
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
150-250 |
7.09e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 67.75 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 229
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 40849888 230 ED-VDVPQPDEKSIITYVSSLY 250
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4300-4338 |
1.52e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.52e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 4300 LLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRI 4338
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
152-251 |
1.85e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 66.21 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 227
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 40849888 228 DPEDVdVPQPDEKSIITYVSSLYD 251
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
977-1577 |
2.19e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 977 ELKDIRLQLEAcETRTVHRLRlpldkdPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1056
Cdd:COG4913 236 DLERAHEALED-AREQIELLE------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1057 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvlktheEHLKEAqavpatLQELEVTKASLKKLRAQAEAQqpvFN 1136
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLERE------IERLERELEERERRRARLEAL---LA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1137 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLSSWLQDAk 1216
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLAL- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1217 sRQEQIQAVPIANS---------QAAREQLRQEKAlleeIER--HGEKV-----EECQKFAKQYINAIKDyELQLITYKA 1280
Cdd:COG4913 446 -RDALAEALGLDEAelpfvgeliEVRPEEERWRGA----IERvlGGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1281 QLEPVASPAKKPKVQSGSEsviqeyvdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-E 1353
Cdd:COG4913 520 RTGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1354 VEAALEK--QRQLAEAH------AQAKAQAELEARELQRRMQEEVTRREEAAvDAQQQKRSIQEELQHLRQSSEAEIqak 1425
Cdd:COG4913 586 NGTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI--- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1426 aqQVEAAERSRMRIEEEIRvvrlQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE 1505
Cdd:COG4913 662 --DVASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1506 LAlRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEK 1577
Cdd:COG4913 729 LD-ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3122-3160 |
3.52e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.52e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3122 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAL 3160
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
152-247 |
3.78e-12 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 65.49 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 230
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 40849888 231 DVDVPQPDEKSIITYVS 247
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3377-3415 |
3.81e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 3.81e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3377 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3415
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1667-1883 |
6.03e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.95 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1746
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1747 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1822
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1823 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1883
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2718-2756 |
6.97e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 6.97e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 2718 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2756
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
152-252 |
7.52e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 64.68 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 152 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 231
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 40849888 232 VdVPQPDEKSIITYVSSLYDA 252
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3955-3993 |
8.99e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 8.99e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3955 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3993
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3788-3826 |
9.26e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.26e-12
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3788 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3826
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1162-1871 |
1.12e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.79 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1162 EVERWRERVtQLLERWQAVLAQTDVRQRELEQLgrqlryyrESAD----PLSSWLQDAKSRQEQIQAVPIANSQAAREQL 1237
Cdd:pfam12128 222 QVEHWIRDI-QAIAGIMKIRPEFTKLQQEFNTL--------ESAElrlsHLHFGYKSDETLIASRQEERQETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1238 RQEKALLEEI--ERHGEKVEECQKFAK--QYINAIKDYELQ-----LITYKAQLEpvaspaKKPKVQSGSESVIQEYVDL 1308
Cdd:pfam12128 293 RTLDDQWKEKrdELNGELSAADAAVAKdrSELEALEDQHGAfldadIETAAADQE------QLPSWQSELENLEERLKAL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1309 RTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERlAEVEAALEKQ-RQLAEAHAQAKAQAELEARELQRR 1385
Cdd:pfam12128 367 TGKHQDVTAKYNRRRSKIKEQNNRDIAgiKDKLAKIREARDRQL-AVAEDDLQALeSELREQLEAGKLEFNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1386 MQEEVTRREEAAVDaqqqkrsiQEELQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQ 1465
Cdd:pfam12128 446 LGELKLRLNQATAT--------PELLLQLENFDE-RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1466 ALRARAEEAEAQ-KRQAQEEAERLRRQVQDESQR-KRQAEAELALRVKAEAEAAREKQRALQALDELKLQ---------- 1533
Cdd:pfam12128 517 ERQSALDELELQlFPQAGTLLHFLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDlkridvpewa 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1534 --AEEAERRLRQAE----AERARQVQVALETAQRSAEVELQSKRASFAektaqlERTLQEEHVTVTQLREEAERRAQQQA 1607
Cdd:pfam12128 597 asEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKASREETFA------RTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1608 EAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA--------EREARRRGKAEEQAVRQRELA 1679
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQvvegaldaQLALLKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1680 EQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEataATQKRQELEAELAKVRAEMEVLL 1757
Cdd:pfam12128 751 ALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQET---WLQRRPRLATQLSNIERAISELQ 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1758 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAERVLTEKLAAISEaTRL 1837
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQGSIGERLAQLED-LKL 900
|
730 740 750
....*....|....*....|....*....|....*....
gi 40849888 1838 KTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 1871
Cdd:pfam12128 901 KRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1415-2041 |
1.49e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.41 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1415 RQSSEAEIQAKAQQVEA--AERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE----RL 1488
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1489 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1568
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1569 SKRASFAEKTAQLERTLQEEHVT-VTQLREEAERRAQQQAEAERAREEAERELE---RWQLKAN------EALRLRLQAE 1638
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALEselREQLEAGklefneEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1639 EVAQQKSLAQADAEK--QKEEAEREARRRGKAEEQAVRQRELAEQELekqrqlaegtAQQRLAAEQELIRLRAETEQGEQ 1716
Cdd:pfam12128 448 ELKLRLNQATATPELllQLENFDERIERAREEQEAANAEVERLQSEL----------RQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1717 QRQLLEEelARLQHEATAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAE 1790
Cdd:pfam12128 518 RQSALDE--LELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1791 EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE 1870
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1871 EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEE--------IMALKASFEKAAAGKAELELELGRiRS 1942
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqaywqvvEGALDAQLALLKAAIAARRSGAKA-EL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1943 NAEDTMRSKELAEQEAARQR--QLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQE 2020
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDViaKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQ 829
|
650 660
....*....|....*....|.
gi 40849888 2021 SARQlqlaQEAAQKRLQAEEK 2041
Cdd:pfam12128 830 LARL----IADTKLRRAKLEM 846
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1443-1825 |
1.58e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.92 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1443 IRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKrqaqeEAERlRRQVQdESQRKRQAEAELALRVKAEAE-AAREKQ 1521
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-----EVER-RRKLE-EAEKARQAEMDRQAAIYAEQErMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1522 RALQaldelKLQAEEAERrlrqaEAERARQVQVALETaQRSAEVElqskrasfaekTAQLERTLQEEHVtvtqlreeaer 1601
Cdd:pfam17380 348 RELE-----RIRQEERKR-----ELERIRQEEIAMEI-SRMRELE-----------RLQMERQQKNERV----------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1602 rAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEvAQQKSLAQADAEKQKeeaerearrrgkaEEQAVRQRELA-E 1680
Cdd:pfam17380 395 -RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE-ARQREVRRLEEERAR-------------EMERVRLEEQErQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1681 QELEKQRQLAEGTAQQRLAAEQE-LIRLRAEteqgEQQRQLLEEELARLQHEATAATQKRQELEAELAKvRAEMEVLLAS 1759
Cdd:pfam17380 460 QQVERLRQQEEERKRKKLELEKEkRDRKRAE----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEE-RQKAIYEEER 534
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1760 KARAEEESRSTSEKSKQRLEAEagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLT 1825
Cdd:pfam17380 535 RREAEEERRKQQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPIT 598
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1708-2024 |
1.74e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.92 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1708 RAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSkqrlEAEAGRFRE 1787
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQ-AAIYAEQERMAMERERELERIRQEERKR----ELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1788 LAEEAARLRALaEEAKRQRQLAEEdAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEA-- 1863
Cdd:pfam17380 370 IAMEISRMREL-ERLQMERQQKNE-RVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAre 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1864 FQRRRLEEQAAQHKAdieERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEimaLKASFEKAAAGKAELELELGRIRSN 1943
Cdd:pfam17380 448 MERVRLEEQERQQQV---ERLRQ----QEEERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1944 AEDTMRSKELAEQEAARQRQlaaeeeqrrREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR 2023
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE---------AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
|
.
gi 40849888 2024 Q 2024
Cdd:pfam17380 589 A 589
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1343-1873 |
2.17e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 70.66 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1343 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR----ELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSS 1418
Cdd:COG3899 713 RRALARGAYAEALRYLERALELLPPDPEEEYRLALLLElaeaLYLAGRFEEAEALLERALAARALAALAALRHGNPPASA 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1419 EAEIQAKAQQVEAAERSRMRIEEEIRVV-RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERL--RRQVQDE 1495
Cdd:COG3899 793 RAYANLGLLLLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLA 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1496 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFA 1575
Cdd:COG3899 873 LAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAA 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1576 EKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQK 1655
Cdd:COG3899 953 ALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAA 1032
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1656 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1735
Cdd:COG3899 1033 AAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALA 1112
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1736 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR 1815
Cdd:COG3899 1113 ALALAAALAALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAA 1186
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1816 QRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1873
Cdd:COG3899 1187 AAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1642-1851 |
3.71e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.68 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1642 QQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAegtaQQRLAAeQELIRLRAETEQGEQQRQLL 1721
Cdd:PRK09510 68 QQQQKSAKRAEEQRKK---------KEQQQAEELQQKQAAEQERLKQLE----KERLAA-QEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1722 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1801
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1802 AKRQRQLAEEDAARQ-RAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1851
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1332-2455 |
4.06e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.82 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1332 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHA----QAKAQAEL--EARELQRRMQ------EEVTRREE 1395
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalqeQLQAETELcaEAEEMRARLAarkqelEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1396 AAVDaQQQKRSIQeeLQHLRQSSEAEIQAKAQQVEAAERSRMrieeeirvvRLQLE--TTERQRGGAEDELQALRARAEE 1473
Cdd:pfam01576 82 SRLE-EEEERSQQ--LQNEKKKMQQHIQDLEEQLDEEEAARQ---------KLQLEkvTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1474 AEAQKRQAQEEAERLRRQVQDESQRKRQaeaelalrvkaeAEAAREKQRALQALDELKLQAEEAERRlrqaEAERARQVQ 1553
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKS------------LSKLKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1554 VALETAQRSAEVELQSKRASFAEKTAQLERTLQeehvtvtqlreeaerraqqqaeaerareEAERELERWQLKANEALRl 1633
Cdd:pfam01576 214 EGESTDLQEQIAELQAQIAELRAQLAKKEEELQ----------------------------AALARLEEETAQKNNALK- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1634 rlQAEEVAQQKSLAQADAEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTaQQRLAAEQELiRLRAETEQ 1713
Cdd:pfam01576 265 --KIRELEAQISELQEDLESERA-----------ARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQEL-RSKREQEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1714 GEQQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfR 1786
Cdd:pfam01576 330 TELKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlQQAKQDSEHKR-K 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-------------LTEKLAAIS-----------EATRLKTEAE 1842
Cdd:pfam01576 409 KLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegknikLSKDVSSLEsqlqdtqellqEETRQKLNLS 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1843 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEIMALKAS 1922
Cdd:pfam01576 489 TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQ 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1923 FEKAAAGKAELELELGRIRSNAEDTMrskelaeQEAARQRQLAAEEEQRRREAEErvqrsLAAEEEAARQRKVALEEVER 2002
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAE 628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2003 LKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqnmLERLRSEAEAARRAAEEA 2082
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHEL 683
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2083 EEAREQAEREAAQSRKQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalKQKQAADAEMEKHKKf 2162
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR- 745
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2163 aeQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2242
Cdd:pfam01576 746 --QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDE 823
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2243 LILRDKDNTQRFLEEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2322
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQ 902
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2323 QQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQrqleMSAEAERLKLRMAEMSRAQ---------------AR 2387
Cdd:pfam01576 903 SNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ----LERQNKELKAKLQEMEGTVkskfkssiaaleakiAQ 978
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2388 AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEA 2455
Cdd:pfam01576 979 LEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1308-1908 |
6.99e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.01 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1308 LRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQ---AELEARELQR 1384
Cdd:pfam07111 53 LELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEglrAALAGAEMVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1385 RMQEEVTRREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSrmrieeeirvvrlqLETTERQRGGAEDEL 1464
Cdd:pfam07111 132 KNLEEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1465 QalraraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALDELKLQAEEAERRLRQA 1544
Cdd:pfam07111 193 A--------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1545 EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLreeaerraqqqaeaeraREEAERELERWQ 1624
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1625 LKANeALRLRLQAEEVAQQKSLAQADAEkqkeEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLAAEQ 1702
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1703 ELIRLRAETEQGEQQRQL------------------LEEELAR---LQHEATAATQKRQELEA------ELAKVRAE--- 1752
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwlettmtrVEQAVARipsLSNRLSYAVRKVHTIKGlmarkvALAQLRQEscp 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1753 ---------MEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAE-EAARLRALAEEAKRQRQLAEEDAARQRAEA 1820
Cdd:pfam07111 468 ppppappvdADLSLELEQLREERNRLDAElqLSAHLIQQEVGRAREQGEaERQQLSEVAQQLEQELQRAQESLASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1821 ERVLTEKLAAISEATRLKTE----AEI---ALKEKEAENErlRRLAEDEAFQRRRLEEQAAQH-KADIEERLAQLRKASE 1892
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQEltqqQEIygqALQEKVAEVE--TRLREQLSDTKRRLNEARREQaKAVVSLRQIQHRATQE 625
|
650
....*....|....*.
gi 40849888 1893 SELERQKGLVEDTLRQ 1908
Cdd:pfam07111 626 KERNQELRRLQDEARK 641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1681-2044 |
7.73e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1681 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EATAATQKRQELEAELAKVRAEMEVLLA 1758
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1759 S--------------KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERvL 1824
Cdd:COG4717 154 RleelreleeeleelEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ-L 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1825 TEKLAAISEATRLKTEAEIAL--------------------------------------------KEKEAENERLRRLAE 1860
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlflvlgllallflllarekASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1861 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKASFEKAAAGKAElelelgR 1939
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------E 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1940 IRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAE-EEAARQRKVALEEVERLKAKVEEAR-RLRERA 2017
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLE 466
|
410 420
....*....|....*....|....*..
gi 40849888 2018 EQESARQLQLAQEAAQKRLQAEEKAHA 2044
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWA 493
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
30-129 |
7.93e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.06 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 101
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 40849888 102 RHRQVKLVNIRNDDIADGNPKLTLGLIW 129
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1705-2511 |
9.33e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.84 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1705 IRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1782
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1783 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdE 1862
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1863 AFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglvedtlrQRRQVEEeimalkasfeKAAAGKAELELELGRIRS 1942
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1943 NAEdtMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESA 2022
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2023 RQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEE 2102
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2103 AERLKQSAEEQAQAQAQAQAAAEKlRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2182
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2183 QLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLkARIEAENRALILRDKDNTQRFLEEEAEKM 2262
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2263 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQR----ALAEKMLKEKMQAVQEATRLKAEAELLQ---QQKELAQEQ-ARR 2334
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLT-LTQERvrehALSIRVLPKELLASRQLALQKMQSEKEQltyWKEMLAQCQtLLR 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2335 LQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlKLRMAEMSRAQARAEEDAQRFrkqaeeigEKLHRTELATQ 2414
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK-ELMHQARTVLKARTEAHFNNN--------EEVTAALQTGA 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2415 EKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL--LQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLL 2492
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
810
....*....|....*....
gi 40849888 2493 QRERFIEQEKAKLEQLFQD 2511
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLSDK 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2147-2349 |
1.32e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2226
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EEL----------GKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2296
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2297 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2349
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1637-2019 |
1.46e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1637 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1716
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1717 QRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1796
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1797 ALAEEAKRQRQLAEE----DAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAF------ 1864
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierlee 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1865 QRRRLEEQAAQHKADIEE---RLAQLRKAS---ESELERQKglvEDTLRQRRQVEEEIMALKASFEKAAAGKAELElELG 1938
Cdd:PRK02224 517 RREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLE 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1939 RIRS------NAEDTM-----RSKELAEQEAARQRQLaaeeeqrrreaeervqrslaaeeEAARQRKVALEEvERLKAKV 2007
Cdd:PRK02224 593 RIRTllaaiaDAEDEIerlreKREALAELNDERRERL-----------------------AEKRERKRELEA-EFDEARI 648
|
410
....*....|..
gi 40849888 2008 EEARRLRERAEQ 2019
Cdd:PRK02224 649 EEAREDKERAEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1326-1797 |
1.49e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1326 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaelEARELqrrmqeevtrREEAAVDaqqqkr 1405
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE-----------RAEEL----------REEAAEL------ 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 siqeelqhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEaqkrqaQEEA 1485
Cdd:PRK02224 369 -------------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR------EREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1486 ErLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARqVQVALETAQRSAEV 1565
Cdd:PRK02224 430 E-LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEE-VEERLERAEDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1566 E-----LQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQaeaerareeaerelERWQLKANEAlrlRLQAEEV 1640
Cdd:PRK02224 508 EdrierLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA--------------EEKREAAAEA---EEEAEEA 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1641 AQqkslAQADAEKQKEEAEREARRRGKAEEQAVRqRELAEQEL----EKQRQLAEGTAQQR--LAAEQELIRLRAET--- 1711
Cdd:PRK02224 571 RE----EVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIerlrEKREALAELNDERRerLAEKRERKRELEAEfde 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1712 ---EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaskaRAEEESRSTSEKSKQRLEAEAGRFREL 1788
Cdd:PRK02224 646 ariEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL-----EELRERREALENRVEALEALYDEAEEL 720
|
....*....
gi 40849888 1789 AEEAARLRA 1797
Cdd:PRK02224 721 ESMYGDLRA 729
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1302-1800 |
1.54e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1302 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaelearE 1381
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1382 LQRRMQEEVTRREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrgg 1459
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1460 aedelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAELAlRVKA-------EAEAAREKQR 1522
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALE-RAKQlcglpdlTADNAEDWLE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1523 ALQA-LDELKLQAEEAERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVTVTQLreeae 1600
Cdd:PRK04863 446 EFQAkEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL----- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1601 rraqqqaeaerareeaerelerwqlkanEALRLRLQAeevAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1680
Cdd:PRK04863 516 ----------------------------QQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1681 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEATAATQKRQELEAELAKvraemevlL 1757
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------L 636
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 40849888 1758 ASKARAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1800
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1103-1595 |
1.93e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1103 EAQAVPATLQELEVTKASLKKLRAQAEAQQPV------FNTLRDELRGAQEVGERLQQRHGERdvEVERWRERVTQLLER 1176
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1177 WQAVLAQTDVRQRELEQLGRQLRYYREsadplsswlqdaksrqeqiqavpiansQAAREQLRQEKALLEEIERHGEKVEE 1256
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEA---------------------------QIRGNGGDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1257 CQKFAKQYINAIKDYELQLITYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------ 1316
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrks 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1317 TLTSQYIKF---ISETLRRMEEEER-LAE--QQRAEERE-RLAeVEAALEKQRQ--LAEAHAQAKAQAELEARELQRRMQ 1387
Cdd:COG4913 437 NIPARLLALrdaLAEALGLDEAELPfVGEliEVRPEEERwRGA-IERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1388 -EEVTRREEAAVDAQQQKRSIQEEL------------QHLRQSSEAEIQAKAQQVEAAERS------------RMRIEEE 1442
Cdd:COG4913 516 yERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleAELGRRFDYVCVDSPEELRRHPRAitragqvkgngtRHEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1443 IRVVRLQL--ETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR-VKAEAEAARE 1519
Cdd:COG4913 596 RRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1520 KQRALQA----LDELKLQAEEAERRLRQAEAERArqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQL 1595
Cdd:COG4913 676 ELERLDAssddLAALEEQLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1465-1861 |
1.93e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.67 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1465 QALRARAEEAEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-----LRVKAEAEAAREK-QRALQALDELKLQAEE 1536
Cdd:PRK04863 287 EALELRRELYTSRRQLAaeQYRLVEMARELAELNEAESDLEQDYQaasdhLNLVQTALRQQEKiERYQADLEELEERLEE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1537 A--------------ERRLRQAEAERAR------QVQVALETAQRSAEVELQSKRAsfAEKTAQLertLQEEHVTVTQLR 1596
Cdd:PRK04863 367 QnevveeadeqqeenEARAEAAEEEVDElksqlaDYQQALDVQQTRAIQYQQAVQA--LERAKQL---CGLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1597 EEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEevaQQKSLAQADAEKQKEEAEREARRRG---------- 1666
Cdd:PRK04863 442 DW---------------------LEEFQAKEQEATEELLSLE---QKLSVAQAAHSQFEQAYQLVRKIAGevsrseawdv 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 --KAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAAtqkRQELEA 1744
Cdd:PRK04863 498 arELLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR---LESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1745 ELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVL 1824
Cdd:PRK04863 573 SVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE-YMQQLLEREREL 643
|
410 420 430
....*....|....*....|....*....|....*...
gi 40849888 1825 TEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAED 1861
Cdd:PRK04863 644 TVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1642-1837 |
1.96e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1642 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1721
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1722 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1801
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 40849888 1802 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRL 1837
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1822-2558 |
2.03e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1822 RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASESELERQKGL 1901
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1902 VEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAED-TMRSKELAEQEAARQRQLAAEEEQRRREAEERVQ 1980
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1981 RSLAAEEEAARQRKVALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFVVQQRE 2051
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2052 EELQQTLQQEQNMLERLRSEaeaarraaeeaeeareqaereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEa 2131
Cdd:TIGR02169 389 DYREKLEKLKREINELKREL-------------------------DRLQEELQRLSEELADLNAAIAGIEAKINELEEE- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2132 eqeaarraqaeqaalkqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAE---VTEA 2208
Cdd:TIGR02169 443 -----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2209 ARQRSQVEEELFS----VRVQMEELGKLKAR------IEAENR--ALILRDKDNTQR---FLEEEA---------EKMKQ 2264
Cdd:TIGR02169 506 VRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2265 VAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEA 2318
Cdd:TIGR02169 586 ERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2319 ELLQQQKElaqEQARRLQEDKEQMAQQLveetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2398
Cdd:TIGR02169 666 ILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2399 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELER-----------------EKEKLKQEAKLLQLK 2461
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelsklEEEVSRIEARLREIE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2462 SEEMQTVQQEQILQ-ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVAS 2540
Cdd:TIGR02169 819 QKLNRLTLEKEYLEkEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
810
....*....|....*...
gi 40849888 2541 MEEARRRQREAEEGVRRK 2558
Cdd:TIGR02169 898 LRELERKIEELEAQIEKK 915
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4376-4414 |
2.24e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.24e-10
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 4376 FLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKL 4414
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1343-1833 |
3.43e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.90 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1343 QRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQAElEARELQRRmQEEVTRREEAAVDaqqqkrsiqeelqHLrqsseAE 1421
Cdd:COG3096 279 ERRELSERALELRRELfGARRQLAEEQYRLVEMAR-ELEELSAR-ESDLEQDYQAASD-------------HL-----NL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1422 IQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEDELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQ 1501
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1502 AEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqSKRASFAEKTAQL 1581
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1582 ERTLQEehvtvtqlreeaerraqqqaeaerareeaERELERWQlKANEALR----LRLQAEEVAQ-QKSLAQAdaekqke 1656
Cdd:COG3096 482 CKIAGE-----------------------------VERSQAWQ-TARELLRryrsQQALAQRLQQlRAQLAEL------- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1657 eaerearrrgkaeEQAVRQRELAEQELEkqrQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEATAAT 1736
Cdd:COG3096 525 -------------EQRLRQQQNAERLLE---EFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1737 QKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1806
Cdd:COG3096 585 QQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLS 664
|
490 500
....*....|....*....|....*..
gi 40849888 1807 QLAEEDAARQRAEAERVLTEKLAAISE 1833
Cdd:COG3096 665 QPGGAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
36-132 |
3.72e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.28 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 36 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 101
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 40849888 102 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 132
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
25-135 |
4.56e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 59.91 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 25 EKYKDERDRVQ--KKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIAL 98
Cdd:cd21222 5 DLFDEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLAL 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 99 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21222 85 ELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
909-1529 |
5.91e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 909 EEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLV----AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQ 984
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 985 LEacetrtvhrlrlpldkdparecaQRIAEQqkaqaeveglgkGVARLSAeaekvlalpepspaaptLRSELELTLGKLE 1064
Cdd:COG4913 328 LE-----------------------AQIRGN------------GGDRLEQ-----------------LEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1065 QVRSLSAIYLEKLKTISLVIRSTqgAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQqpvFNTLRDELrg 1144
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS--AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE---LRELEAEI-- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1145 aqevgERLQQRHGERDVEVERWRERVTQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----RY 1200
Cdd:COG4913 429 -----ASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppEH 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1201 YREsadpLSSWLQDAKSRQE-QIQAVPIANSQAAREQLrQEKALLEEIERhgeKVEECQKFAKQYINAIKDYELqlityk 1279
Cdd:COG4913 498 YAA----ALRWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC------ 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1280 aqlepVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERER 1350
Cdd:COG4913 564 -----VDSPE-----------------ELR-RHPRAITRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1351 LAEVEAALEKQRQLAEAHAQAKAQaeLEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKAQQVE 1430
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDA--LQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1431 AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELALR 1509
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEERI 775
|
650 660
....*....|....*....|
gi 40849888 1510 VKAEAEAAREKQRALQALDE 1529
Cdd:COG4913 776 DALRARLNRAEEELERAMRA 795
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1342-1963 |
5.97e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.98 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1342 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQeevtrreeAAVDAQQQKRSIQEELQHLRQSSEAE 1421
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ--------ALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1422 I-----QAKAQQVEAAERSRMRIEEEirVVRLQLETTERQ--RGGAEDELQALRA------------------RAEEA-- 1474
Cdd:PRK10246 291 QlrphwERIQEQSAALAHTRQQIEEV--NTRLQSTMALRAriRHHAAKQSAELQAqqqslntwlaehdrfrqwNNELAgw 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1475 EAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELALRVKA-EAEAAREKQRALQALDE--LKLQAEEAERRLRQAEAERA 1549
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQqlTHAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1550 RQvqvALETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVTVTQLREEAERRAQQQAEAE--RAREEAERELERWQL 1625
Cdd:PRK10246 449 IQ---NVTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEAYQALEP 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1626 KANEALRLRLQaEEVAQQKS-----LAQADAEKQKEEaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAA 1700
Cdd:PRK10246 526 GVNQSRLDALE-KEVKKLGEegaalRGQLDALTKQLQ---------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQP 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1701 EQELIRLRAETEQGEQQRQLLEEELArLQHEATAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKS 1774
Cdd:PRK10246 595 QDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1775 KQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLTEKLAAISEATrLKTEAEIALKEKEAENER 1854
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1855 lRRLAE-----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASESELERQKGLVE---DTLRQRRQVEEEIMALKAS 1922
Cdd:PRK10246 745 -QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVTqtaQALAQHQQHRPDGLDLTVT 823
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 40849888 1923 FEKAAAGKAELELELgrirsnAEDTMRSKELAEQ----EAARQRQ 1963
Cdd:PRK10246 824 VEQIQQELAQLAQQL------RENTTRQGEIRQQlkqdADNRQQQ 862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1330-1546 |
7.11e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1330 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQE 1409
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ---ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE 1486
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1487 RLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALDEL--KLQAEEAERRLRQAEA 1546
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1364-1588 |
7.37e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1364 LAEAHAQAKAQAELEARelQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEI 1443
Cdd:COG4942 12 ALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1444 RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1516
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1517 AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1588
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1314-1531 |
9.43e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 64.51 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1314 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAELEA 1379
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1380 RELQRRMQEEVTRRE-EAAVDAQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEirvvrlqLETTERQRg 1458
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANAEREVQRQ-------LEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1459 gAEDELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELK 1531
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1340-1551 |
9.43e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrREEAAVDAQQQKRSIQEEL-------Q 1412
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAELaelekeiA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1413 HLRQSSEAEIQAKAQQVEAAERSRMR-----------IEEEIRVVRLQLETTERQRggaeDELQALRARAEEAEAQKRQA 1481
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1482 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1551
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1089-1585 |
1.03e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1089 GAEEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELrgAQEVGERLQQRHGERDVEVERWRE 1168
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1169 RVTQLLER--------WQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQE 1240
Cdd:COG4913 317 RLDALREEldeleaqiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1241 KALLEEIErhgekveecqkfakqyiNAIKDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSELTTLTS 1320
Cdd:COG4913 397 EEELEALE-----------------EALAEAEAALRDLRRELRELE--AEIASLERRKSNIPARLLALRDALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1321 QYIKFISETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAELEAR 1380
Cdd:COG4913 458 AELPFVGELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1381 ELQRRM-----------QEEVTRREEAA-VDAQQQ----KRSIQEELQ--------------HLR------QSSEAEIQA 1424
Cdd:COG4913 535 SLAGKLdfkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRsryvlgFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1425 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGG---------AEDELQALRARAEEAEAQKRQAQE---EAERLRRQV 1492
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDAssdDLAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1493 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSK 1570
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEER 774
|
570
....*....|....*
gi 40849888 1571 RASFAEKTAQLERTL 1585
Cdd:COG4913 775 IDALRARLNRAEEEL 789
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4298-4335 |
1.52e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.52e-09
10 20 30
....*....|....*....|....*....|....*...
gi 40849888 4298 QRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMV 4335
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1455-1993 |
1.64e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 64.49 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1455 RQRGGAEDELQALRaRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQA 1534
Cdd:COG3899 716 LARGAYAEALRYLE-RALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARA 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1535 EEAERRLRQAEAERARQV-QVALETAQRSAEVELQskrasfaektAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAR 1613
Cdd:COG3899 795 YANLGLLLLGDYEEAYEFgELALALAERLGDRRLE----------ARALFNLGFILHWLGPLREALELLREALEAGLETG 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1614 EEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGT 1693
Cdd:COG3899 865 DAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAA 944
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1694 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1773
Cdd:COG3899 945 LAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAAL 1024
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1774 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENE 1853
Cdd:COG3899 1025 AALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1854 RLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 1933
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLA 1184
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1934 ELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 1993
Cdd:COG3899 1185 AAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1423-1655 |
1.85e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1423 QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1502
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1503 EAELALRVKAEAEAAREKQR-ALQALDELKLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1580
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1581 LERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQKSLAQADAEKQK 1655
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1356-1588 |
2.04e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.81 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1356 AALEKQRQLAEAHAQAKAQaeLEARelQRRMQEEVTRREE-----AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKAQQ 1428
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKAR--FEAR--QARLEREKAAREArhkkaAEARAAKDKDAVAAALARVKakKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1429 VEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL 1508
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1509 RVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1588
Cdd:PRK05035 592 KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1196-1811 |
2.40e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1196 RQLRYYRESADPLSSWLQDAKSRQEQIQAvpIANSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDY---- 1271
Cdd:PRK03918 111 SSVREWVERLIPYHVFLNAIYIRQGEIDA--ILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikrt 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1272 ---ELQLITYKAQLEPVASPAKK-----PKVQSGSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAEQQ 1343
Cdd:PRK03918 189 eniEELIKEKEKELEEVLREINEisselPELREELEKLEKEVKELEELKEEIEELEKE-LESLEGSKRKLEEKIRELEER 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1344 RAEERERLAEVEaalEKQRQLAEAHAQAKAQAEL-----------------------EARELQRRMqEEVTRREEAAVDA 1400
Cdd:PRK03918 268 IEELKKEIEELE---EKVKELKELKEKAEEYIKLsefyeeyldelreiekrlsrleeEINGIEERI-KELEEKEERLEEL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1401 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ 1480
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1481 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELKLQAEEAERRLRQAEAERARQ--VQVALET 1558
Cdd:PRK03918 424 LKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTA--ELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1559 AQ--RSAEVELQSKRASFAEKTAQLERTLQEEHVTVT--------------QLREEAERRAQQQAEAERAREEAERELER 1622
Cdd:PRK03918 502 AEqlKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkelekleELKKKLAELEKKLDELEEELAELLKELEE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1623 WQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQ 1702
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1703 ELIRLRAETEQgeqqrqlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlaSKARAEEESrstSEKSKQRLEAEA 1782
Cdd:PRK03918 660 EYEELREEYLE-------LSRELAGLRAELEELEKRREEIKKTLEKLKEELEER--EKAKKELEK---LEKALERVEELR 727
|
650 660
....*....|....*....|....*....
gi 40849888 1783 GRFRELAEEAARlRALAEEAKRQRQLAEE 1811
Cdd:PRK03918 728 EKVKKYKALLKE-RALSKVGEIASEIFEE 755
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1321-1960 |
2.49e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1321 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDA 1400
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1401 QQQKRSIQEELQHLRQ---SSEAEIQA-KAQQVEAAERSRMRIEEEIRVVRLQLetteRQRGGA--------EDELQALR 1468
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1469 AR----AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAldelklQAEEAERRLRQ 1543
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1544 AEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERW 1623
Cdd:pfam15921 311 QNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1624 QLKanealrLRLQAEevaQQKSLAQADAekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLA---------EGTA 1694
Cdd:pfam15921 390 EKE------LSLEKE---QNKRLWDRDT--------------GNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1695 QQRLAAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheataaTQKRQELEAELAKVrAEMEVLLASKARAEEESRST 1770
Cdd:pfam15921 447 ERQMAAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1771 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLTEKLAAISEATRL-KTEAEIA 1844
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKE 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1845 LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEIMA 1918
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEV 678
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 40849888 1919 LKASF----EKAAAGKAELELELGRIRSNAE---DTMRSKELAEQEAAR 1960
Cdd:pfam15921 679 LKRNFrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1409-1783 |
2.55e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 63.38 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1409 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETT----ERQRGGAEDELQALRARAEEAEAQKRQAQEE 1484
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1485 AERL---RRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELKLQAEEAERRLRQAEAERaRQVQVALETAQ- 1560
Cdd:pfam07888 110 SEELseeKDALLAQRAAHEARIRELEEDIKTLTQRVLERE---TELERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEe 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1561 --RSAEVELQSKRASFAEKTAQLERtLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKAnEALRLRLqaE 1638
Cdd:pfam07888 186 elRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV-EGLGEEL--S 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1639 EVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1718
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1719 QLLEEELARlqhEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1783
Cdd:pfam07888 342 EKLEVELGR---EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1359-1563 |
3.44e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1359 EKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKAQQVEAAERsrmr 1438
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1439 ieeeirvvrlQLETTERQRGGAEDELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1517
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 40849888 1518 REKQRALQALDELKLQAE-EAERRLRQAEAERARQVQVALETAQRSA 1563
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAaEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
150-252 |
3.49e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.39 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 150 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 228
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 40849888 229 PEDVDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1640-1874 |
3.98e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1640 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1719
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1720 LLEEELARLQHEAtaatqKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRAL 1798
Cdd:COG4942 94 ELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1799 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1874
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1677-2548 |
5.00e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.89 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1677 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeME 1754
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1755 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLTEKLAAISEA 1834
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1835 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleEQAAQHKADIEErlaqlrkasesELERQKGLVEDTLRQRRQVEE 1914
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGE-----------ELEALKTELEDTLDTTAAQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1915 EimalkasfekaaagKAELELELGRIRSNAEDTMRSKELAEQEAaRQRQLaaeeeqrrreaeervqrslAAEEEAARQrk 1994
Cdd:pfam01576 321 L--------------RSKREQEVTELKKALEEETRSHEAQLQEM-RQKHT-------------------QALEELTEQ-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1995 vaLEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLERLRSEA 2072
Cdd:pfam01576 365 --LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQSEL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2073 EAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAA 2152
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2153 DAEMEKHKKFAEQTL-------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA----RQRSQVEeelfs 2221
Cdd:pfam01576 523 QAQLSDMKKKLEEDAgtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVS----- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2222 vrvQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKmkqvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2301
Cdd:pfam01576 598 ---NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK----ETRALSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2302 --------------KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQL-- 2365
Cdd:pfam01576 671 sskddvgknvheleRSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2366 ---EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIA 2442
Cdd:pfam01576 750 qvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2443 ELEREKEKLKQEAKLLQLKSE----EMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQ 2518
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDlaasERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL 907
|
890 900 910
....*....|....*....|....*....|
gi 40849888 2519 LQEEQQRQQQQMEQEKQELVASMEEARRRQ 2548
Cdd:pfam01576 908 LNDRLRKSTLQVEQLTTELAAERSTSQKSE 937
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
35-134 |
5.41e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 35 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILH 134
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
145-247 |
6.35e-09 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 56.71 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 145 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 223
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 40849888 224 TRLLDPEDVDVPQPDEKSIITYVS 247
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1717-2048 |
6.36e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1717 QRQLLEEELARLQHEATAATQKRQEL--EAELAKVRAEMEvllaSKARAEEESRSTSEKSKQRlEAEAGRFRELAEEAAR 1794
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKE----EKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1795 LralaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAisEATRLKtEAEIALKEKEAENERLRRlaEDEAFQRRRLEEQAA 1874
Cdd:pfam17380 342 M-----AMERERELERIRQEERKRELERIRQEEIAM--EISRMR-ELERLQMERQQKNERVRQ--ELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1875 QHKADIEER-LAQLRKASESELERQ-KGLVEDTLRQRRQVEEEIMalkasfekaaagkaELELELGRIRSNAEDTMRSKE 1952
Cdd:pfam17380 412 QRKIQQQKVeMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQ--------------ERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1953 LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEeaaRQRKVALEEVE-RLKAKVEEARR------LRERAEQESARQL 2025
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKEMEeRQKAIYEEERRreaeeeRRKQQEMEERRRI 554
|
330 340
....*....|....*....|....*.
gi 40849888 2026 QLAQEAA---QKRLQAEEKAHAFVVQ 2048
Cdd:pfam17380 555 QEQMRKAteeRSRLEAMEREREMMRQ 580
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
511-700 |
6.76e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.38 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 511 LRYLHDLLAWVEENQRRIDGAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAY---RDCLGRLD 587
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 588 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEI 664
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 40849888 665 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 700
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1091-1581 |
6.77e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.68 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1091 EEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQpvfnTLRDELRGAQEVGERL--QQRHGERDVEVERWRE 1168
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT----SIREISCQQHTLTQHIhtLQQQKTTLTQKLQSLC 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1169 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIE 1248
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1249 RHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyI 1323
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQ-R 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1324 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQ 1403
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1404 K----------------------------RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTER 1455
Cdd:TIGR00618 639 QelalkltalhalqltltqervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDR 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1456 QRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAE 1535
Cdd:TIGR00618 719 EF---NEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLRE 795
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 40849888 1536 EAERRLRQAEAE---RARQVQVALETAQRSAEVELQSKRASFAEKTAQL 1581
Cdd:TIGR00618 796 EDTHLLKTLEAEigqEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATL 844
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1331-1564 |
7.45e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.09 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKrsIQEE 1410
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1411 LQHLRQSSEAEIQAKAQQVEAAERSRMRI---------EEEIRVVRLQLETTERQRggAEDELQALRARAEEAEAQKRQA 1481
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1482 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQR 1561
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 40849888 1562 SAE 1564
Cdd:pfam13868 272 EDE 274
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1234-1523 |
7.47e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.06 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1234 REQLRQEKA-LLEEIERHgEKVEECQKFAKQYINA----IKDYELQLITYKAQLEPVASPAKKPKVQsgsesviqeyvdl 1308
Cdd:pfam17380 298 QERLRQEKEeKAREVERR-RKLEEAEKARQAEMDRqaaiYAEQERMAMERERELERIRQEERKRELE------------- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1309 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELqRRMQE 1388
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV-RRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1389 EVTR-----REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQV-----------EAAERSRMRIEEEIRVVRLQLET 1452
Cdd:pfam17380 443 ERARemervRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRaeeqrrkilekELEERKQAMIEEERKRKLLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1453 TERQRGGAEDElqalRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRA 1523
Cdd:pfam17380 523 EERQKAIYEEE----RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1091-1281 |
7.50e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.00 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1091 EEVLKTHEEHLKEAQaVPATLQELEVTKASLKKLRAQAEAQQPVFNTLrdelrgaQEVGERLQQRHGERDVEVerwRERV 1170
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1171 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLSSWLQDAKSRQEQIQavPIANSQAAREQLRQEKALLEEIERH 1250
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 40849888 1251 GEKVEECQKFAKQYINAIKDYELQLITYKAQ 1281
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
154-249 |
8.42e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.93 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 154 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 209
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 40849888 210 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 249
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1678-1909 |
9.50e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.63 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAelakvraemevll 1757
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1758 askARAEEESRSTSEKSKQRLEAEAGRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERvlteklaAISEATRL 1837
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAEAK-------KKAEEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1838 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASESELERQKGLVEDTLRQR 1909
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1219-1870 |
1.08e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1219 QEQIQAVPIANSQAAR-EQLRQEKALLEEIERHGEKVEE-----CQKFAKQYINAIkDYELQLITYKAQLEPVAspAKKP 1292
Cdd:COG3096 498 RELLRRYRSQQALAQRlQQLRAQLAELEQRLRQQQNAERlleefCQRIGQQLDAAE-ELEELLAELEAQLEELE--EQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1293 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKfISETLRRMEEE---------------ERLAEQQRA--EERERLAEVE 1355
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLA-AQDALERLREQsgealadsqevtaamQQLLEREREatVERDELAARK 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1356 AALEKQ---------------RQLAEA-----------------------------HAQAKAQAELEARELQRR------ 1385
Cdd:COG3096 654 QALESQierlsqpggaedprlLALAERlggvllseiyddvtledapyfsalygparHAIVVPDLSAVKEQLAGLedcped 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1386 ---MQEEVTRREEAAVDAQQQKRSI--QEELQHLRQSSEAEI-----QAKAQQVEAAERSRMRIEEEIRVVRLQLETTER 1455
Cdd:COG3096 734 lylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVplfgrAAREKRLEELRAERDELAEQYAKASFDVQKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1456 QRGGAEDEL-----QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAeaelalrvkaeAEAAREKQRALQAL--- 1527
Cdd:COG3096 814 LHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ-----------LDQLKEQLQLLNKLlpq 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1528 ------DELKLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVeLQSKRASFAEKTAQLERTLQEEHVTVTQLreea 1599
Cdd:COG3096 883 anlladETLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLVAV-LQSDPEQFEQLQADYLQAKEQQRRLKQQI---- 957
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1600 erraqqqaeaerareeaerelerwqlkanEALrlrlqaEEVAQQKS-LAQADAEKQkeeaereaRRRGKAEEQAVRQR-E 1677
Cdd:COG3096 958 -----------------------------FAL------SEVVQRRPhFSYEDAVGL--------LGENSDLNEKLRARlE 994
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA----RLQHEATA-ATQKRQELEAELAKVRAE 1752
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEelgvQADAEAEErARIRRDELHEELSQNRSR 1074
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1753 MEVLLASKARAEEESRSTSEKSKQrLEAEAGRFRELAEEA----ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKl 1828
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSLQKRLRK-AERDYKQEREQVVQAkagwCAVLRLARDNDVERRLHRRELAYLSADELRSMSDK- 1152
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 40849888 1829 aaiseatrlkteAEIALKEKEAENERLR---RLAEDEAFQRRRLE 1870
Cdd:COG3096 1153 ------------ALGALRLAVADNEHLRdalRLSEDPRRPERKVQ 1185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1324-1566 |
1.09e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1324 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQ 1403
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1404 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEDELQALRARAEEaEAQKRQAQE 1483
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1484 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALDELKLQAEEAER-RLRQAEAERARQVQVAL 1556
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 40849888 1557 ETAQRSAEVE 1566
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2263-2483 |
1.12e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2263 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2338
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2339 KEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2418
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2419 LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKS 2483
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1367-1822 |
1.23e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.57 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1367 AHAQAKAQAELEARELQRRMQEEVTRReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVV 1446
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1447 RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1526
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1527 LDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQ 1606
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1607 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1686
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1687 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1766
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1767 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1822
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAA 927
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1137-1962 |
1.49e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.51 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1137 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQREleQLGRqlryYRESADPLSSW 1211
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1212 LQdaksrqEQIQAVPIANSQAAREQLRQEKALlEEIERHG-------EKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1283
Cdd:COG3096 363 LE------EQEEVVEEAAEQLAEAEARLEAAE-EEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1284 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEER-ERLAEVEAALEK- 1360
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELlRRYRSQQALAQRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1361 ---QRQLAEAHAQAKAQAELE--ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERS 1435
Cdd:COG3096 515 qqlRAQLAELEQRLRQQQNAErlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1436 RM--RIEEEIRVVRLQLETTERQRGGAEDELQALRA-------RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1506
Cdd:COG3096 595 KElaARAPAWLAAQDALERLREQSGEALADSQEVTAamqqlleREREATVERDELAARKQALESQIERLSQPGGAEDPRL 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1507 A--------------------------------LR---VKAEAEAAREKQRAL--------------QALDELKLQAEEA 1537
Cdd:COG3096 675 LalaerlggvllseiyddvtledapyfsalygpARhaiVVPDLSAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEEL 754
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1538 ERRL------RQAEAER----------ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE---EHVTVtqlree 1598
Cdd:COG3096 755 EDAVvvklsdRQWRYSRfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAV------ 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1599 aerraqqqaeaeRAREEAERELERWQLKANEALR-LRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1677
Cdd:COG3096 829 ------------AFAPDPEAELAALRQRRSELEReLAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLE 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAEQELEKQRQLAEGTAQQRLAAEQ---ELIRLRAETEQGEQqrqlleeelarLQHEATAATQKRQELEAE---LAKVRA 1751
Cdd:COG3096 897 ELREELDAAQEAQAFIQQHGKALAQlepLVAVLQSDPEQFEQ-----------LQADYLQAKEQQRRLKQQifaLSEVVQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1752 EMEVLLASKARAE-EESRSTSEKSKQRLEAeagrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAERVLTeklaa 1830
Cdd:COG3096 966 RRPHFSYEDAVGLlGENSDLNEKLRARLEQ------------------AEEARREAREQLRQAQAQYSQYNQVLA----- 1022
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1831 iSEATRLKTEAEIaLKEKEAENERLRRLAEDEAfqrrrlEEQAAQHKADIEERLAQLRkASESELERQKGLVE---DTLR 1907
Cdd:COG3096 1023 -SLKSSRDAKQQT-LQELEQELEELGVQADAEA------EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQ 1093
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1908 QR-RQVEEEIMALKASFEKAAAGKAELeLELGRiRSNAEDTMRSKELAEQEAARQR 1962
Cdd:COG3096 1094 KRlRKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVERRLHRRELAYLSADELR 1147
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1672-2044 |
1.84e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1672 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEATAATQK----RQ 1740
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1741 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1798
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1799 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAAQHK 1877
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1878 AdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 1957
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1958 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQ 2037
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
....*..
gi 40849888 2038 AEEKAHA 2044
Cdd:COG3096 660 IERLSQP 666
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1331-1592 |
1.88e-08 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 60.05 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR--REEAAVDAQQQKRSIQ 1408
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1409 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqletterqRGGAEDELQALRARAEEAEaQKRQAQEEAERL 1488
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1489 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1564
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 40849888 1565 VELQSKRASFAEKTAQLERTLQEEHVTV 1592
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1251-2020 |
1.91e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1251 GEKVEECQ---KFAKQYINAIKDYELQLITYKAQLEPVASPAKK------------PKVQSGSESVIQ---EYVDLRTRY 1312
Cdd:TIGR00606 199 GQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLESSREIVKSyeneldplknrlKEIEHNLSKIMKldnEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1313 SELTTLTSQYIKFISETLRRMEEEERLAEQQRA----EERERLAEVEAALEKQRQLAEAHAQAKAqaELEARELQRRMQE 1388
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQrtvrEKERELVDCQRELEKLNKERRLLNQEKT--ELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1389 EVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaqqveaaersrmrieeeiRVVRLQLETTERQRGGAEDELQALR 1468
Cdd:TIGR00606 357 DRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK------------------NFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1469 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKlqaeEAERRLRQAEAER 1548
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEKNS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1549 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLER---------TLQEEHVTVTQLREEAERRAQQQAEAERAREEAERE 1619
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1620 LERW-QLKANEALRLRLQAEEVaqQKSLAQADAEKQKEEAerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQrl 1698
Cdd:TIGR00606 575 LEDWlHSKSKEINQTRDRLAKL--NKELASLEQNKNHINN---------------ELESKEEQLSSYEDKLFDVCGSQ-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1699 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQ----------ELEAELAKVRAEMEVLLASKARAEEESR 1768
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1769 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR---AEAERVLTEKLAAISEATRLKTEAEIAL 1845
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPEEESAKVCLTDVTIME 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1846 KEKEAENERLRRLAE----------DEAFQRRRLEEQAAQHKAD------------IEERLAQLR--KASESELERQKGL 1901
Cdd:TIGR00606 796 RFQMELKDVERKIAQqaaklqgsdlDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNELKSEKLQ 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1902 VEDTLRQRRQVEE-------EIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAarQRQLAAEEEQRRRE 1974
Cdd:TIGR00606 876 IGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA--QDKVNDIKEKVKNI 953
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 40849888 1975 AEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQE 2020
Cdd:TIGR00606 954 HGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
145-252 |
1.93e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 55.10 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 145 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 223
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 40849888 224 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
37-131 |
2.80e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 37 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 108
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 40849888 109 VNIRNDDIADGNPKLTLGLIWTI 131
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2247-2582 |
3.53e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2247 DKDNTQRFLEEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaEAELLQQQKE 2326
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2327 LAQEQARRLQEDKEQmaqqlveetqgfQRTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGE-K 2405
Cdd:pfam17380 342 MAMERERELERIRQE------------ERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2406 LHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAkllQLKSEEMQTVQQEQILQETQALQKSFL 2485
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE---QERQQQVERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2486 SEKDSLL--QRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVAsmEEARRRQREAEEGVR------- 2556
Cdd:pfam17380 483 KRDRKRAeeQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA--EEERRKQQEMEERRRiqeqmrk 560
|
330 340
....*....|....*....|....*...
gi 40849888 2557 --RKQEELQRLEQQRQQQEKLLAEENQR 2582
Cdd:pfam17380 561 atEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1331-1538 |
3.83e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERErlaEVEAALEKQRQLAEAHAQAkaqaelearelqrrmQEEVTRREEAAVDAQQQKRsiQEE 1410
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQ---KQAAEQERLKQLEKERLAA---------------QEQKKQAEEAAKQAALKQK--QAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1411 LQHLRQSSEAEIQAKAQQVEAAERSRmRIEEEIRvVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERlrr 1490
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK--- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 40849888 1491 qVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELKLQAEEAE 1538
Cdd:PRK09510 211 -AAAEAKKKAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1006-1590 |
4.06e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1006 RECAQRIAEQQKAQAEVEGLGKGVARLSAEAEkvlalpepspaaptlrsELELTLGKLEQVRslsaiyleklktislvir 1085
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----------------ELEELLAELEAQL------------------ 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1086 stqgaeevlKTHEEHLKEAQAVPATL-QELEVTKASLKKLRAQAEA---QQPVFNTLRDE----LRGAQEVGERLQQR-H 1156
Cdd:COG3096 567 ---------EELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPAwlaAQDALERLREQsgeaLADSQEVTAAMQQLlE 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1157 GERDVEVER-----WRERVTQLLERWQAVLAQTDVRQREL-EQLGRQLryYRESADPLSswLQDAK--------SRqeqi 1222
Cdd:COG3096 638 REREATVERdelaaRKQALESQIERLSQPGGAEDPRLLALaERLGGVL--LSEIYDDVT--LEDAPyfsalygpAR---- 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1223 QAVPIANSQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKK 1291
Cdd:COG3096 710 HAIVVPDLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRL 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1292 PKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQR----QLAEA 1367
Cdd:COG3096 788 EELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRaqeqQLRQQ 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1368 HAQAKAQAELEARELQRRM-------QEEVTRREEAAVDAQQQKRSIQEELQHLR---------QSSEAEIQAKAQQVEA 1431
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQANlladetlADRLEELREELDAAQEAQAFIQQHGKALAqleplvavlQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1432 AERSRMRIEEEI--------RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR----- 1498
Cdd:COG3096 946 AKEQQRRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVlaslk 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1499 -----KRQAEAEL-----ALRVKAEAEAArekQRALQALDELKLQAEEAERRLRQAEAERARQvqvaletaqrSAEVELQ 1568
Cdd:COG3096 1026 ssrdaKQQTLQELeqeleELGVQADAEAE---ERARIRRDELHEELSQNRSRRSQLEKQLTRC----------EAEMDSL 1092
|
650 660
....*....|....*....|..
gi 40849888 1569 SKRASFAEKTAQLERTLQEEHV 1590
Cdd:COG3096 1093 QKRLRKAERDYKQEREQVVQAK 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1515-1962 |
4.15e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1515 EAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtq 1594
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1595 lreeaerraqqqaeaerareeaereLERW-QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRgKAEEQAV 1673
Cdd:COG4717 145 -------------------------PERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-EELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1674 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1753
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1754 EVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISE 1833
Cdd:COG4717 279 LFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1834 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR-R 1910
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElE 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1911 QVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQR 1962
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1036-1582 |
4.59e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1036 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEaqaVPATLQELE 1115
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1116 VTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLqqrhgerdveverwrERVTQLLERWQAVLAQTDVRQRELEQLG 1195
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---------------SRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1196 RQLRYYRESADPLSSW---LQDAKSRQEQIqavpiansqaarEQLRQEKALL--EEIERHGEKVEECQKFAKQYINAIKD 1270
Cdd:PRK03918 345 KKLKELEKRLEELEERhelYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1271 YELQLITYKAQLEPVASPAKKPKVQ---SGSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEE 1347
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKcpvCGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1348 RERLAEVEAALEKQRQLAEAHAQAKAQAELEaRELQRRMQEEVTRREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKAQ 1427
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1428 QVEAAErsrmRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1507
Cdd:PRK03918 547 ELEKLE----ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1508 lRVKAEAEAAREK-QRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1582
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1328-1550 |
4.99e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1328 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQkr 1405
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 siqeelQHLRQSSEAEIQAKAQQveaaersrmrieeeirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQEE- 1484
Cdd:TIGR02794 146 ------EEAAKQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1485 ---AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERAR 1550
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1431-1935 |
5.13e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 59.87 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1431 AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQ---------VQDESQRKRQ 1501
Cdd:COG3899 731 ALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASarayanlglLLLGDYEEAY 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1502 AEAELALRVKAEAEAAREKQRALQALDEL---KLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT 1578
Cdd:COG3899 811 EFGELALALAERLGDRRLEARALFNLGFIlhwLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAA 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1579 AQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqksLAQADAEKQKEEA 1658
Cdd:COG3899 891 AAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAAL---AAALALAAAAAAA 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1659 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1738
Cdd:COG3899 968 AAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLA 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1739 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRA 1818
Cdd:COG3899 1048 ALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAA 1127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1819 EAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQ 1898
Cdd:COG3899 1128 AARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLA 1207
|
490 500 510
....*....|....*....|....*....|....*..
gi 40849888 1899 KGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELEL 1935
Cdd:COG3899 1208 ALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1699-2508 |
5.64e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1699 AAEQELIRLRAETEQGEQQRQLLEEElaRLQHEataatqKRQELEAELAKVRAEmevLLASKARAEEESRSTSEKSKQRL 1778
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRE--REKAE------RYQALLKEKREYEGY---ELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1779 EAEAGRFRELAEE-----AARLRALAEEAKRQRQLAEEDAARQRAEAERVlteklaaisEATRLKTEAEIALKEKEAEnE 1853
Cdd:TIGR02169 250 EEELEKLTEEISElekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL---------EAEIASLERSIAEKERELE-D 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1854 RLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglVEDTLRQRrqVEEEIMALKASFEKAAAGKAEL 1933
Cdd:TIGR02169 320 AEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE--ELEDLRAE--LEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1934 ELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKVEEARRl 2013
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE----WKLEQLAADLSKYEQ- 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2014 RERAEQESARQLQLAQEAAQKRLqAEEKAHAFVVQQREEELQQTLQqeqnMLERLRSEAEAARRAAEEAEEAREQAEREA 2093
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQREL-AEAEAQARASEERVRGGRAVEE----VLKASIQGVHGTVAQLGSVGERYATAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2094 AQSRKQ--VEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAqaeqaaLKQKQAADAEM------EKHKKFAEQ 2165
Cdd:TIGR02169 545 AGNRLNnvVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSI------LSEDGVIGFAVdlvefdPKYEPAFKY 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2166 TLRQKAQVEQELTTLRLQLEetdHQKSILDEELQRLKAEVTEAARQRS-------QVEEELFSVRVQMEELGKLKARIEA 2238
Cdd:TIGR02169 619 VFGDTLVVEDIEAARRLMGK---YRMVTLEGELFEKSGAMTGGSRAPRggilfsrSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2239 ENRALILRDKDNTQRFLEEEaekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavQEATRLkaEA 2318
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK----SELKEL--EA 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2319 ELLQQQKELAQEQARrLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlklrmAEMSRAQARAEEDAQRFRKQ 2398
Cdd:TIGR02169 766 RIEELEEDLHKLEEA-LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-----KLNRLTLEKEYLEKEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2399 AEEIGEKLHRTELATQekvtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQ------ 2472
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKE-----IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELeaqiek 914
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 40849888 2473 ------ILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQL 2508
Cdd:TIGR02169 915 krkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV 956
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2237-2614 |
6.53e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 6.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2237 EAENRALILRDKDNTQRFLEEEAEKMKQvaeeaarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmQAVQEATRLKA 2316
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKED--------NRADEATEEAFGKAEEAKKTETGKAEEARKAE-EAKKKAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2317 EAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKlRMAEMSRAQ-ARAEEDAQRF 2395
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEdARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2396 rkQAEEIGEKLHRTELAtqEKVTLVQTLEiqrqQSDQDAERLREAIAELEREKEKLKQEAKLLQ-------LKSEEMQTV 2468
Cdd:PTZ00121 1209 --EEERKAEEARKAEDA--KKAEAVKKAE----EAKKDAEEAKKAEEERNNEEIRKFEEARMAHfarrqaaIKAEEARKA 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2469 QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQQQQMEQEKQELVASmEEARRRQ 2548
Cdd:PTZ00121 1281 DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA-KKKAEEAKKKADAAKKKAEEAKKAAEAAKAE-AEAAADE 1358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 2549 REAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAlahsEEIATSQAAATKA 2614
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKKKA 1420
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1700-1900 |
7.25e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1700 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1779
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1780 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA 1841
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1842 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKG 1900
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1370-2606 |
7.36e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1370 QAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAqqveaaersrmrieEEIRVvRLQ 1449
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEA--------------EEMRA-RLA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1450 LETTErqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAElalrvkaeaEAAREKqralqalde 1529
Cdd:pfam01576 68 ARKQE-----LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEE---------EAARQK--------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1530 LKLQAEEAERRLRQAEAErarqvqVALETAQRSaevELQSKRASFAEKTAQLERTLQEEHVTV---TQLREEAERRAQQQ 1606
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEED------ILLLEDQNS---KLSKERKLLEERISEFTSNLAEEEEKAkslSKLKNKHEAMISDL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1607 AEAERAREEAERELERWQLKAN--------EALRLRLQAEEVAQQksLAQADAEKQkeeaereaRRRGKAEEQAVRQREL 1678
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKLEgestdlqeQIAELQAQIAELRAQ--LAKKEEELQ--------AALARLEEETAQKNNA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1679 AEQELEKQRQLAEgtAQQRLAAEqelirlRAETEQGEQQRQLLEEELARLQHE---ATAATQKRQELEAelakvRAEMEV 1755
Cdd:pfam01576 263 LKKIRELEAQISE--LQEDLESE------RAARNKAEKQRRDLGEELEALKTEledTLDTTAAQQELRS-----KREQEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1756 LLASKArAEEESRSTSEKSKQRLEAEAGRFRELAEEAarlralaEEAKRQRQLAEEdaARQRAEAERV-LTEKLAAISEA 1834
Cdd:pfam01576 330 TELKKA-LEEETRSHEAQLQEMRQKHTQALEELTEQL-------EQAKRNKANLEK--AKQALESENAeLQAELRTLQQA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1835 trlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE-------------RLAQLRKASESELERQKGL 1901
Cdd:pfam01576 400 ---KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESvssllneaegkniKLSKDVSSLESQLQDTQEL 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1902 VEDTLRQR-------RQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTmrsKELAEQEAARQRQLAAEEEQrrre 1974
Cdd:pfam01576 477 LQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM---KKKLEEDAGTLEALEEGKKR---- 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1975 aeervqrsLAAEEEAARQRkvaLEEVERLKAKVEEAR-RLRERAE-----QESARQLQLAQEAAQKR---LQAEEKA-HA 2044
Cdd:pfam01576 550 --------LQRELEALTQQ---LEEKAAAYDKLEKTKnRLQQELDdllvdLDHQRQLVSNLEKKQKKfdqMLAEEKAiSA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2045 FVVQQREEELQQTLQQEQNMLERLRSEAEAarraaeeaeeareqaereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAA 2124
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEA----------------------LEAKEELERTNKQLRAEMEDLVSSKDDV 676
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2125 EKLRKEAEQEAARRAQAEQAALKQKQAADAEM---EKHKKFAEQTLRQ-KAQVEQELTTLRLQLEEtdhQKSILDEELQR 2200
Cdd:pfam01576 677 GKNVHELERSKRALEQQVEEMKTQLEELEDELqatEDAKLRLEVNMQAlKAQFERDLQARDEQGEE---KRRQLVKQVRE 753
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2201 LKAEVTEAARQRSQveeeLFSVRVQME-ELGKLKARIEAENRAlilRDkdntqrfleeeaEKMKQVAEEAARLSVAAQEA 2279
Cdd:pfam01576 754 LEAELEDERKQRAQ----AVAAKKKLElDLKELEAQIDAANKG---RE------------EAVKQLKKLQAQMKDLQREL 814
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2280 ARLRQLAEEDLAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLVEETQGfqRTL 2357
Cdd:pfam01576 815 EEARASRDEILAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSA 879
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2358 EAERQRQLEmsaeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDQDAERL 2437
Cdd:pfam01576 880 LQDEKRRLE-----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKEL 950
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2438 REAIAELERE-KEKLKQEAKLLQLKSEEMQtvqqEQILQETQALQKSflsekdsllqrERFIEQEKAKLEQLfqdevaka 2516
Cdd:pfam01576 951 KAKLQEMEGTvKSKFKSSIAALEAKIAQLE----EQLEQESRERQAA-----------NKLVRRTEKKLKEV-------- 1007
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2517 kqlqeeqqrqqqqmeqekqelVASMEEARRRQreaeEGVRRKQEELQRLEQQRQQQEKLLAEENQRL---RERLQR-LEE 2592
Cdd:pfam01576 1008 ---------------------LLQVEDERRHA----DQYKDQAEKGNSRMKQLKRQLEEAEEEASRAnaaRRKLQReLDD 1062
|
1290
....*....|....
gi 40849888 2593 EHRAALAHSEEIAT 2606
Cdd:pfam01576 1063 ATESNESMNREVST 1076
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1733-1887 |
7.42e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1733 TAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRAlaEEAKRQRQLAEED 1812
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1813 AARQR------AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1886
Cdd:COG2268 286 AEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEK 365
|
.
gi 40849888 1887 L 1887
Cdd:COG2268 366 L 366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1462-1921 |
7.46e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1462 DELQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELALrvkAEAEAAREKQRALQALDELKLQAEEAERRL 1541
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL------EELEEELEELEAEL---EELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1542 RQaEAERARQVQVALEtAQRSAEVELQSKRASFAEKTAQLERTLQeehvtvtQLREEAERRAQQQAEAERAREEAERELE 1621
Cdd:COG4717 142 AE-LPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLE-------QLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG--------- 1692
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallfll 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1693 TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstsE 1772
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEL---E 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1773 KSKQRLEAEAGrfrelAEEAARLRALAEEAKRQRQLAEEdaarqRAEAERVLTEKLAAISEATRLKTEAEIalkekEAEN 1852
Cdd:COG4717 370 QEIAALLAEAG-----VEDEEELRAALEQAEEYQELKEE-----LEELEEQLEELLGELEELLEALDEEEL-----EEEL 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1853 ERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLrkASESELERQKGLVEDTLRQRRQVEEEIMALKA 1921
Cdd:COG4717 435 EELEEELEELEEELEELREE----LAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1348-1817 |
7.53e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 58.88 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1348 RERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQqqkrsiqeelqhLRQSSEAEIQAKAQ 1427
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAA------------LRWALAHGDAELAL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1428 QVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1507
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1508 LRvkAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1587
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1588 EHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGK 1667
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1668 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1747
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1748 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1817
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1401-1582 |
7.59e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1401 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEDELQalraraEEAEAQKRQ 1480
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERL--------------AAQEQK------KQAEEAAKQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1481 AQEEaerlrrQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAER---ARQVQVALE 1557
Cdd:PRK09510 127 AALK------QKQAEEAAAKAAAAAKA---KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 40849888 1558 TAQRSAEVELQSKRASFAEKTAQLE 1582
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1150-1457 |
8.10e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.98 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1150 ERLQQRHGERDVEVERWRervtQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplsswlQDAKSRQEQIQAVPIAN 1229
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1230 SQAAREQLRQEKALLE-----EIERHGEKVEECQKFAKQYINAIKDYELQ--LITYKAQLEPVASPAKKPKVQSGSESVI 1302
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILeeERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEAREL 1382
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1383 QRRMQEEVTRREEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQR 1457
Cdd:pfam17380 515 RKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMEREREMMRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1741-2605 |
8.52e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1741 ELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEaKRQRQLAEEDAARQRAEA 1820
Cdd:TIGR02169 167 EFDRKKEKALEELEEV---EENIERLDLIIDEKRQQL-----ERLRREREKAERYQALLKE-KREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1821 ERVLTEKlaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRL-EEQAAQHKADIEErlaqlrkaSESELERQK 1899
Cdd:TIGR02169 238 QKEAIER--QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGE--------LEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1900 GLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTM-RSKELAEQEAARQRQLAAEEEqrrreaeer 1978
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDK--------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1979 vqrSLAAEEEAARQRKVALEEVERLKAKVE-EARRLRERAEQESARQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQ 2056
Cdd:TIGR02169 379 ---EFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2057 TLQQEQNMLERLRSEAEAARRAAEEAEEAREqaereaaQSRKQVEEAERLKQSAEEQAQAQAqaqaaaeklrkeaeqeaa 2136
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELS-------KLQRELAEAEAQARASEERVRGGR------------------ 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2137 rraqaeqaalkqkqAADAEMEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-E 2204
Cdd:TIGR02169 511 --------------AVEEVLKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgR 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2205 VTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENR-----ALILRDKDNTQRfLEEEAEKMKQV-------------- 2265
Cdd:TIGR02169 575 ATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTLVVED-IEAARRLMGKYrmvtlegelfeksg 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2266 ------AEEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQE 2330
Cdd:TIGR02169 654 amtggsRAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2331 QARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTE 2410
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2411 LATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMqtvqqEQILQETQALQKSfLSEKDS 2490
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRD-LESRLG 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2491 LLQRERfiEQEKAKLEQLfQDEVAKAKqlqeeqqRQQQQMEQEKQELVASMEEARRRQREAEEGVRRkqeelQRLEQQRQ 2570
Cdd:TIGR02169 886 DLKKER--DELEAQLREL-ERKIEELE-------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-----DEEIPEEE 950
|
890 900 910
....*....|....*....|....*....|....*
gi 40849888 2571 QQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIA 2605
Cdd:TIGR02169 951 LSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVL 985
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1006-1590 |
9.09e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1006 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLE-------- 1075
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMAlrqqleql 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1076 -----KLKTISLVIRSTQGAEEVLKTH-EEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQpvfntlrdelRGAQEVG 1149
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQsGEEFEDSQDVTEYMQQLLERERELTVERDELAARK----------QALDEEI 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1150 ERLQQRHGERDveverwrERVTQLLERWQAVLAQTDVRQRELEQLGrqlrYYRESADPLSswlqdaksrqeqiQAVPIAN 1229
Cdd:PRK04863 662 ERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFSALYGPAR-------------HAIVVPD 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1230 SQAAREQLRQEKALLEEI-------ERHGEKVEECQKFAKQYINAIKDYELQLITYKAqlEPVASPAKKPK----VQSGS 1298
Cdd:PRK04863 718 LSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRAER 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1299 ESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRaeeRERLAEVEAALEKQRQLAEAHAQAKA 1373
Cdd:PRK04863 796 EELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRR---VELERALADHESQEQQQRSQLEQAKE 872
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1374 QAELEARELQRRM--------------QEEVTRREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE---- 1433
Cdd:PRK04863 873 GLSALNRLLPRLNlladetladrveeiREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqr 952
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1434 RSRMRIE--EEIRVVRLQLETTERQR-GGAEDELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalr 1509
Cdd:PRK04863 953 DAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL--- 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1510 vKAEAEAAREK-QRALQALDELKLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAEKTA 1579
Cdd:PRK04863 1026 -KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDY 1104
|
650
....*....|.
gi 40849888 1580 QLERTLQEEHV 1590
Cdd:PRK04863 1105 HEMREQVVNAK 1115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1709-2271 |
9.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1709 AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAGRFR 1786
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-LTEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 1860
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1861 DEAFQRRRLEEQAAQHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEIMALKASfekaaagKAELE 1934
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1935 LELGRIRSNAEDTMRSK--------ELAEQEAARqrqlaaeEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2006
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgrELTEEHRKE-------LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2007 VEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAFvvqqreeelqqtlqqeQNMLERLRSEAEAARRAAEEAEEAR 2086
Cdd:PRK03918 492 ESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEY----------------EKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2087 EQAEREAAQSRKqVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQT 2166
Cdd:PRK03918 553 ELKKKLAELEKK-LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2167 LRQKAQVEQELTTLRLQLEETDHQKSI------------LDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKA 2234
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSEeeyeelreeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590
....*....|....*....|....*....|....*..
gi 40849888 2235 RIEAENRALilrdkdntqRFLEEEAEKMKQVAEEAAR 2271
Cdd:PRK03918 712 ELEKLEKAL---------ERVEELREKVKKYKALLKE 739
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2305-2450 |
9.42e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 58.49 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2305 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLVEEtQGFQRTLEAERQRQLEMSAEAERLKL 2376
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2377 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDQDAERlREAIAELEREKEK 2450
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4029-4065 |
9.91e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 9.91e-08
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 4029 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4065
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1636-1819 |
1.15e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.51 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1636 QAEEVAQQKslaQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1711
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1712 EQGEQQRQLLEEELARLQHEATAatqkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEAGRFRELAE 1790
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 40849888 1791 EAArlRALAEEAKRQRQLAEEDAARQRAE 1819
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1636-1822 |
1.39e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.16 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1636 QAEEVAQQKSlAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1715
Cdd:TIGR02794 51 QANRIQQQKK-PAAKKEQERQK---------KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1716 QQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EA 1792
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEA 200
|
170 180 190
....*....|....*....|....*....|
gi 40849888 1793 ARLRALAEEAKRQRQLAeedAARQRAEAER 1822
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1485-1941 |
1.47e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 58.11 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1485 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALdelkLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1564
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLAR----LDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1565 VELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1644
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1645 SLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1724
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1725 LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1804
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1805 QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 1884
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1885 AQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIR 1941
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1632-2040 |
1.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1632 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRA 1709
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1710 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1789
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1790 EEAARLRALAEEAKRQRQLAEED---------------AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENER 1854
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1855 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKASFEKAAAGKAEl 1933
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1934 elelgRIRSNAEDTMRSKELAEQEAARQRQLaaeeeqrrreaeervqrslaAEEEAARQRKVALEEVERLKAKVEEARRL 2013
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQL--------------------EELLGELEELLEALDEEELEEELEELEEE 440
|
410 420
....*....|....*....|....*..
gi 40849888 2014 RERAEQESARQLQLAQEAAQKRLQAEE 2040
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEE 467
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1330-1870 |
1.97e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.44 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1330 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQE 1409
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ELQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALR------ARAEEAEAQKRQAQE 1483
Cdd:pfam05557 133 ELEELQERLD-LLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnskselARIPELEKELERLRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1484 EAERLRRQVQDESQRKRQAE---AELALRVKAEAEAAR---EKQRALQALDELKLQAEEAERRLRQAEAERARQVQvale 1557
Cdd:pfam05557 212 HNKHLNENIENKLLLKEEVEdlkRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQ---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1558 taqrsaeveLQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEaerareeaerelERWQLKANEALRLRLQa 1637
Cdd:pfam05557 288 ---------LQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIED------------LNKKLKRHKALVRRLQ- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1638 eevaQQKSLA--QADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL--IRLRAETEQ 1713
Cdd:pfam05557 346 ----RRVLLLtkERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggYKQQAQTLE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1714 GEQQ---RQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK---QRLEAEAGRFRE 1787
Cdd:pfam05557 422 RELQalrQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlhLSMNPAAEAYQQ 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1788 LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTeklAAISEATRLKTEAEIAlkekEAENERLRrlaedEAFQRR 1867
Cdd:pfam05557 502 RKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTST---MNFKEVLDLRKELESA----ELKNQRLK-----EVFQAK 569
|
...
gi 40849888 1868 RLE 1870
Cdd:pfam05557 570 IQE 572
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2196-2464 |
2.00e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2196 EELQRLKAEVTEAARQRSQVE------EELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEA 2269
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2270 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2349
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2350 TQGFQRTLEAERQRQLEMSAEAERLklrmaemSRAQARAEEDAQRFRKQAEEIgeklhRTELAtqekvtlvqtlEIQRQQ 2429
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL-------EEALAEAEAALRDLRRELREL-----EAEIA-----------SLERRK 435
|
250 260 270
....*....|....*....|....*....|....*...
gi 40849888 2430 S--DQDAERLREAIAE-LEREKEKLKQEAKLLQLKSEE 2464
Cdd:COG4913 436 SniPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2155-2607 |
2.08e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2155 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSVRVQMEE 2228
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2229 LGKLKARIEAENRALI--LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2306
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2307 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2381
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2382 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKL-KQEAKL 2457
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2458 LQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRER-----FIEQEKAKLEQL--FQDEVAKAKQLQEEQQRQQQQM 2530
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELepFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 2531 EQEKQELVASMEEARRRQREAEEgvrRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATS 2607
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEE---LRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1091-1750 |
2.20e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 57.49 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1091 EEVLKTHEEHLKE-----AQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVER 1165
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1166 WRERVTQ-------LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKS-RQEQIQAvPIANSQAAReQL 1237
Cdd:pfam01576 417 LQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQ-KLNLSTRLR-QL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1238 RQEKALLEEieRHGEKVEECQKFAKQyinaIKDYELQLITYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1305
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1306 ------------------VDLRTRYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlaeveaalekqrqlAEA 1367
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR--------------AEA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1368 HAQAKaqaELEARELQRRMQEEVTRREEAavdaQQQKRSIQEELQHLRQSSEAeiqaKAQQVEAAERSRMRIEEEIRVVR 1447
Cdd:pfam01576 630 EAREK---ETRALSLARALEEALEAKEEL----ERTNKQLRAEMEDLVSSKDD----VGKNVHELERSKRALEQQVEEMK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1448 LQLETTERQRGGAED-------ELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEA-------- 1504
Cdd:pfam01576 699 TQLEELEDELQATEDaklrlevNMQALKAqferdlqaRDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakkkleld 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1505 --------ELALRVKAEA------------EAAREKQRALQALDELKLQAEEAERRLRQAEAE--RARQVQVALETAQRS 1562
Cdd:pfam01576 779 lkeleaqiDAANKGREEAvkqlkklqaqmkDLQRELEEARASRDEILAQSKESEKKLKNLEAEllQLQEDLAASERARRQ 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1563 AEVE-----------------LQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELE---- 1621
Cdd:pfam01576 859 AQQErdeladeiasgasgksaLQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQkses 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 -RWQL-KANEALRLRLQAEEVA---QQKSLAQA------DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1690
Cdd:pfam01576 939 aRQQLeRQNKELKAKLQEMEGTvksKFKSSIAAleakiaQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHA 1018
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1691 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVR 1750
Cdd:pfam01576 1019 DQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1542-2460 |
2.28e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 57.67 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1542 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERElE 1621
Cdd:TIGR00618 56 RRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIH-D 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGtaqQRLAAE 1701
Cdd:TIGR00618 135 LLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQL---LTLCTP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1702 QELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAemevllASKARAEEESRSTSEKSKQRLEAE 1781
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL------LKQLRARIEELRAQEAVLEETQER 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1782 AGRFRELAEEAARLRALaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKtEAEIALKEKEAENERLRRLAED 1861
Cdd:TIGR00618 286 INRARKAAPLAAHIKAV-TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1862 EAFQRRRLEEQAAqhkadIEERLAQLRKASESELERQKGLVEDTLRQRR---QVEEEIMALKASFEKAAAGKAELELELG 1938
Cdd:TIGR00618 364 ATSIREISCQQHT-----LTQHIHTLQQQKTTLTQKLQSLCKELDILQReqaTIDTRTSAFRDLQGQLAHAKKQQELQQR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1939 RI---RSNAEDTMRSKELAEQEAARQRQlaaeeeqrrreaeervqrSLAAEEEAARQRKVALEEVERLKAkvEEARRLRE 2015
Cdd:TIGR00618 439 YAelcAAAITCTAQCEKLEKIHLQESAQ------------------SLKEREQQLQTKEQIHLQETRKKA--VVLARLLE 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2016 RAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQ 2095
Cdd:TIGR00618 499 LQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2096 SRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRkeaeqeaarraqaeqaALKQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2175
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA----------------CEQHALLRKLQPEQDLQDVRLHLQQCSQELA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2176 ELTTLRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFL 2255
Cdd:TIGR00618 643 LKLTALHALQLTLTQERV-REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2256 EEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2335
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2336 QEDKEQMAQQLVEETQgfQRTLEAERQRQlemsaEAERLKLRMAEMSRAQAraeedaqRFRKQAEEIGEKLHRTELATQE 2415
Cdd:TIGR00618 802 KTLEAEIGQEIPSDED--ILNLQCETLVQ-----EEEQFLSRLEEKSATLG-------EITHQLLKYEECSKQLAQLTQE 867
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 40849888 2416 KVTLVQTLE----IQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQL 2460
Cdd:TIGR00618 868 QAKIIQLSDklngINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
30-137 |
2.33e-07 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 52.70 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 102
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 40849888 103 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 137
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2263-2479 |
2.45e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2263 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2342
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2343 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2422
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 2423 LEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2479
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1412-1700 |
2.62e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 57.27 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1412 QHLRQSsEAEIQAKAQQVEAAERSRMRIEEeiRVVRLqletterqrggaEDELQALRARAEEAEAQKRQAQEEA-----E 1486
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARL------------EREKAAREARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1487 RLRRQVQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEV 1565
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1566 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAeaerareeaerelerwqlkANEALRLRLQAEEVAQQKS 1645
Cdd:PRK05035 574 EVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------------------AVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1646 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1700
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1369-2038 |
2.79e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.12 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1369 AQAKAQAELearelqrrmQEEVTRRE-EAAVDAQ--QQKRSIQEELQHLR-QSSEAEIQAKAQQVEAAERSRMRIEEEIR 1444
Cdd:PRK10246 164 AKPKERAEL---------LEELTGTEiYGQISAMvfEQHKSARTELEKLQaQASGVALLTPEQVQSLTASLQVLTDEEKQ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1445 -VVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAErlrrqvqdesqrKRQAEAELALRVKAEAEAAREKQRA 1523
Cdd:PRK10246 235 lLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKAQ------------PQLAALSLAQPARQLRPHWERIQEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1524 LQALDELKLQAEEAERRLRQAEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLER------TLQEEHVTVTQLRE 1597
Cdd:PRK10246 303 SAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLAEHDRfrqwnnELAGWRAQFSQQTS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1598 EAERRAQQQAEAERAreeaereleRWQLKANEALRLRLQAEEVAQqkslAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1677
Cdd:PRK10246 378 DREQLRQWQQQLTHA---------EQKLNALPAITLTLTADEVAA----ALAQHAEQRPLRQRLVALHGQIVPQQKRLAQ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAE------QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQ------------HEATAATQ-- 1737
Cdd:PRK10246 445 LQVaiqnvtQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-EARIKDLEAQRAQLQagqpcplcgstsHPAVEAYQal 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1738 -------KRQELEAELAK-------VRAEMEVLLASKARAEEESRSTSEKSK------QRLEAEAGRFRELAEEAARLRA 1797
Cdd:PRK10246 524 epgvnqsRLDALEKEVKKlgeegaaLRGQLDALTKQLQRDESEAQSLRQEEQaltqqwQAVCASLNITLQPQDDIQPWLD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1798 LAEEAKRQ-RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEI---ALKEKEAENERL---RRLAEDEAFQRRRLE 1870
Cdd:PRK10246 604 AQEEHERQlRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALagyALTLPQEDEEASwlaTRQQEAQSWQQRQNE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1871 EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLrqrRQVEEEIMALKASF-----------EKAAAGKAELELELGR 1939
Cdd:PRK10246 684 LTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNW---RQVHEQCLSLHSQLqtlqqqdvleaQRLQKAQAQFDTALQA 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1940 IRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE---VERLKAKVEE-ARRLRE 2015
Cdd:PRK10246 761 SVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLtvtVEQIQQELAQlAQQLRE 840
|
730 740
....*....|....*....|...
gi 40849888 2016 RAEQESARQLQLAQEAAQKRLQA 2038
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQ 863
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1362-1574 |
3.14e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1362 RQLAEAHAQAKAQAELEARELQRRMQEEVTRR--EEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAER 1434
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1435 SRMRIEEEIRVVRLQLETTERQRGGAEDE---------LQALRARAEEAEAQKRQAQE-------EAERLRRQVQDESQR 1498
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1499 KRQAEAELALRVKAEAEAAREKQRALQA-LDELKLQAE---EAERRLR--QAEAERARQVQVALETAQRSAEVELQSKRA 1572
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAqLAQLEARLAelpELEAELRrlEREVEVARELYESLLQRLEEARLAEALTVG 386
|
..
gi 40849888 1573 SF 1574
Cdd:COG3206 387 NV 388
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1420-1557 |
3.88e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1420 AEIQAKAQQVEAAersrmrieeeIRVVRLQLETTERQRGgAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--SQ 1497
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGavSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1498 RKRQaEAELALRV-KAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERArQVQVALE 1557
Cdd:COG1566 148 QELD-EARAALDAaQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1634-2069 |
4.72e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1634 RLQAEEVAQQKSLaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQ 1713
Cdd:pfam05557 59 LLEKREAEAEEAL-REQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQIQRAELELQSTNSELEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1714 GEQQRQLLE----------EELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKAraEEESRSTSEKSKQRLEAEAG 1783
Cdd:pfam05557 137 LQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKS--ELARIPELEKELERLREHNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1784 RFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTE----KLAAISEATRLKTEAEIALKEKEAENERLR 1856
Cdd:pfam05557 215 HLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQElqswVKLAQDTGLNLRSPEDLSRRIEQLQQREIV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1857 RLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASESE---LERQKGLVEDTLRQRRQVEEEIMALKA---SFEKAAAGK 1930
Cdd:pfam05557 295 LKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1931 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQR-SLAAEEEAARQRKVALEEVERLKAKVEE 2009
Cdd:pfam05557 373 NYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERElQALRQQESLADPSYSKEEVDSLRRKLET 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 2010 ARRLRER-AEQESARQLQLAQEAAQkrlQAEEKAHAFVVQQREEELQQTLQQEQNMLERLR 2069
Cdd:pfam05557 453 LELERQRlREQKNELEMELERRCLQ---GDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1055-1503 |
4.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1055 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEAQAVPATLQELEvtkaslkKLRAQAEAQQPV 1134
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-------ALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1135 FNTLRDELRGAQEVGERLQqrhgERDVEVERWRERVTQLLERWQAVLAQTDVR-QRELEQLGRQLRYYRESADPLSSWLQ 1213
Cdd:COG4717 148 LEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1214 DAKSRQEQIQAVpiANSQAAREQLRQEK----------ALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLE 1283
Cdd:COG4717 224 ELEEELEQLENE--LEAAALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1284 PVASPAKKPKVQSGSESVIQE------YVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEvEAA 1357
Cdd:COG4717 302 KEAEELQALPALEELEEEELEellaalGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA-EAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1358 LEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRM 1437
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL----EEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1438 RIEEEIRvvrlQLETterqrggaEDELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1503
Cdd:COG4717 457 ELEAELE----QLEE--------DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2260-2621 |
5.08e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2260 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2338
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2339 keqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2418
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2419 LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQqEQILQETQALQKSFLSEKDSLLQRERFI 2498
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2499 EQEKAKLEQLfqdevakaKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAE 2578
Cdd:TIGR02169 395 EKLKREINEL--------KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 40849888 2579 ENQ---RLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDA 2621
Cdd:TIGR02169 467 YEQelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2168-2507 |
5.09e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2168 RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK---AEVTEAARQRSQVEeelfsvRVQmEELGKLKARIEAENRALi 2244
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASdhlNLVQTALRQQEKIE------RYQ-ADLEELEERLEEQNEVV- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2245 lrdkdntqrflEEEAEkmkQVAEEAARLSVAAQEAARLR-QLAEE----DLAQQRALA---EKMLKEKMQAVQEATRLKA 2316
Cdd:PRK04863 372 -----------EEADE---QQEENEARAEAAEEEVDELKsQLADYqqalDVQQTRAIQyqqAVQALERAKQLCGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2317 E------AELLQQQKELAQEQ---ARRL---QEDKEQMAQ--QLV----------EETQGFQRTL-EAERQRQLEMSAEA 2371
Cdd:PRK04863 438 DnaedwlEEFQAKEQEATEELlslEQKLsvaQAAHSQFEQayQLVrkiagevsrsEAWDVARELLrRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2372 ERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEK 2450
Cdd:PRK04863 518 LRMRLSELEQRlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 2451 LKQEA--------KLLQLKS---EEMQTVQQ-EQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ 2507
Cdd:PRK04863 598 LAARApawlaaqdALARLREqsgEEFEDSQDvTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1666-1875 |
5.28e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1666 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheataATQKRQEL 1742
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1743 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakRQRQLAEEDAARQRAEAER 1822
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAERAEAEKQR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1823 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 1875
Cdd:pfam15709 454 QKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1679-1894 |
5.33e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1679 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1758
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1759 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK 1827
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1828 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE 1894
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1334-1744 |
5.78e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1334 EEEERLAEQQRaeeRERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRM--------------QEEVTRREEAAVD 1399
Cdd:PRK04863 836 EAELRQLNRRR---VELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNlladetladrveeiREQLDEAEEAKRF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1400 AQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE----RSRMRIE--EEIRVVRLQLETTERQR-GGAEDELQ-ALRA 1469
Cdd:PRK04863 913 VQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQ 992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1470 RAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalrvKAEAEAAREK-QRALQALDELKLQA-EEAERRLRQAEAE 1547
Cdd:PRK04863 993 RLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDE 1064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1548 ------RARQVQVALETAQRSAEVELQS--KRASFAEKTAQLERTLQEEHVTVTQ--LREEAERRAQQQAEAERAREEAE 1617
Cdd:PRK04863 1065 lharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYHEMREQVVNAKAGWCavLRLVKDNGVERRLHRRELAYLSA 1144
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1618 RELERWQLKANEALRLrlqaeevaqqkslAQADAEKqkEEAEREARRRGKAEEQAVRQRELAEQEL-EKQRQLAEGTAQQ 1696
Cdd:PRK04863 1145 DELRSMSDKALGALRL-------------AVADNEH--LRDVLRLSEDPKRPERKVQFYIAVYQHLrERIRQDIIRTDDP 1209
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1697 RLAAEQ---ELIRLRAETEQGEQQRQLLEEELA-----RLQHEATAATQKRQELEA 1744
Cdd:PRK04863 1210 VEAIEQmeiELSRLTEELTSREQKLAISSESVAniirkTIQREQNRIRMLNQGLQN 1265
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1323-1563 |
6.98e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1323 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQ 1402
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1403 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAE----EAEAQK 1478
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1479 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALET 1558
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 40849888 1559 AQRSA 1563
Cdd:COG3883 258 AAGSA 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1143-1568 |
7.01e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1143 RGAQEvgERLQQRHGERDVEVERW--RERVTQLLERWQ-----------AVLAQTDVRQrELEQLGRQLRY-YRESADpl 1208
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYatLSFDVQKLQRLHqafsrfigshlAVAFEADPEA-ELRQLNRRRVElERALAD-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1209 sswlQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEiERHGEKVEECQ---KFAKQYINAIKDYELQLitykAQLEPV 1285
Cdd:PRK04863 856 ----HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD-ETLADRVEEIReqlDEAEEAKRFVQQHGNAL----AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1286 AS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereRLAEVEAALE 1359
Cdd:PRK04863 927 VSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1360 KQRqlaEAHAQAKAQAElEARELQRRMQEEVTRreeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKAQqveaaersRM 1437
Cdd:PRK04863 1003 RAR---EQLRQAQAQLA-QYNQVLASLKSSYDA-------KRQMLQELKQELQDLgvPADSGAEERARAR--------RD 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1438 RIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEAELALRV 1510
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRLHRRELAYLS 1143
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1511 KAEAEAAREKqrALQALdelklqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1568
Cdd:PRK04863 1144 ADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3710-3745 |
7.10e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.10e-07
10 20 30
....*....|....*....|....*....|....*.
gi 40849888 3710 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3745
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3451-3487 |
7.24e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.24e-07
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3451 IRLLEAQIATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3487
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2153-2506 |
7.28e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.00 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2153 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2221
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2222 VRvqmeeLGKLKARIeaeNRALILRDKDNTQRFLEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRaLAEKM 2300
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2301 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLE 2366
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2367 MSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDQDAERLR 2438
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2439 EAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLE 2506
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARR 742
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2156-2459 |
7.51e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2156 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKAR 2235
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2236 IEAENRAL------ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2307
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2308 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaerqrqlemsaeaeRLKLRMAEMSRAQAR 2387
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2388 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2459
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1706-2322 |
7.97e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1706 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1785
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1786 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 1859
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1860 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 1933
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1934 ELELGRIRSNAEDtmrskelaeqeaARQRqlaaeeeqrrreaeervQRSLAAEEEAARQRkvaleeverlkakVEEARRL 2013
Cdd:PRK02224 411 EDFLEELREERDE------------LRER-----------------EAELEATLRTARER-------------VEEAEAL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2014 RERAEQESARQlqlaqeaaqkrlQAEEKAHAFVVQQREEELQQtlqqeqnmLERLRSEAEAARRAAEEAEEAREQAEREA 2093
Cdd:PRK02224 449 LEAGKCPECGQ------------PVEGSPHVETIEEDRERVEE--------LEAELEDLEEEVEEVEERLERAEDLVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2094 AQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFaEQTLRQKAQV 2173
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL-NSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2174 EQELTTLRLQLEETDHqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGklkARIEAENRALILRDKDNTQR 2253
Cdd:PRK02224 588 IESLERIRTLLAAIAD----AEDEIERLREKREALAELNDERRERLAEKRERKRELE---AEFDEARIEEAREDKERAEE 660
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2254 FLEEEAEKMKQVAEEAARLSVAA----QEAARLRQLAEEdlaqQRALAEKmlKEKMQAVQEatrlkaEAELLQ 2322
Cdd:PRK02224 661 YLEQVEEKLDELREERDDLQAEIgaveNELEELEELRER----REALENR--VEALEALYD------EAEELE 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1670-2363 |
8.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1670 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1749
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1750 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA 1829
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1830 AISEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKAseseLERQKGLVEDTLRqr 1909
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDA----LAEALGLDEAELP-- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1910 rqVEEEIMALKASFEK--AAAgkaelELELGRIRSN----AEDTMRSKELAEQEAARQRqlaaeeeqrrreaeervQRSL 1983
Cdd:COG4913 462 --FVGELIEVRPEEERwrGAI-----ERVLGGFALTllvpPEHYAAALRWVNRLHLRGR-----------------LVYE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1984 AAEEEAARQRKVALEE---VERLKAKVEEARR-LRERAEQ-------ESARQLQLAQEAAQKRLQAEEKAHAFVVQQREE 2052
Cdd:COG4913 518 RVRTGLPDPERPRLDPdslAGKLDFKPHPFRAwLEAELGRrfdyvcvDSPEELRRHPRAITRAGQVKGNGTRHEKDDRRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2053 ELQQTLQQEQNM--LERLRseaeaarraaeeaeeareqaereaaqsrkqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKE 2130
Cdd:COG4913 598 IRSRYVLGFDNRakLAALE-------------------------------AELAELEEELAEAEERLEALEAELDALQER 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2131 AEQEAArraqaeqaaLKQKQAADAEMEkhkkfaeQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAAR 2210
Cdd:COG4913 647 REALQR---------LAEYSWDEIDVA-------SAEREIAELEAELE----RLDASSDDLAALEEQLEELEAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2211 QRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEAARLSVAAQEAARLRQLAEEDL 2290
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA---AALGDAVERELRENLEERIDALRARLN 783
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2291 AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ-QKELAQEQARRLQEDKEQMAQQLVEETQ----GFQRTLEAERQR 2363
Cdd:COG4913 784 RAEEELERAMRAFNREWPAETADLDADLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIefvaDLLSKLRRAIRE 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2208-2456 |
8.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2208 AARQRSQVEEELFSVRVQMEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAE 2287
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2288 EDLAQQRALaekmLKEKMQAVQEATRLKAEAELLQQQKELaqeQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEM 2367
Cdd:COG4942 97 AELEAQKEE----LAELLRALYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2368 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDQDAERLREAIAELERE 2447
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKEL--------------AELAAELAELQQEAEELEALIARLEAE 235
|
....*....
gi 40849888 2448 KEKLKQEAK 2456
Cdd:COG4942 236 AAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1462-2016 |
8.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1462 DELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqraLQALDELKLQAEEAERRL 1541
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE---KLEKE--------VKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1542 RQAEAERArqvqvALETAQRsaevELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaerareeaereLE 1621
Cdd:PRK03918 248 ESLEGSKR-----KLEEKIR----ELEERIEELKKEIEELEEKVKE--------------------------------LK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GT 1693
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1694 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR--LQHEATAATQKRQELEAELAKVRAEMEVLLASKARA-------E 1764
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1765 EESR-----------STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAE 1819
Cdd:PRK03918 447 EEHRkelleeytaelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1820 AERVLTEKLAAISEATRLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA------ 1890
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneyle 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1891 ---SESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAaagKAELElELGRIRSNAEDTMRSKELAEQEAARQRqlAAE 1967
Cdd:PRK03918 607 lkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYSEEEYEELREEYLELSRELAG--LRA 680
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 40849888 1968 EEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRER 2016
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1770-2213 |
9.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1770 TSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1848
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1849 EAENERLRRLAEDEAFQRRRLEEQaaqhKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAA 1928
Cdd:COG4717 145 PERLEELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1929 GKAELELELGRIRSNAEDTMRSKELAEQEAArQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-- 2006
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2007 -VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEA 2085
Cdd:COG4717 300 lGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2086 REQAEREAAQSRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQAALKQK-QAADAEMEKHKKFAE 2164
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKE----------ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 40849888 2165 QTLRQKAQVEQELTTLrlqleETDHQKSILDEELQRLKAEVTEAARQRS 2213
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4132-4160 |
9.45e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.45e-07
10 20
....*....|....*....|....*....
gi 40849888 4132 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4160
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1336-1713 |
1.05e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1336 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrREEAAVDAQQQKRSIQEELQHLR 1415
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE----LKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1416 QSSEAEIQAKAQQVEAAERSRMRIEE-EIRVVRLQLETTERqrggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1494
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1495 ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKRA 1572
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1573 SFAEKTAQLERTLQEEH---VTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrLRLQAEEVAQQKSLAQA 1649
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-EKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1650 DAEKQKEEAEREARRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1713
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRREL--QELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1356-1526 |
1.09e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1356 AALEKQRQLAEAHAQAKAQAELEARelQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLR---QSSEAEIQAKAQQVEAA 1432
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKTELEDLEkeiKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1433 ERSRMRI--EEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrv 1510
Cdd:COG1579 79 EEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL---- 154
|
170
....*....|....*.
gi 40849888 1511 KAEAEAAREKQRALQA 1526
Cdd:COG1579 155 EAELEELEAEREELAA 170
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
21-143 |
1.10e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 51.21 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 21 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMR 87
Cdd:cd21325 15 EGTQHSYSEE----EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTP 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 88 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 143
Cdd:cd21325 91 FIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1146-1551 |
1.18e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1146 QEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSrqeqiqav 1225
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN-------- 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1226 piansqaareQLRQEKALLEEIERHGEKVEECQK---FAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVI 1302
Cdd:TIGR00606 766 ----------DIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQA---E 1376
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQLVELSTEVQsLIREIKDAKEQDsplE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1377 LEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHL------------------RQSSEAEIQAKAQQVEAAERSRMR 1438
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKHQEK 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1439 IEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeAAR 1518
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKR 1068
|
410 420 430
....*....|....*....|....*....|...
gi 40849888 1519 EKQRALQALDELKLQAEEAERRLRQAEAERARQ 1551
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1384-1565 |
1.21e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.49 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1384 RRMQEEVTRREEAAVDAQQQKRSIQEElQHLRQSSEAEIQAkaqqveaaersrmriEEEIRVVRLQLETTERQRGGAEDE 1463
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIA-QANREAEEAELEQ---------------EREIETARIAEAEAELAKKKAEER 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1464 LQALRARAEeAEAQKRQAQEEAERLRRQ------------VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELK 1531
Cdd:COG2268 255 REAETARAE-AEAAYEIAEANAEREVQRqleiaerereieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIR 333
|
170 180 190
....*....|....*....|....*....|....*.
gi 40849888 1532 LQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1565
Cdd:COG2268 334 AKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
21-142 |
1.36e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 50.81 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 21 EEVREKYKDErdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMR 87
Cdd:cd21323 15 EGTQHSYSEE----EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTP 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 88 FHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 142
Cdd:cd21323 91 FTISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1361-1489 |
1.53e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 53.51 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1361 QRQLAEAHAQ-AKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSRMRI 1439
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 40849888 1440 EEEIRVVRLQLETTERQRGGAEdELQALRARAEEAEAQKRQAQEEAERLR 1489
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2792-2828 |
1.73e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.73e-06
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 2792 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFDEEM 2828
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1309-1428 |
1.75e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 52.68 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1309 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELearelqR 1384
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 40849888 1385 RMQEEVTRREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKAQQ 1428
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1757-2558 |
1.77e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1757 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATR 1836
Cdd:TIGR00618 50 LYGKLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1837 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ----HKADIEERLAQLRKASESELERQKGLVEDTLRQRRQ- 1911
Cdd:TIGR00618 130 EVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELlmnlFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLc 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1912 VEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAaEEEAAR 1991
Cdd:TIGR00618 210 TPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEET-QERINR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1992 QRKVA-----LEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLE 2066
Cdd:TIGR00618 289 ARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2067 RLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2146
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAIT 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEmEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARqrsqveeELFSVRVQM 2226
Cdd:TIGR00618 449 CTAQCEKLE-KIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI-------HPNPARQDI 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EELGKLKARIEA-ENRALILRDK-DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEk 2304
Cdd:TIGR00618 521 DNPGPLTRRMQRgEQTYAQLETSeEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2305 MQAVQEATRLKAEA---ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQlemsaEAERLKLRMAEM 2381
Cdd:TIGR00618 600 TEKLSEAEDMLACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE-----HALSIRVLPKEL 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2382 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQdaeRLREAIAELEREKEKLKQEAKLLQlk 2461
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN---ASSSLGSDLAAREDALNQSLKELM-- 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2462 sEEMQTVQQEQILQETQALQKSFLSEKdsLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQmeqEKQELVASM 2541
Cdd:TIGR00618 750 -HQARTVLKARTEAHFNNNEEVTAALQ--TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS---DEDILNLQC 823
|
810
....*....|....*..
gi 40849888 2542 EEARRRQREAEEGVRRK 2558
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEK 840
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2163-2597 |
1.81e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2163 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELfSVRVQMEELGKLKARIEAENRA 2242
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2243 LI-LRDKDNTQRFLEEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2321
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2322 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2400
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2401 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqQEQILQETQAL 2480
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2481 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQD-----EVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGV 2555
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEEllgelEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 40849888 2556 RRkQEELQRLEQQRqqqekllaEENQRLRERLQRLEEEHRAA 2597
Cdd:COG4717 463 EQ-LEEDGELAELL--------QELEELKAELRELAEEWAAL 495
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1726-2456 |
1.97e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 54.34 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1726 ARLQHEATAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1802
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1803 KRQRQLAEEDAAR---QRAEAERVLTEKLAAISEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 1876
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1877 KADIEERLAQLRKASESELERQKGL---VEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKEL 1953
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1954 AEQEaarqrqlAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2033
Cdd:pfam05483 315 LEED-------LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2034 KRLQAEEKAHAFVVQQREEelqqtlqqeqnmLERLRSEAEAARRAAEEaeeareqaereaaqsRKQVEE-AERLKQSAEE 2112
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVE------------LEELKKILAEDEKLLDE---------------KKQFEKiAEELKGKEQE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2113 QAQAQAQAQAAAEKLRkeaeQEAARRAQAEQAALKQKQAADAEMEKHK-KFAEQT------LRQKAQVEQELTTLRLQLE 2185
Cdd:pfam05483 441 LIFLLQAREKEIHDLE----IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTahcdklLLENKELTQEASDMTLELK 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2186 etDHQKSILDEELQ--RLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkarieaENRALILRDKDNTQRFLEEEAEKMK 2263
Cdd:pfam05483 517 --KHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFIQKGD-------EVKCKLDKSEENARSIEYEVLKKEK 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2264 QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ---EATRLKAEAELLQQQKELAQEQARRLQEDKE 2340
Cdd:pfam05483 588 QMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQKEIEDKK 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2341 QMAQQLVEETQGFQRTLEAERQRQLEMSaeaERLKLRMAEMSraqARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2420
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMV---ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK 741
|
730 740 750
....*....|....*....|....*....|....*.
gi 40849888 2421 QTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2456
Cdd:pfam05483 742 AALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1292-1485 |
2.14e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1292 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1371
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1372 KAQAELEAR--ELQRRMQEEVTRREE---AAVDAQQQKRS----IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1442
Cdd:COG3206 263 PVIQQLRAQlaELEAELAELSARYTPnhpDVIALRAQIAAlraqLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 40849888 1443 IRV---VRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEA 1485
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1335-1530 |
2.14e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.66 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1335 EEERLAEQQR--AEERERLAEVE----------AALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAvdaqq 1402
Cdd:PRK09510 93 QQKQAAEQERlkQLEKERLAAQEqkkqaeeaakQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1403 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAErsrmrieeeirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQ 1482
Cdd:PRK09510 168 KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAE--------------------AKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 40849888 1483 EEAErlrrqvqdesqRKRQAEAELALRVKAEAEAAREKQRAlqALDEL 1530
Cdd:PRK09510 228 AKAA-----------AEAKAAAEKAAAAKAAEKAAAAKAAA--EVDDL 262
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1471-1587 |
2.48e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1471 AEEAEAQKRQAQEEAErLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALdELKLQAEEAErrlrqaeaeraR 1550
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARAEAEA-AYEIAEANAE-----------R 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 1551 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1587
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3915-3952 |
2.49e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.49e-06
10 20 30
....*....|....*....|....*....|....*...
gi 40849888 3915 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3952
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1564-2398 |
3.05e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1564 EVELQSKRASFAEKTAQ-LERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELerwQLKANEALRLRLQAEEVAQ 1642
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEhIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDL---QTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1643 QKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQqrlaaeqELIRLRAETEQGEQQRQLLE 1722
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1723 EELARLQHEA--TAATQKRQELEAELA-------KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEA 1792
Cdd:pfam15921 208 DSMSTMHFRSlgSAISKILRELDTEISylkgrifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1793 ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1872
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1873 AAQHKADIEERLAQL-----RKASESELERQK-----------GLVEDTLRqrRQVEEEIMALKasfekaaagkaELELE 1936
Cdd:pfam15921 368 FSQESGNLDDQLQKLladlhKREKELSLEKEQnkrlwdrdtgnSITIDHLR--RELDDRNMEVQ-----------RLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1937 LGRIRSNAEDTMRSKELAEQeaARQRQLAAEEEQRRREAEERVQRSLAAEEEAARqrKVALEEVERLKAKVEEARRLRER 2016
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQ--GKNESLEKVSSLTAQLESTKEMLRKVVEELTAK--KMTLESSERTVSDLTASLQEKER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2017 AEQESARQLQLAQEAAQKRLQ-----AEEKAHAFVVQQREEELQQTLQQEQNMLERLRseaeaarraaeeaeeareqaer 2091
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQelqhlKNEGDHLRNVQTECEALKLQMAEKDKVIEILR---------------------- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2092 eaaqsrKQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkqkqaadaeMEKHKKFAEQTLRQKA 2171
Cdd:pfam15921 569 ------QQIENMTQL-------------------------------------------------VGQHGRTAGAMQVEKA 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2172 QVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----EEELFSVRVQMEELGKLKARIE---------A 2238
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrnelnslS 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2239 ENRALILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK----MLKEKMQAV 2308
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQFL 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2309 QEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLvEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQAR 2387
Cdd:pfam15921 754 EEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQR 829
|
890
....*....|.
gi 40849888 2388 AEEDAQRFRKQ 2398
Cdd:pfam15921 830 QEQESVRLKLQ 840
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1715-1906 |
3.20e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1715 EQQRQLLEEELAR-LQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFR----ELA 1789
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1790 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1868
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 40849888 1869 LEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 1906
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1667-2040 |
3.22e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.33 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1746
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1747 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1824
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1825 TEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRRLEEQAAQhkadieerlaqlrkASESELERQKGLVED 1904
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKSQ--------------NGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1905 TLRQRRQVEEEimalkasfEKAAAGKAELELELGRIR-SNAEdtmrsKELAEQEAARQRQLAAEEEQRRREAEERVQRSL 1983
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1984 AAEEEaaRQRKValEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2040
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1410-1577 |
3.34e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlqlETTERQRGGAEDELQALRARAEEAEAQKRQA--QEEAER 1487
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1488 LRRQVqdESQRKRQAEAELALRvkaEAEAAREKQRAlqALDELKLQAEEAERRLRQAEAERARQVQvaletAQRSAEVEL 1567
Cdd:COG1579 94 LQKEI--ESLKRRISDLEDEIL---ELMERIEELEE--ELAELEAELAELEAELEEKKAELDEELA-----ELEAELEEL 161
|
170
....*....|
gi 40849888 1568 QSKRASFAEK 1577
Cdd:COG1579 162 EAEREELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1138-1587 |
3.48e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1138 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKS 1217
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1218 RQEQIQAVpiansQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAkkpkvqsg 1297
Cdd:COG4717 127 LLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1298 SESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEE-ERLAEQQRAEERERLAEVEAAL----------EKQRQ 1363
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEEleeAQEELEELEEELEQLENElEAAALEERLKEARLLLLIAAALlallglggslLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1364 LAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQS-------SEAEIQAKAQQVEAAERSR 1436
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1437 MRIEEEIRVVRLQLETTERQ----RGGAEDElQALRARAEEAEaQKRQAQEEAERLRRQVQDEsqrkrqAEAELALRVKA 1512
Cdd:COG4717 354 REAEELEEELQLEELEQEIAallaEAGVEDE-EELRAALEQAE-EYQELKEELEELEEQLEEL------LGELEELLEAL 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1513 EAEAAREKqralqaLDELKLQAEEAERRLRQAEAERARqvqVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1587
Cdd:COG4717 426 DEEELEEE------LEELEEELEELEEELEELREELAE---LEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1369-1583 |
3.63e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1369 AQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAqqveaAERSRMRIEEEIRvvrl 1448
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1449 qletterqrggaedelQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALD 1528
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1529 ELKLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1583
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3120-3156 |
3.76e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.76e-06
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3120 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3156
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1091-1807 |
3.76e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1091 EEVLKTHEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAqqpvfntLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1169
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1170 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESadplsswlqdaksrqeqiQAVPIANSQAAREQLR-QEKALLEEIE 1248
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAG------------------EAKQLAEAQKEAELLRkQLSKTQEELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1249 RHGEKVEECQKFAKQYInaikdyelqlitykaqLEPVASPAKKPKVQSGSESViQEYVDLRTRYSELTTLTSQYIKFISE 1328
Cdd:pfam07111 215 AQVTLVESLRKYVGEQV----------------PPEVHSQTWELERQELLDTM-QHLQEDRADLQATVELLQVRVQSLTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1329 TLRRMEEE-ERLAEQQRAEERERLAEVEAALEKQRQLAEA-HAQAKAQaELEARELQRRMQEEVTRREEAAVDAQQQKRS 1406
Cdd:pfam07111 278 MLALQEEElTRKIQPSDSLEPEFPKKCRSLLNRWREKVFAlMVQLKAQ-DLEHRDSVKQLRGQVAELQEQVTSQSQEQAI 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1407 IQEELQHLRQSSEAE-IQAKAQQVE--AAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1483
Cdd:pfam07111 357 LQRALQDKAAEVEVErMSAKGLQMElsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1484 EAERLRR----------------QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldELKLQA----EEAERRLRQ 1543
Cdd:pfam07111 437 RLSYAVRkvhtikglmarkvalaQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA--ELQLSAhliqQEVGRAREQ 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1544 AEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerareeaerelerw 1623
Cdd:pfam07111 515 GEAERQQLSEVAQQLEQ-----ELQRAQESLASVGQQLEVARQGQ----------------------------------- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1624 QLKANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQE 1703
Cdd:pfam07111 555 QESTEEAASLR--QELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK-ERNQE 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1704 LIRLRAETEQGEQQR-----QLLEEE----LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----S 1769
Cdd:pfam07111 632 LRRLQDEARKEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavP 711
|
730 740 750
....*....|....*....|....*....|....*...
gi 40849888 1770 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1807
Cdd:pfam07111 712 TRESIKGSLTVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2148-2333 |
4.38e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2148 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQME 2227
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2228 ELGKLKARIEaenRAL-ILRDKDNT----QRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2299
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 40849888 2300 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2333
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1351-1763 |
4.85e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 53.32 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1351 LAEVEAALEKQRQLAEAHAQAKaqaelEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1419
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1420 --------AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQ 1491
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1492 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1571
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1572 ASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADA 1651
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1652 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1731
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 40849888 1732 ATAATQKRQELEAELAKVRAEMEVLLASKARA 1763
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1327-1577 |
5.20e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1327 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA-------KAQAELEARELQRRMQEEVTRREEAAVD 1399
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEkesvaerKENNEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1400 AQQQK-RSIQEELQH---LRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLET----------------TERQRGG 1459
Cdd:pfam02029 132 ETEIReKEYQENKWStevRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKkvkyeskvfldqkrghPEVKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1460 AEDELQALRARAEEAEAQKRQAQ----EEAERLRRQVQDESQRKRQAEAElalrvKAEAEAAREKQR-ALQALDELKLQA 1534
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQereeEAEVFLEAEQKLEELRRRRQEKE-----SEEFEKLRQKQQeAELELEELKKKR 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 40849888 1535 -------EEAERRLRQAEAERarqvQVALETAQRSAEVELQSKRASFAEK 1577
Cdd:pfam02029 287 eerrkllEEEEQRRKQEEAER----KLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1347-1910 |
5.30e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.72 E-value: 5.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1347 ERERLAEVEAALEKQ-----RQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRsiQEELQHLRQ----- 1416
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeyKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ--DSELAKLRVeemeq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1417 --SSEAEIQAKAQqVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQd 1494
Cdd:pfam05701 113 giADEASVAAKAQ-LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1495 esqrkrQAEAELALRVKAEAEAAREKQRALQALDELKL-------QAEEAERRLRQaEAERARQVQVALETAqrsaEVEL 1567
Cdd:pfam05701 191 ------ATKESLESAHAAHLEAEEHRIGAALAREQDKLnwekelkQAEEELQRLNQ-QLLSAKDLKSKLETA----SALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1568 QSKRASFAektAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRLRLQAEevaqqkSLa 1647
Cdd:pfam05701 260 LDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAA------SL- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1648 QADAEKQKeeaerearrrgkAEEQAVRQRELA--------EQELEKQRQLAEgTAQQRLAAEQE--------LIRLRAET 1711
Cdd:pfam05701 327 RSELEKEK------------AELASLRQREGMasiavsslEAELNRTKSEIA-LVQAKEKEAREkmvelpkqLQQAAQEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1712 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK------ARAEEESRSTSEKSKQrlEAEAGRF 1785
Cdd:pfam05701 394 EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEklalaaIKALQESESSAESTNQ--EDSPRGV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1786 RELAEEAARLRALAEEakrqrqlAEEDAARQRAEAervltekLAAISEAtrlkteaeialkeKEAENERLRRLAEdeafq 1865
Cdd:pfam05701 472 TLSLEEYYELSKRAHE-------AEELANKRVAEA-------VSQIEEA-------------KESELRSLEKLEE----- 519
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 40849888 1866 rrrLEEQAAQHKADIEERLAQLRKASESELErqkglVEDTLRQRR 1910
Cdd:pfam05701 520 ---VNREMEERKEALKIALEKAEKAKEGKLA-----AEQELRKWR 556
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1449-1855 |
5.33e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1449 QLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALD 1528
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1529 ELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1608
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1609 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1688
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1689 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1768
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1769 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1848
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 40849888 1849 EAENERL 1855
Cdd:COG5278 511 AAAEAAL 517
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2165-2558 |
5.98e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2165 QTLRQKAQVE------QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS----QVEEELFSVRVQMEELGKLKA 2234
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaSLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2235 RIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedLAQQRALAEKMLKEKMQAVQEAT 2312
Cdd:pfam15921 525 RVDLKLQELQhLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEIN 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2313 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDA 2392
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2393 QRFRKQAEEIgeklhrtELATQEkvtlvqtLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlkseEMQTVQQEQ 2472
Cdd:pfam15921 681 RNFRNKSEEM-------ETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ----KQITAKRGQ 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2473 IlqetQALQK--SFLSEKDSLLQRER-FIEQEKAKLEQLFQdEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRR-- 2547
Cdd:pfam15921 743 I----DALQSkiQFLEEAMTNANKEKhFLKEEKNKLSQELS-TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKas 817
|
410 420
....*....|....*....|.
gi 40849888 2548 ----------QREAEEGVRRK 2558
Cdd:pfam15921 818 lqfaecqdiiQRQEQESVRLK 838
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1669-1894 |
6.66e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1669 EEQAVRQRELAEQELEK-QRQLAEgtAQQRL-AAEQELIRLRAETE--QGEQQRQLLEEELARLQHEATAATQKRQELEA 1744
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPE--LRKELeEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1745 ELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1824
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1825 TEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESE 1894
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
608-700 |
6.75e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 608 HGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQA 687
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 40849888 688 ALQTQWSWMLQLC 700
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2199-2483 |
6.82e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 52.34 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2199 QRLKAEVTEAARQRSQVEEELFSVRVQmeelgKLKARIEAENRALILRDKDNTQRFLEEEAE--KMKQVAEEAARLSVAA 2276
Cdd:pfam05667 220 QEWEEEWNSQGLASRLTPEEYRKRKRT-----KLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSSTTDTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2277 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQ 2354
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2355 RTLEAERQRQLEMSAEAE--RLKLRMAE--------MSRAQARAEEDAQRFRKQAEEIGEklHRT--------------- 2409
Cdd:pfam05667 367 QVEEELEELKEQNEELEKqyKVKKKTLDllpdaeenIAKLQALVDASAQRLVELAGQWEK--HRVplieeyralkeaksn 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2410 -ELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEA-------KLLQL-KSEEMQTVQQEQILQETQAL 2480
Cdd:pfam05667 445 kEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrsaytrRILEIvKNIKKQKEEITKILSDTKSL 524
|
...
gi 40849888 2481 QKS 2483
Cdd:pfam05667 525 QKE 527
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1391-1534 |
7.05e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.59 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1391 TRREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKAQQVEAAERSRMRIEEEI-RVVRLQletteRQRGGAEDELQA 1466
Cdd:COG1566 78 PTDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDE 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1467 LRARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKqrALQALDELKLQA 1534
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQ--AELNLARTTIRA 212
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1429-1554 |
7.20e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1429 VEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRAR--------AEEAEAQKRQAQEEAERLRRQVQDEsqrkr 1500
Cdd:COG1193 520 IEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEkeeilekaREEAEEILREARKEAEELIRELREA----- 594
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1501 qaeaelalrvKAEAEAAREKQRALQALDElKLQAEEAERRLRQAEAERARQVQV 1554
Cdd:COG1193 595 ----------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAKPAKPPEELKV 637
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1351-1445 |
7.24e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.65 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1351 LAEVEAALEKQRQLAEAHAQAKAQAELEARelqrRMQEEVTRREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKAQQV 1429
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAE----AQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 40849888 1430 EAAERSRMRI---EEEIRV 1445
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
145-252 |
7.53e-06 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 47.88 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 145 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 223
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 40849888 224 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 252
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1710-2040 |
7.78e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1710 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRleaeagrfrela 1789
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKR------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1790 eEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATR-LKTEAEIALKEKEAENERLRRLAEDEAFQRRR 1868
Cdd:pfam02029 72 -EERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKeEKRDSRLGRYKEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1869 LEEQAAQHKADIEERLAQLRKASESELErqkgLVEDTLRQRRQVEEE---IMALKASFEKAAAGKAELELELGRIRSNAE 1945
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEE----VKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1946 DTMRSkELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALeEVERLKAKVEEARRLRERAEQ--ESAR 2023
Cdd:pfam02029 227 QGGLS-QSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAEL-ELEELKKKREERRKLLEEEEQrrKQEE 304
|
330
....*....|....*..
gi 40849888 2024 QLQLAQEAAQKRLQAEE 2040
Cdd:pfam02029 305 AERKLREEEEKRRMKEE 321
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1341-1523 |
9.86e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.31 E-value: 9.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1341 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRrmqeEVTRREEAAVDAQQQKRSIQEELQHLRqsSEA 1420
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1421 EIQAKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1500
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 40849888 1501 QAEAELALRVKAEAEAAREKQRA 1523
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1258-1589 |
9.93e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1258 QKFAKQYINAIKDYelqlitYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1336
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1337 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR----------ELQRRMQE-EVTRREEAAVDAQQQKR 1405
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 SIQEELQHLRQSSEAEiQAKAQQVEAAERSRMRIEEE---IRVVRLQLETTERQRGGAEDELQALRARAEEAE-AQKRQA 1481
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEakrRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEpATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1482 QEEAERLRRQVQDE-------SQRKRQAEAElalRVKAEAEAAREKQR-------ALQALDELKLQAEEAERRLRQAEA- 1546
Cdd:NF033838 280 ENDAKSSDSSVGEEtlpspslKPEKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKVKEAELe 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 40849888 1547 ---ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1589
Cdd:NF033838 357 lvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1326-1531 |
1.05e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1326 ISETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeahAQAKAQAELEARELqRRMQEEVTRREEAAVDAQQQKR 1405
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 siqeelQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKR------ 1479
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1480 -----QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALDELK 1531
Cdd:COG1842 157 gidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2252-2482 |
1.05e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2252 QRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2331
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2332 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2411
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2412 ATQEKvtlvqtleIQRQQSDQDAERLREAIAELER-EKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2482
Cdd:pfam13868 191 AQQEK--------AQDEKAERDELRAKLYQEEQERkERQKEREEAEKKARQRQELQQAREEQIELKERRLAE 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1341-1738 |
1.08e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1341 EQQRAEERERLAEVEAALEKQR----QLAEAHAQAKAQAELEARELQRRM-------QEEVTRREEAAVDAQQQKRSIQE 1409
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQLLNKLLPQANlladetlADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ELQHLR---------QSSEAEIQAKAQQVEAAERSRMRIEEEI--------RVVRLQLETTERQRGGAEDELQALRARAE 1472
Cdd:COG3096 915 HGKALAqleplvavlQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsevvqRRPHFSYEDAVGLLGENSDLNEKLRARLE 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1473 EAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAEL-----ALRVKAEAEAArekQRALQALDELKLQAEEA 1537
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVlaslkssrdaKQQTLQELeqeleELGVQADAEAE---ERARIRRDELHEELSQN 1071
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1538 ERRLRQAEAERARQvqvaletaqrSAEVELQSKRASFAEKTAQLERTLQEEHVtvtqlreeaerraqqqaeaerareeae 1617
Cdd:COG3096 1072 RSRRSQLEKQLTRC----------EAEMDSLQKRLRKAERDYKQEREQVVQAK--------------------------- 1114
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1618 relERW----QLKANEALRLRLQAEEVAQQkslaqaDAEKQKEEAerearrrgkaeEQAVRQRELAEQELEKQRQLAEGT 1693
Cdd:COG3096 1115 ---AGWcavlRLARDNDVERRLHRRELAYL------SADELRSMS-----------DKALGALRLAVADNEHLRDALRLS 1174
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1694 AQQR---------LAAEQEL-IRLRAETEQGEQQRQLLEE---ELARLQHEATAATQK 1738
Cdd:COG3096 1175 EDPRrperkvqfyIAVYQHLrERIRQDIIRTDDPVEAIEQmeiELARLTEELTSREQK 1232
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1459-1738 |
1.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1459 GAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAE 1538
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1539 RRLRQAEAERARQVQVALETAQRSA-EVELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerraqqqaeaerareeae 1617
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPA----------------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1618 relerwqlkanealrLRLQAEEVAQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaqqr 1697
Cdd:COG4942 148 ---------------RREQAEELRADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR------ 203
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 40849888 1698 laAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1738
Cdd:COG4942 204 --LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1699-1794 |
1.09e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.88 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1699 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1778
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 40849888 1779 EAEAGRFrELAEEAAR 1794
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3917-3955 |
1.13e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.13e-05
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3917 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3955
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1705-1946 |
1.19e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.49 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1705 IRLRA-ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1777
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAervlteKLAAISEATRLKTEAEIALKEKEAenerlrr 1857
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKA------KKAAQQAANAEAEEEVDPKKAAVA------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1858 lAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAS-ESELER---QKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAEL 1933
Cdd:PRK05035 584 -AAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAvAAAIARakaKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQ 662
|
250
....*....|...
gi 40849888 1934 ELELGRIRSNAED 1946
Cdd:PRK05035 663 QQANAEPEEAEDP 675
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1474-1684 |
1.23e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1474 AEAQKRQAQEEAERLRRQVQDESQRKRQAEaELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1553
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1554 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEaerelerwqlKANEALRL 1633
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA----------KKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1634 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1684
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
26-131 |
1.25e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 47.65 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 26 KYKDERDRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYL 101
Cdd:cd21285 2 KSWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFL 81
|
90 100 110
....*....|....*....|....*....|
gi 40849888 102 RHRQVKLVNIRNDDIADGNPKLTLGLIWTI 131
Cdd:cd21285 82 AAKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1401-1547 |
1.29e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1401 QQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAED--ELQALRARAEEAE 1475
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1476 AQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAE 1547
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2157-2633 |
1.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2157 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL-G 2230
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2231 KLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA 2307
Cdd:COG4913 338 DRLEQLEREIERLerELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2308 VQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM---------------------------AQQLVEETQG 2352
Cdd:COG4913 418 RRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervlggfALTLLVPPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2353 FQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQS-- 2430
Cdd:COG4913 498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-ELGRRFDYVCVDSPEELRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2431 -----------------DQDAERL--------REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKS 2483
Cdd:COG4913 577 itragqvkgngtrhekdDRRRIRSryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2484 FLSEKDsLLQRERFIEQEKAKLEQL--FQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEE 2561
Cdd:COG4913 657 SWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2562 LQRLEQQRQQQEKLLAEE----------NQRLRERLQ-RLEEEHRAALAHSEEIATSQAAATKALPNGRDALDgPSMEAE 2630
Cdd:COG4913 736 LEAAEDLARLELRALLEErfaaalgdavERELRENLEeRIDALRARLNRAEEELERAMRAFNREWPAETADLD-ADLESL 814
|
...
gi 40849888 2631 PEY 2633
Cdd:COG4913 815 PEY 817
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2317-2603 |
1.41e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2317 EAELLQQQKELAQEQA----RRLQEDKEQMAQQLVEETQGfQRTLEAERQRQLEMS-----AEAERLKLRMAEMSRAQAR 2387
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2388 AEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDqdaERLREAIAELEREKEKLKQEAKLLQLKSEEM 2465
Cdd:pfam17380 346 RERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2466 QTVQQEQILQETQALQKsFLSEKDSLLQRERFIEQEKA-KLEQLFQDEvakakqlqeeQQRQQQQMEqekqelvasMEEA 2544
Cdd:pfam17380 423 EQIRAEQEEARQREVRR-LEEERAREMERVRLEEQERQqQVERLRQQE----------EERKRKKLE---------LEKE 482
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 2545 RRRQREAEEgVRRKQEELQRLEQQRQQQekllaeENQRLRERLQRLEEEHRAALAHSEE 2603
Cdd:pfam17380 483 KRDRKRAEE-QRRKILEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1640-1883 |
1.51e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1640 VAQQKSLAQADA--EKQKEEAEREARRRGKAEEQAVRQRelaeQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ 1717
Cdd:NF012221 1535 VATSESSQQADAvsKHAKQDDAAQNALADKERAEADRQR----LEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1718 RQLLEEELARLQHEATAATQKRQELEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----R 1786
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQ 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1866
Cdd:NF012221 1686 KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQA 1765
|
250
....*....|....*..
gi 40849888 1867 RRLEEQAAQHKADIEER 1883
Cdd:NF012221 1766 QADAKGAKQDESDKPNR 1782
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1315-1554 |
1.53e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1315 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAELEARELQRrMQEEVTR 1392
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1393 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggAEDELQALRAR-A 1471
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA---REKQRALQALDELKLQAEEAerrlRQAEAER 1548
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrleREVEVARELYESLLQRLEEA----RLAEALT 384
|
....*.
gi 40849888 1549 ARQVQV 1554
Cdd:COG3206 385 VGNVRV 390
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1809-2482 |
1.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1809 AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdEAFQRRRLEEQAAQHKADIEERLAQLR 1888
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE-EIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1889 KASESELERQKGLVEDT--LRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAA 1966
Cdd:PRK03918 266 ERIEELKKEIEELEEKVkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1967 eeeqrrreaeervqrslaaEEEAARQRKVALEEVERLkakVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV 2046
Cdd:PRK03918 346 -------------------KLKELEKRLEELEERHEL---YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2047 VQQREeelqqtlqqeqNMLERLRSEAEAARRAaeeaeeareqaereaaqsRKQVEEAERLKqsaeeqaqaqaqaqaaaek 2126
Cdd:PRK03918 404 EEEIS-----------KITARIGELKKEIKEL------------------KKAIEELKKAK------------------- 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2127 lRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEeLQRLKAEVT 2206
Cdd:PRK03918 436 -GKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2207 EAARQRSQVEEELFsvRVQMEELGKLKARIEAENRALilRDKDNTQRFLEEEAEKMKQVAEEAARLsvaaqeaarLRQLA 2286
Cdd:PRK03918 514 KYNLEELEKKAEEY--EKLKEKLIKLKGEIKSLKKEL--EKLEELKKKLAELEKKLDELEEELAEL---------LKELE 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2287 EEDLAQQRALAEKmLKEKMQAVQEATRLK-AEAELLQQQKELAQEQarrlqedkeqmaqqlveetqgfqRTLEAERQRQL 2365
Cdd:PRK03918 581 ELGFESVEELEER-LKELEPFYNEYLELKdAEKELEREEKELKKLE-----------------------EELDKAFEELA 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2366 EMSAEAERLKLRMAEMSRAQAraEEDAQRFRKQAEEIGEKLHRTElatqekvTLVQTLEIQRQQSDQDAERLREAIAELE 2445
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLR-------AELEELEKRREEIKKTLEKLKEELEERE 707
|
650 660 670
....*....|....*....|....*....|....*..
gi 40849888 2446 REKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2482
Cdd:PRK03918 708 KAKKELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1768-1934 |
1.67e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1768 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1846
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1847 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEIMALKASFE 1924
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 40849888 1925 KAAAGKAELE 1934
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2146-2603 |
1.71e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2146 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILdeelqRLKAEVTEAARQRSQVEEELFSVRVQ 2225
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2226 MEELGKLKARIEA--ENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA---RLRQLAEE---DLAQQRALA 2297
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2298 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLVEETQ-----------GFQRTLEAERQ---- 2362
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2363 -----RQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERL 2437
Cdd:TIGR00618 479 eqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2438 REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQeqILQETQALQKSFLSEKDSLLQRERFIEQEKakleqlfQDEVAKAK 2517
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLTEKLSEAEDMLACEQHALLRKL-------QPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2518 QLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAA 2597
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
....*.
gi 40849888 2598 LAHSEE 2603
Cdd:TIGR00618 710 ETHIEE 715
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1624-1820 |
1.88e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1624 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQE 1703
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1704 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAE 1781
Cdd:COG2268 268 -----YEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAE 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 40849888 1782 AGRFRELAEEAARLRALAEEAKRQRQLAEedAARQRAEA 1820
Cdd:COG2268 340 AEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEAAAKP 376
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3083-3119 |
1.90e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.90e-05
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3083 KLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQG 3119
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2195-2414 |
1.94e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2195 DEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIlRDKDNTQRFLEEEAEKMKQVAEEAARLSV 2274
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2275 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM---A 2343
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaeL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 2344 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2414
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1566-1887 |
1.98e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.45 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1566 ELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1645
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1646 LAQADAEKQKEEAEREARRRGKAEEQ---AVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLE 1722
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQlaaETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1723 EELARLQheataatqkrqeleaelaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1802
Cdd:pfam19220 174 QENRRLQ------------------ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1803 KRQRQlAEEDAARQRAEAervLTEKLAAiseATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1882
Cdd:pfam19220 236 VEAHR-AERASLRMKLEA---LTARAAA---TEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLER 308
|
....*
gi 40849888 1883 RLAQL 1887
Cdd:pfam19220 309 RTQQF 313
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1340-1768 |
2.06e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.68 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSE 1419
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1420 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1499
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1500 RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1579
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1580 QLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAE 1659
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1660 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1739
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 40849888 1740 QELEAELAKVRAEMEVLLASKARAEEESR 1768
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2153-2609 |
2.06e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2153 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE-TDHQKSILDE-ELQRLKAEVTEAAR-----QRSQVEEELFSVRVQ 2225
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEaGLDDADAEAVEARReeledRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2226 MEELGK----LKARI-EAENRALILRDKDNTqrfLEEEAEKMK-QVAEEAARLSVAAQEAARLRQL---AEEDLAQQRAL 2296
Cdd:PRK02224 337 AQAHNEeaesLREDAdDLEERAEELREEAAE---LESELEEAReAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2297 AEKMLKEKMQAVQEATRLKAEaelLQQQKELAQEQARRLQEDKEQMAQQLVEETqGFQRTLEAERQRQLEMSAEAERLKL 2376
Cdd:PRK02224 414 LEELREERDELREREAELEAT---LRTARERVEEAEALLEAGKCPECGQPVEGS-PHVETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2377 RMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEK 2450
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2451 LKQEAKLLQLKSEEM-QTVQQEQILQETQALQKSFLSEKDSLL-QRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQrqqq 2528
Cdd:PRK02224 570 AREEVAELNSKLAELkERIESLERIRTLLAAIADAEDEIERLReKREALAELNDERRERLAEKRERKRELEAEFDE---- 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2529 qmeqekqelvASMEEARRRQREAEE------GVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSE 2602
Cdd:PRK02224 646 ----------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYD 715
|
....*..
gi 40849888 2603 EIATSQA 2609
Cdd:PRK02224 716 EAEELES 722
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2170-2595 |
2.14e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2170 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSVRVQMEELGKLKAriEAENRALILRDKD 2249
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2250 NTQ-RFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2324
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2325 ----KELAQEQARRLQEDKEQMaQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2400
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2401 EIGEKLHRTElatQEKVTLVQT-------LEIQRQQSDQDAERLREAIAEL--EREKEKLKQeaklLQLKSE-EMQTVQQ 2470
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQLTAIKTSEEHYLKEVEDLktELEKEKLKN----IELTAHcDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2471 EQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVakakqlqeeqqRQQQQMEQEKQELVASMEEARRRQRE 2550
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEM-----------NLRDELESVREEFIQKGDEVKCKLDK 570
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 40849888 2551 AEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2595
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1783-2029 |
2.18e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1783 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1862
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1863 AFQRRRLEEQAAQHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELE 1936
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1937 LGRIRSN-AEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALeeverLKAKVEEARRLRE 2015
Cdd:pfam07888 194 FQELRNSlAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG-----LGEELSSMAAQRD 268
|
250
....*....|....*
gi 40849888 2016 RAEQESAR-QLQLAQ 2029
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2152-2393 |
2.25e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2152 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGK 2231
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2232 LKARI----EAENRALILRDKDNTQRFLEEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQA 2307
Cdd:COG3883 91 RARALyrsgGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2308 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2387
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*.
gi 40849888 2388 AEEDAQ 2393
Cdd:COG3883 243 AASAAG 248
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
35-142 |
2.28e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 47.31 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 35 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 101
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40849888 102 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 142
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
30-138 |
2.46e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 100
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 40849888 101 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2147-2356 |
2.87e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSVRV 2224
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2225 QMEELGKLKARIEAENRaLILRDKDNTQRFLEEEAE---KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2301
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2302 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2356
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1002-1473 |
2.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1002 KDPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAaptlrseleltLGKLEQVRSLSAIYLEKLKTIS 1081
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL-----------YQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1082 LVIRSTQGAEEVLKTHEEHLKEAQAVPATLQEL--EVTKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRhgER 1159
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE--LE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1160 DVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAD--------PLSSWLQDAKSRQEQIQAVPIANSQ 1231
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlglLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1232 AAREQLRQEKaLLEEIERHGEKVEECQKFAKQYINAIKDYElQLITYKAQLEpvaspakkpkvqsgSESVIQEYVDLRTR 1311
Cdd:COG4717 311 PALEELEEEE-LEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELE--------------EELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1312 YSELTTLTSqyikfiSETLRRMEEeerlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVT 1391
Cdd:COG4717 375 LLAEAGVED------EEELRAALE----QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1392 RREEAavDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDE-LQALRAR 1470
Cdd:COG4717 445 EEELE--ELREELAELEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLER 520
|
...
gi 40849888 1471 AEE 1473
Cdd:COG4717 521 ASE 523
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1632-1764 |
2.99e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1632 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQREL--AEQELEKQRQLaegtAQQRLAAEQELIRLRA 1709
Cdd:COG1566 80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlAQRELERYQAL----YKKGAVSQQELDEARA 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1710 ETEQGEQQRQLLEEELARLQHEATAATQKRQeLEAELAKVRAEMEVLLASKARAE 1764
Cdd:COG1566 156 ALDAAQAQLEAAQAQLAQAQAGLREEEELAA-AQAQVAQAEAALAQAELNLARTT 209
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2146-2448 |
3.06e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2146 LKQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSVRVQ 2225
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2226 MEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2304
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2305 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRT---LEAERQRQLEMSAEAERLKLRMAEM 2381
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2382 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDQDAERLREaiaELEREK 2448
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1331-1504 |
3.07e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElearELQRRMQEEVTRREEAAVdAQQQKRSIQEE 1410
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE----ERQRQEEEERKQRLQLQA-AQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1411 LQHLRQsseaEIQAKAQQVE---AAERSRMRIEEEIRVVrlqlETTERQRGGAEDELQALRARAEEAEAQKRQAQEEaer 1487
Cdd:pfam15709 428 FRRKLQ----ELQRKKQQEEaerAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE--- 496
|
170
....*....|....*..
gi 40849888 1488 lRRQVQDESQRKRQAEA 1504
Cdd:pfam15709 497 -RRQKEEEAARLALEEA 512
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1472-1808 |
3.12e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1551
Cdd:pfam15709 163 ETPASISHAERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1552 VQVALETA----QRSAEVELQSKRASFAEKTAQL------------------ERTLQEEHVTVTQLREEAERRAQQQAEA 1609
Cdd:pfam15709 243 LEVAAELSgpdvINSKETEDASERGAFSSDSVVEdpwlsskydaeesqvsidGRSSPTQTFVVTGNMESEEERSEEDPSK 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1610 ERAREEAERELERWQLKANEALRLRLQAE----EVAQQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEK 1685
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVErkrrEQEEQRRLQQEQLERAEKM---------REELELEQQRRFEEIRLRK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1686 QRQLAEGTAQQRLAAEQELiRLRAETEQGEQQRQLLEEELARLQHE--------ATAATQKRQELEAELA---KVRAEMe 1754
Cdd:pfam15709 394 QRLEEERQRQEEEERKQRL-QLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAeeqKRLMEM- 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1755 vllASKARAEEESRSTSEKSKQRLEAEAGRFRElaEEAARLraLAEEAKRQRQL 1808
Cdd:pfam15709 472 ---AEEERLEYQRQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQE 518
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2234-2604 |
3.13e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2234 ARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLS-------VAAQEAARLRQLAEEDLAQQRAL--AEKMLKEK 2304
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDHLNLVQTALRQQEKIerYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2305 MQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMS 2382
Cdd:PRK04863 361 EERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQL---CGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2383 RAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiqRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKS 2462
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2463 EEMQTVQQEQILQETQALQKSFLSEKDSllqrERFIEQEKAKLEQLFQDEvakakqlqeeqqRQQQQMEQEKQELVASME 2542
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDE------------DELEQLQEELEARLESLS 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2543 EARRRQREAEEGVRRKqeelQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEI 2604
Cdd:PRK04863 572 ESVSEARERRMALRQQ----LEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDV 629
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1417-1588 |
3.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1417 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1494
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1495 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAErARQVQVALETAQR 1561
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180
....*....|....*....|....*..
gi 40849888 1562 SAEVELQSKRASFAEKTAQLERTLQEE 1588
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1816-2206 |
3.59e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1816 QRAEAERVLTEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasESEL 1895
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1896 ERQKglVEDTLRQRRQVEEEIMALKASFEKaaagkaELE-LELGRIRSNaedtmrSKELAEQEAARQRQLAaeeeqrrre 1974
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1975 aeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQReee 2053
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2054 lqqtlqqeqnmleRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeq 2133
Cdd:pfam17380 474 -------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2134 eaarraqaeqaalKQKQAADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2206
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1326-2042 |
3.67e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1326 ISETLRRMEEEERLAEQ-QRAEE-----RERLAEVEAALEKQR-QLAEAHAQAKaQAELEARELQRRMQEEVTRREEaav 1398
Cdd:PRK04863 333 ASDHLNLVQTALRQQEKiERYQAdleelEERLEEQNEVVEEADeQQEENEARAE-AAEEEVDELKSQLADYQQALDV--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1399 daqQQKRSIQ--------EELQHLRQSSE----------AEIQAKAQQVEAAERS---RMRIEEEIR---------VVRL 1448
Cdd:PRK04863 409 ---QQTRAIQyqqavqalERAKQLCGLPDltadnaedwlEEFQAKEQEATEELLSleqKLSVAQAAHsqfeqayqlVRKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1449 --QLETTERQRGGAEDELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQ 1525
Cdd:PRK04863 486 agEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1526 ALDELKLQAEEA-ERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvtVTQLREEAERRAQ 1604
Cdd:PRK04863 566 RLESLSESVSEArERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQD----VTEYMQQLLERER 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1605 QQAEAERAREEAERELERW-----QLKANEALRLRLQAEEV---------------------AQQKSLAQA----DAEKQ 1654
Cdd:PRK04863 642 ELTVERDELAARKQALDEEierlsQPGGSEDPRLNALAERFggvllseiyddvsledapyfsALYGPARHAivvpDLSDA 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1655 KEEAEREARRRG-----KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARL 1728
Cdd:PRK04863 722 AEQLAGLEDCPEdlyliEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAER 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1729 QHEATAATQKRQEL--------------------EAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR---LEAEA 1782
Cdd:PRK04863 802 YATLSFDVQKLQRLhqafsrfigshlavafeadpEAELRQLNRrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLL 881
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1783 GRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAEAERVltEKLAAI-----SEATRLKTEAEIALKEKEAENERL 1855
Cdd:PRK04863 882 PRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNALAQL--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQA 958
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1856 RRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGK 1930
Cdd:PRK04863 959 FALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQML 1036
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1931 AELELELGRIrsnaedTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERlkaKVEEA 2010
Cdd:PRK04863 1037 QELKQELQDL------GVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLER---DYHEM 1107
|
810 820 830
....*....|....*....|....*....|...
gi 40849888 2011 RRLRERAEQESARQLQLAQE-AAQKRLQAEEKA 2042
Cdd:PRK04863 1108 REQVVNAKAGWCAVLRLVKDnGVERRLHRRELA 1140
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1770-2049 |
3.68e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.15 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1770 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA-EIALKEK 1848
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1849 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKAsfeKAAA 1928
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1929 GKAELELELGRIRSNAEDTMRSKElaEQEAAR-QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK- 2006
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKA--ERDELRaKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEe 255
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 40849888 2007 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQ 2049
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3339-3377 |
3.74e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.74e-05
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3339 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3377
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1392-1745 |
3.86e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1392 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARA 1471
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1551
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1552 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1631
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1632 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1711
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 40849888 1712 EQGEQQRQLLEEELARLQHEATAATQKRQELEAE 1745
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4374-4411 |
4.00e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.00e-05
10 20 30
....*....|....*....|....*....|....*...
gi 40849888 4374 QRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTA 4411
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2258-2417 |
4.03e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2258 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2337
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2338 DKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2417
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3339-3374 |
4.12e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.12e-05
10 20 30
....*....|....*....|....*....|....*.
gi 40849888 3339 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3374
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1003-1496 |
4.29e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.11 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1003 DPARECAQRIAEQQKAQAE-VEGLGKGVARLSAEAEKV-LALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLK-- 1078
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIkMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNka 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1079 --TISLVIR----STQGAEEVLKTHEEHLKEAQavpatlQELEVTKASLKKLRAQAEAQQPVFNTLRDELrgaqevgERL 1152
Cdd:pfam05483 344 kaAHSFVVTefeaTTCSLEELLRTEQQRLEKNE------DQLKIITMELQKKSSELEEMTKFKNNKEVEL-------EEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1153 QQRHGERDV---EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESADPLSSWLQDAKSRQEQI 1222
Cdd:pfam05483 411 KKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1223 QAVPIANSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK------KPKVQS 1296
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1297 GSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA 1369
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1370 QAKA-----QAELEAREL-QRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRmriEEEI 1443
Cdd:pfam05483 651 KFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1444 RVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1496
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4125-4153 |
4.54e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.54e-05
10 20
....*....|....*....|....*....
gi 40849888 4125 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4153
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1382-2015 |
4.59e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.72 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1382 LQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAe 1461
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLC- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1462 DELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEAAREKQRALQALDELKLQAEEAERRL 1541
Cdd:pfam05483 158 NLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL----RVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1542 RQAEAERarqvQVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELE 1621
Cdd:pfam05483 234 EINDKEK----QVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQRLaae 1701
Cdd:pfam05483 300 DIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQRL--- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1702 qelirlraetEQGEQQRQLLEEELARLQHEATAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1777
Cdd:pfam05483 373 ----------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKEQEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeialkekeaENERLRR 1857
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------ENKELTQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1858 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEIMALKASFEKAA 1927
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYEVLKKE 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1928 AGKAELELELGRIRSNAEDTMRSKELAEQE--------AARQRQLAAEEEQRRREAEERVQRSLAAEE------EAARQR 1993
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEiidnyqKEIEDK 666
|
650 660
....*....|....*....|....*.
gi 40849888 1994 KVA----LEEVERLKAKVEEARRLRE 2015
Cdd:pfam05483 667 KISeeklLEEVEKAKAIADEAVKLQK 692
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3006-3043 |
4.82e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.82e-05
10 20 30
....*....|....*....|....*....|....*...
gi 40849888 3006 RQALRGTSVIAGVWLEEAGQKLSIYEALRRDLLQPEVA 3043
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2273-2551 |
5.58e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.83 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2273 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmaQQLVEETQG 2352
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK----QQQLAAISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2353 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDQ 2432
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2433 DAE---RLREAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSllqrerfiEQEKAKLEQ 2507
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 40849888 2508 LFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRR-QREA 2551
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2240-2604 |
5.60e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2240 NRALILRDKDNTQRflEEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2314
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2315 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2380
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2381 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQL 2460
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2461 KSEEMQTVQQEQILQEtqalqksfLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAkqlqeeqqrqqqqmeqekQELVAS 2540
Cdd:COG3096 505 RSQQALAQRLQQLRAQ--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAA------------------EELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2541 MEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSEEI 2604
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEV 628
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
34-135 |
5.69e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.49 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHF 135
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1461-1819 |
5.91e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.76 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1461 EDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA----EAEAAREKQRALQALDELKLQAEE 1536
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERAleeeEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1537 AERRlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaeraREEA 1616
Cdd:pfam13868 85 REQK-RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE-------------------------FNEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1617 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1696
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI----------EEEKEREIARLRAQQEKAQDEKAERDELRA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1697 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAatQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1776
Cdd:pfam13868 209 KLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 40849888 1777 RLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1819
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1432-1551 |
5.92e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.19 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1432 AERSRMRIEEEIRVVRLQLETTERQRggaedELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvK 1511
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 40849888 1512 AEAEAAREKQRALQALDELKLQAEEAERRLRQaEAERARQ 1551
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2241-2437 |
5.92e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2241 RALILRDKDNTQRFLEEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2320
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2321 LQQQKELAQEQARRLQEDKEQMAQQL--VEETQGFQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQR 2394
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQqeLEKKEEELEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 40849888 2395 FRKQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDQDAERL 2437
Cdd:PRK12704 174 LIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2246-2401 |
6.07e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 6.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2246 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2322
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2323 QQKELAQEQARRLQEDKE---QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2395
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 40849888 2396 -RKQAEE 2401
Cdd:pfam15709 512 aMKQAQE 518
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1456-1654 |
6.12e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1456 QRGGAEDELQALRARAEEAEAQ-KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELKLQA 1534
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVErKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1535 EEAER---RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLreeaerraqqqa 1607
Cdd:pfam15709 404 EEEERkqrLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM------------ 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1608 eaerareEAERELERWQLKANEALRLRLQAEEVAQQKS----LAQADAEKQ 1654
Cdd:pfam15709 472 -------AEEERLEYQRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQ 515
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1307-1586 |
6.45e-05 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 49.06 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1307 DLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAELE-A 1379
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1380 RELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVE------AAERSRMRIEEEirVVRLQLETT 1453
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1454 ERQRGGAEDE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqaldelkl 1532
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA--------- 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1533 qaeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1586
Cdd:pfam15450 453 --------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2190-2593 |
6.78e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2190 QKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALilRDKDNTQRFLEEEAEKMKQVAEEA 2269
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA--SDHLNLVQTALRQQEKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2270 ARLSVAAQEAARLRQLAEEDLAQQRALAEkmlkekmQAVQEATRLKA------EAELLQQQKELAQEQA-RRLQEDKE-- 2340
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSqladyqQALDVQQTRAIQYQQAvQALERAKQlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2341 QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERlKLRMAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVTLV 2420
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2421 QTLEIQRQQSDQdAERLREAIAELEREKEKLKQEAKLLQ----------LKSEEMQTVQQEQ-ILQETQALQKSFLSEKD 2489
Cdd:PRK04863 503 RRLREQRHLAEQ-LQQLRMRLSELEQRLRQQQRAERLLAefckrlgknlDDEDELEQLQEELeARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2490 SLLQRERfiEQEKAKLEQLFQDEVA--KAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEgvrrkqeelqrleq 2567
Cdd:PRK04863 582 MALRQQL--EQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------------- 645
|
410 420
....*....|....*....|....*.
gi 40849888 2568 qrqqqekllaeENQRLRERLQRLEEE 2593
Cdd:PRK04863 646 -----------ERDELAARKQALDEE 660
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1370-1526 |
6.83e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.19 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1370 QAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQ-------EELQHLRQSSEAEIQAKAQQVEAAER--SRMRIE 1440
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELaisrqdyDGATAQLRAAQAAVKAAQAQLAQAQIdlARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1441 EEIRVV-RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAAR 1518
Cdd:pfam00529 133 APIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLER 209
|
....*...
gi 40849888 1519 EKQRALQA 1526
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1703-2026 |
7.57e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1703 ELIRLRAETEQGEQQ--RQLLEEELARLQHEATAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1777
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LEAEAGRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LTEKLAAISEATRLKTEAEIA 1844
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1845 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsESELERQKGLVE---DTLRQRRQVEEEIMALKA 1921
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1922 S---FEKAAAGKAELELELGRIRSNAE-----DTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 1993
Cdd:pfam05557 236 KlerEEKYREEAATLELEKEKLEQELQswvklAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
330 340 350
....*....|....*....|....*....|...
gi 40849888 1994 KValEEVERLKAKVEEARRLRERAEqESARQLQ 2026
Cdd:pfam05557 316 LE--QELAQYLKKIEDLNKKLKRHK-ALVRRLQ 345
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1307-1587 |
8.09e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1307 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAELEARELQRRM 1386
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1387 QEEVTRREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDE 1463
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1464 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEA 1537
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1538 --ERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1587
Cdd:pfam07888 316 dkDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2146-2364 |
8.14e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.45 E-value: 8.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2146 LKQKQAA-DAEMEKHKKFAE-QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRSQVEEELFSV 2222
Cdd:NF012221 1551 AKQDDAAqNALADKERAEADrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2223 RVQMEELGKlkaRIEA----------------ENRALILRDK-----DNTQRFLEEEAEKMKQ--------VAEEAARLS 2273
Cdd:NF012221 1619 TKELTTLAQ---GLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2274 VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlveETQGF 2353
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAKGA 1772
|
250
....*....|.
gi 40849888 2354 QRTLEAERQRQ 2364
Cdd:NF012221 1773 KQDESDKPNRQ 1783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3786-3822 |
8.27e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.27e-05
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3786 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3822
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1340-1471 |
8.71e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1340 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAELEARELQRRMQEevtrREEAAVDAQQqkrsiQEELQHLRQ 1416
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQAL----YKKGAVSQQE-----LDEARAALD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1417 SSEAEIQAKAQQVEAAeRSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARA 1471
Cdd:COG1566 159 AAQAQLEAAQAQLAQA-QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
27-132 |
9.64e-05 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 27 YKDErdrvQKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQN 93
Cdd:cd21292 21 YSEE----EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHEN 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 40849888 94 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 132
Cdd:cd21292 97 LTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1006-1555 |
1.05e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1006 RECAQRIAEQQKAQA-EVEGLGKGVARLSAEAEkvlALPEPSPAAPTLRSELELTLGK-LEQVRSLSAIYLEKL-----K 1078
Cdd:pfam07111 86 RETSLQQKMRLEAQAmELDALAVAEKAGQAEAE---GLRAALAGAEMVRKNLEEGSQReLEEIQRLHQEQLSSLtqaheE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1079 TISLVIRSTQGAEEVLKTHE-EHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPVFNTLRdelrgaQEVGERLQQRHG 1157
Cdd:pfam07111 163 ALSSLTSKAEGLEKSLNSLEtKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTLVESLR------KYVGEQVPPEVH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1158 ERDVEVERWR--ERVTQLLE---RWQAVLAQTDVRQREL--------EQLGRQLR--------YYRESADPLSSWLQDAK 1216
Cdd:pfam07111 237 SQTWELERQEllDTMQHLQEdraDLQATVELLQVRVQSLthmlalqeEELTRKIQpsdslepeFPKKCRSLLNRWREKVF 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1217 SRQEQIQAVPIANSQAAReQLRQEKALLEEierhgekveecQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQS 1296
Cdd:pfam07111 317 ALMVQLKAQDLEHRDSVK-QLRGQVAELQE-----------QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1297 GSESviqeyvdlRTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAK 1372
Cdd:pfam07111 385 AQEA--------RRRQQQQTASAEEQLKFVvnamSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1373 AQAELEAR-----------ELQRRMQEEVTRREEAAVDAQQQ--KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRI 1439
Cdd:pfam07111 457 ALAQLRQEscpppppappvDADLSLELEQLREERNRLDAELQlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1440 EEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEA-----ERLRRQVQDESQ-----RKRQAEAELALR 1509
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKvaeveTRLREQLSDTKRrlneaRREQAKAVVSLR 616
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 40849888 1510 vKAEAEAAREKQRAlQALDELKLQA--EEAERRLRQA-EAERARQVQVA 1555
Cdd:pfam07111 617 -QIQHRATQEKERN-QELRRLQDEArkEEGQRLARRVqELERDKNLMLA 663
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
172-249 |
1.09e-04 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 44.22 E-value: 1.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 172 DNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 249
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1465-1703 |
1.10e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1465 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LDELKLQAEEAERRL 1541
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1542 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREeaerraqqqaeaerareeaerele 1621
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA------------------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1622 rwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELA--EQELEKQRQLAEGTAQQRLA 1699
Cdd:COG3206 299 --QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEE 376
|
....
gi 40849888 1700 AEQE 1703
Cdd:COG3206 377 ARLA 380
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2277-2507 |
1.22e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2277 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2356
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2357 LEaERQRQLEmsAEAERLKLRMAEMSRAQAR--AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDA 2434
Cdd:pfam12128 680 AN-ERLNSLE--AQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2435 ERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEqILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ 2507
Cdd:pfam12128 757 KRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQE-VLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1481-1775 |
1.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1481 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELKLQAEEAERRLRQAEAERArqvqvALETAQ 1560
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1561 RSAEVELQSKRASFAEKTAQLERTLQEehvtvtqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEV 1640
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRA----------------------------------LYRLGRQPPLALLLSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1641 AQQKSLAQAdaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL 1720
Cdd:COG4942 132 LDAVRRLQY------------LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1721 LEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1775
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1746-1903 |
1.38e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1746 LAKVRAEmevllASKARAE---EESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAEEAKrqrqlaeeDAARQRAEAE 1821
Cdd:COG2268 194 IAEIIRD-----ARIAEAEaerETEIAIAQANREAEEAELEQEREIETaRIAEAEAELAKKK--------AEERREAETA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1822 RVLTEKLAAISEAtrlKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHK-ADIEERLAQLRKASESELERQKG 1900
Cdd:COG2268 261 RAEAEAAYEIAEA---NAEREVQRQLEIAEREREIELQEKEA-EREEAELEADVRKpAEAEKQAAEAEAEAEAEAIRAKG 336
|
...
gi 40849888 1901 LVE 1903
Cdd:COG2268 337 LAE 339
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3955-3989 |
1.40e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*
gi 40849888 3955 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3989
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1369-1850 |
1.43e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.11 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1369 AQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrl 1448
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1449 qletterqRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlQALD 1528
Cdd:COG3064 78 --------KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAA-EAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1529 ELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1608
Cdd:COG3064 149 AAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1609 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1688
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1689 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1768
Cdd:COG3064 309 GAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1769 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1848
Cdd:COG3064 389 AGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
..
gi 40849888 1849 EA 1850
Cdd:COG3064 469 VA 470
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
955-1534 |
1.44e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 955 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKDPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1033
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1034 AEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTQGAEEVLKTHEEHLKEAQAVpaTLQE 1113
Cdd:TIGR00618 421 DLQGQLAHA----------KKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1114 LEVTKASLKKLRAQAEAQQPVFNTLR---------DELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQT 1184
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1185 DVRQRELEQLGRQLRYYRESADPLSSWLQDAksrQEQIQAVPIANSQAAREQLRQEKALLEEIERHgEKVEECQKFAKQY 1264
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQ-DVRLHLQQCSQEL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1265 INAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAEQQR 1344
Cdd:TIGR00618 642 ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYDREF 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1345 AEERERLAEVEAALEKQRqlaEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQqkrsIQEELQHLRQSSEAEIQA 1424
Cdd:TIGR00618 721 NEIENASSSLGSDLAARE---DALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ----TGAELSHLAAEIQFFNRL 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1425 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE 1503
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFlSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
570 580 590
....*....|....*....|....*....|.
gi 40849888 1504 AELALRVKAEAEAAREKQRALQALDELKLQA 1534
Cdd:TIGR00618 874 LSDKLNGINQIKIQFDGDALIKFLHEITLYA 904
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1332-1519 |
1.44e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1332 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEEL 1411
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1412 QHLRQSSEAEIQAKAqqveaaersrmrieeeirvvrlqlETTERQRGGAEDELqALRARAEEAEAQKRqaQEEAERLRRQ 1491
Cdd:pfam05262 280 KREIEKAQIEIKKND------------------------EEALKAKDHKAFDL-KQESKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 40849888 1492 VQDESQR-KRQAEAElalrVKAEAEAARE 1519
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2147-2459 |
1.63e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAE---MEKHKKFAEQTLRQKAqVEQEL-----------TTLRLQlEETDHQKSILDEELQRLKAE---VTEAA 2209
Cdd:COG3096 297 ARRQLAEEQyrlVEMARELEELSARESD-LEQDYqaasdhlnlvqTALRQQ-EKIERYQEDLEELTERLEEQeevVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2210 RQRSQVEEELFSVRVQMEELGKLKARI-----EAENRAL----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA 2280
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYqqaldVQQTRAIqyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2281 RLR-----QLAEEDLAQQR-----ALAEKMLKE--KMQAVQEATRL-------KAEAELLQQ---------QKELAQEQA 2332
Cdd:COG3096 455 EEVleleqKLSVADAARRQfekayELVCKIAGEveRSQAWQTARELlrryrsqQALAQRLQQlraqlaeleQRLRQQQNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2333 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE---EIGEKLHRT 2409
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERL 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2410 ELATQEKVTLVQTLEIQRQQSdqdAERLREAIAE---LEREKEKLKQEAKLLQ 2459
Cdd:COG3096 615 REQSGEALADSQEVTAAMQQL---LEREREATVErdeLAARKQALESQIERLS 664
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3673-3709 |
1.71e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.71e-04
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3673 RYLYGTGSVAGVYLPGSRQTLTIYQALKKGLLSAEVA 3709
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1758-1955 |
1.73e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1758 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLTEKLAAISEATRL 1837
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1838 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIM 1917
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 40849888 1918 ALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAE 1955
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2266-2717 |
1.76e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 48.04 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2266 AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2345
Cdd:COG4995 23 ALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2346 LVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2425
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2426 QRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKL 2505
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2506 EQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRLRE 2585
Cdd:COG4995 263 ALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2586 RLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDALdgpsmeaepeytfEGLRQKVPAQQLQEAGILSMEELQRLTQGH 2665
Cdd:COG4995 343 ALLAAALAAALALAAALALALLAALLLLLAALLALLL-------------EALLLLLLALLAALLLLAAALLALAAAQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 2666 TTVAELTQREDVHRYLKGGSSIAGLLLKP--TNEKLSVYTALQRQLLSPGTALI 2717
Cdd:COG4995 410 RLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1438-1583 |
1.76e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.97 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1438 RIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1517
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1518 REKQRAL-----QALDELKLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1583
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKVNEALSGIDSDDATSALER 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1787-2022 |
1.77e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1787 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRlaedeafQR 1866
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1867 RRLEEQAAQHKADIEERLAQLRKASESE----LERQKGlVEDTLRQRRQVEEEIMALKASFEKAAAGKAELElelgRIRS 1942
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1943 NAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESA 2022
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1412-1855 |
1.77e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.13 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1412 QHLRQSSEAEIQAKAQQVEA----------AERSRMRIEEEIRVVR--LQLETTERQRGGAE-DELQALRAR--AEEAEA 1476
Cdd:PRK10929 30 QELEQAKAAKTPAQAEIVEAlqsalnwleeRKGSLERAKQYQQVIDnfPKLSAELRQQLNNErDEPRSVPPNmsTDALEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1477 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR---EKQRALQALDELKLQAEEAERRLRQAEAerarqvq 1553
Cdd:PRK10929 110 EILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRqlnEIERRLQTLGTPNTPLAQAQLTALQAES------- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1554 valetAQRSAEVElqskrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeaerELERWQLKAN---EA 1630
Cdd:PRK10929 183 -----AALKALVD----------------------------------------------------ELELAQLSANnrqEL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1631 LRLRLqaeEVAQQKSlAQADAEKQKEeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1710
Cdd:PRK10929 206 ARLRS---ELAKKRS-QQLDAYLQAL----------RNQLNSQRQRE-AERALESTELLAEQSGDLPKSIVAQFKINREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1711 TEQGEQQRQLLeEELARLQHEATAATQK-RQELEA------ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEAG 1783
Cdd:PRK10929 271 SQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1784 RFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAA---------------ISEATRLK---TEAEI 1843
Cdd:PRK10929 344 QLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLED 418
|
490
....*....|...
gi 40849888 1844 ALKE-KEAENERL 1855
Cdd:PRK10929 419 ALKEvNEATHRYL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2147-2594 |
1.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2226
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2301
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSN-----IPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2302 ------KEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQED-----------------KEQMAQQL----VEETQ 2351
Cdd:COG4913 489 ltllvpPEHYAAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcVDSPE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2352 GFQRT--------------------------------LEAERQRQ-LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2398
Cdd:COG4913 569 ELRRHpraitragqvkgngtrhekddrrrirsryvlgFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2399 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---SDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQ 2475
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2476 ETQALQK--SFLSEKDSLLQRERFIEQekakLEQLFQDEVAKAkqlqeeqqrqqqqmeqEKQELVASMEEARRRQREAEE 2553
Cdd:COG4913 728 ELDELQDrlEAAEDLARLELRALLEER----FAAALGDAVERE----------------LRENLEERIDALRARLNRAEE 787
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 40849888 2554 GVRRKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2594
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2155-2605 |
1.90e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2155 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDE---ELQRLKAEVTEAARQRSQVEE---ELFSVRVQMEE 2228
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2229 LGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSvaaQEAARL------------------RQLAEED- 2289
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKELkkaieelkkakgkcpvcgRELTEEHr 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2290 ---LAQQRALAEKMLKEKMQAVQEATRLKAEAE----LLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAE 2360
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2361 RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtLEIQRQQSDQDAE-RLRE 2439
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-ERLKELEPFYNEYlELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2440 AIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKSFlSEKDSLLQRERFIEQEKakleqlfqdEVAKAK 2517
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKY-SEEEYEELREEYLELSR---------ELAGLR 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2518 QLQEEQQRQQQQMEQEKQELVASMEEarrrQREAEEGVRrkqeelqrleqqrqqQEKLLAEENQRLRERLQRLE-EEHRA 2596
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEE----REKAKKELE---------------KLEKALERVEELREKVKKYKaLLKER 740
|
....*....
gi 40849888 2597 ALAHSEEIA 2605
Cdd:PRK03918 741 ALSKVGEIA 749
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4264-4297 |
1.90e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.90e-04
10 20 30
....*....|....*....|....*....|....
gi 40849888 4264 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4297
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1670-1991 |
2.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1670 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1749
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1750 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA 1829
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1830 AISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR 1909
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1910 RQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 1989
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 40849888 1990 AR 1991
Cdd:COG4372 368 AD 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2150-2310 |
2.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2150 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQmEEL 2229
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2230 GKLKARIEAENRALILRDKDnTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2309
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 40849888 2310 E 2310
Cdd:COG1579 171 K 171
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1379-1551 |
2.19e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1379 ARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVeaaersrmrieeeirvvrlqlETTERQRG 1458
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI---------------------ATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1459 GAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRALQALDELKLQAEEAE 1538
Cdd:COG3524 232 ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASLLAEYERLELEREFAE 299
|
170
....*....|....*
gi 40849888 1539 RRLRQAEA--ERARQ 1551
Cdd:COG3524 300 KAYTSALAalEQARI 314
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2680-2718 |
2.26e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.16 E-value: 2.26e-04
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 2680 YLKGGSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALIL 2718
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1667-1882 |
2.30e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1738
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1739 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQR 1817
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARaKAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1818 AEAERVLTEKL-AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1882
Cdd:PRK05035 607 VAEVDPKKAAVaAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2166-2398 |
2.33e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2166 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIL 2245
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2246 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2319
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 2320 LLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2398
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1781-1890 |
2.66e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.64 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1781 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLTEKLAAISEATRLKTEAEIA-LKEKEAE 1851
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 40849888 1852 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA 1890
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKA 247
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1328-1550 |
2.71e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.90 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1328 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAELEARELQRRMQ-----EEVTRREEAA 1397
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQkregtEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1398 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER-SRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEA 1476
Cdd:PRK07735 93 AKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1477 QKRQAQEEAER---LRRQVQDESQRKRQAEAELALRVKAEAEAAR-EKQRALQ----ALDELKLQAEEAERRLRQAEAER 1548
Cdd:PRK07735 173 AKAKAAALAKQkaaEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAlAKQKASQgngdSGDEDAKAKAIAAAKAKAAAAAR 252
|
..
gi 40849888 1549 AR 1550
Cdd:PRK07735 253 AK 254
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2161-2615 |
2.73e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2161 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAEN 2240
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2241 RALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2320
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2321 LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2400
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2401 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2480
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2481 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQE 2560
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2561 ELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKAL 2615
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2214-2461 |
2.79e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2214 QVEEELFSVRVQMEELGKlkARIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEAARLsvAAQEAAR--LRQLAEedla 2291
Cdd:COG3096 438 NAEDYLAAFRAKEQQATE--EVLELEQK---LSVADAARRQFEKAYELVCKIAGEVERS--QAWQTARelLRRYRS---- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2292 qQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ--EDKEQMAQQLVEETQGFQRTLEAERQRQLEMSA 2369
Cdd:COG3096 507 -QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2370 EAERLKLRMAEMsRAQARAEEDAQ-RFRKQAEEIGEklhrtELATQEKVT--LVQTLEIQRQQSdQDAERLREAIAELER 2446
Cdd:COG3096 586 QLEQLRARIKEL-AARAPAWLAAQdALERLREQSGE-----ALADSQEVTaaMQQLLEREREAT-VERDELAARKQALES 658
|
250 260
....*....|....*....|
gi 40849888 2447 EKEKLKQ-----EAKLLQLK 2461
Cdd:COG3096 659 QIERLSQpggaeDPRLLALA 678
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1666-2044 |
2.83e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 47.32 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1666 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQHEATAATQK 1738
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1739 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1813
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1814 ARQRAEAERvlteklaaiSEATRL---KTEAEIA---------LKEKEAENERLRRLAEDEAFQRRR---LEEQAAQHKA 1878
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAeeeakrradAKLKEAVEKNVATSEQDKPKRRAKrgvLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1879 DIEErlaqlrKASESELERQKgLVEDTLRQRRQVEEEIMALKASFEKAAAGKAE------------LELELGriRSNAED 1946
Cdd:NF033838 280 ENDA------KSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEIA--ESDVKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1947 TMRSKELAEQEAARQRqlaaeeeqrrreaeervqrslaaEEEAARQRKvalEEVERLKA---KVEEARRLRERAEQESAR 2023
Cdd:NF033838 351 KEAELELVKEEAKEPR-----------------------NEEKIKQAK---AKVESKKAeatRLEKIKTDRKKAEEEAKR 404
|
410 420
....*....|....*....|.
gi 40849888 2024 QLQLAQEAAQKRLQAEEKAHA 2044
Cdd:NF033838 405 KAAEEDKVKEKPAEQPQPAPA 425
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1373-1710 |
2.83e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1373 AQAELEARELQRRMQEEVTR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQl 1450
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1451 ETTERQRggaEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA--REKQRALQALD 1528
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwsTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1529 ELKLQAEEAERRLRQAEAERarqvQVALETAQRSAEVELQSKrASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAE 1608
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKE----EVKDEKIKKEKKVKYESK-VFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1609 AERAREEAERELERWQlkANEALRLRLQA--EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQElekq 1686
Cdd:pfam02029 233 SQEREEEAEVFLEAEQ--KLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE---- 306
|
330 340
....*....|....*....|....
gi 40849888 1687 RQLAEGTAQQRLaaEQELIRLRAE 1710
Cdd:pfam02029 307 RKLREEEEKRRM--KEEIERRRAE 328
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1642-1788 |
2.83e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.97 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1642 QQKSLAQA--DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQR 1718
Cdd:pfam17045 101 QRKQLKEAreEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1719 QLLEEELARLQH-----EATAATQKRQELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1788
Cdd:pfam17045 181 QCLEASQSEIQRlrsklERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2150-2403 |
2.85e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2150 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-----VEEELFSVRV 2224
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvareLLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2225 QMEELGKLKARI-EAENRaliLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2303
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2304 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLveeTQGFQRTLEAERQRQLEMSAEAERLKLRMAE 2380
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 40849888 2381 MSRAQARAEEDAQRFRKQAEEIG 2403
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3749-3785 |
2.94e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.94e-04
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 3749 RLLSAERAVTGYRDPYTEQPISLFQAMKKELIPAEEA 3785
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2170-2597 |
3.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2170 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEaENRALILRDK 2248
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2249 DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAArLRQLAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQQQ 2324
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2325 KELAQEQARRLQEDkeqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2404
Cdd:PRK02224 351 ADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2405 KLH--RTELATQEKVT-----------------------LVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ 2459
Cdd:PRK02224 427 REAelEATLRTARERVeeaealleagkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2460 LKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERfieQEKAKLEQLFQD--EVAKAKQLQEEQQRQQQQMEQEKQEL 2537
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEELR---ERAAELEAEAEEkrEAAAEAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2538 VASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQRL---RERLQRLEEEHRAA 2597
Cdd:PRK02224 584 LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLaekRERKRELEAEFDEA 646
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1690-2186 |
3.47e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.16 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1690 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV----------RAEMEVLLAS 1759
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1760 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKT 1839
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1840 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 1919
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1920 KASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE 1999
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2000 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLERLRSEAEAARRAA 2079
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2080 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2159
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 40849888 2160 KKFAEQTLRQKAQVEQELTTLRLQLEE 2186
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2147-2351 |
3.55e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.21 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAaDAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR----------S 2213
Cdd:PRK11281 50 KQKLL-EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2214 QVEE-------------------------------ELFSVRVQMEELGKLKARIEAENRALI--LRDKDNT-QRFLEEEA 2259
Cdd:PRK11281 129 RLAQtldqlqnaqndlaeynsqlvslqtqperaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAeQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2260 EKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElLQQQKELAQEQARR 2334
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEIN 287
|
250
....*....|....*..
gi 40849888 2335 LqedkeQMAQQLVEETQ 2351
Cdd:PRK11281 288 L-----QLSQRLLKATE 299
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3046-3080 |
3.68e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|....*
gi 40849888 3046 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEM 3080
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2427-2553 |
3.78e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2427 RQQSDQDAERLREAIAELEREKEKLKQEAKLLqlkseemqtvqqEQILQETQALQKSFLSEKDSLLQRErfiEQEKAKLE 2506
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAE 572
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 40849888 2507 QLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVAS--MEEARRRQREAEE 2553
Cdd:PRK00409 573 KEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAheLIEARKRLNKANE 621
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1691-2040 |
3.87e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1691 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1770
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1771 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA 1850
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1851 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGK 1930
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1931 AELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEA 2010
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 40849888 2011 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2040
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1005-1697 |
3.89e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1005 ARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISLVI 1084
Cdd:PRK10246 256 QQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1085 RSTQGAEEVLKTHEEHLKEAQAVPATLQELevtkaslkklrAQAEAQQPVFNTLRDELRG-----AQEVGERLQQRhger 1159
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR---- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1160 dveveRWRERVTQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLSSWLQDAKSRQEQIQAvpiANSQAAR 1234
Cdd:PRK10246 384 -----QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNVTQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1235 EQLRQEKALLEEIERHGEKVEE-------CQKFAKqyinaIKDYElqliTYKAQLEPvASPAkkPKVQSGSESVIQEYVD 1307
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLE----AQRAQLQA-GQPC--PLCGSTSHPAVEAYQA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1308 LRtryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAE----------L 1377
Cdd:PRK10246 523 LE----------------PGVNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEqaltqqwqavC 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1378 EARELQRRMQEEVTRREEAAVDAQQQKRSIQEelQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETterq 1456
Cdd:PRK10246 586 ASLNITLQPQDDIQPWLDAQEEHERQLRLLSQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLPQ---- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1457 rggAEDELQALRARAEEAeAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEE 1536
Cdd:PRK10246 660 ---EDEEASWLATRQQEA-QSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQT 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1537 AERRLRQaEAERARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvTVTQLREEAERRAQQQAEAERAREEA 1616
Cdd:PRK10246 736 LQQQDVL-EAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQT 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1617 ERELERWQLKANEALRLRLQAEEVAQQksLAQadaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQ 1696
Cdd:PRK10246 804 AQALAQHQQHRPDGLDLTVTVEQIQQE--LAQ---------------LAQQLRENTTRQGEIRQQ----LKQDADNRQQQ 862
|
.
gi 40849888 1697 R 1697
Cdd:PRK10246 863 Q 863
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1388-1872 |
3.97e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1388 EEVTRREEAAVDAQQQK--RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAED-EL 1464
Cdd:NF033838 53 NESQKEHAKEVESHLEKilSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1465 QALRARAEEAEAQK------RQAQEEAERLRRQVQDESQRKRQAE-AELALRVKaEAEAAREKQRALQALDELKLQAEEA 1537
Cdd:NF033838 133 DTLEPGKKVAEATKkveeaeKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1538 ERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaektaqlertlqeehvtvtqlreeaerraqqqaeaerareeae 1617
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAK----------------------------------------------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1618 relERWQLKANEALRLRLQAEEVAQQKSLAQADAeKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1697
Cdd:NF033838 239 ---RRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE--AEKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1698 LAAEQElirlRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQR 1777
Cdd:NF033838 313 VEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQAKAKVESK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1778 LeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1857
Cdd:NF033838 382 K-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK 446
|
490
....*....|....*..
gi 40849888 1858 LAEDEAFQ--RRRLEEQ 1872
Cdd:NF033838 447 PADQQAEEdyARRSEEE 463
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1420-1553 |
4.02e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.82 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1420 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1499
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1500 RQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1553
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE 186
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1667-2047 |
4.23e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 46.57 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQRELAEQElekQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElarlqheataATQKRQELEAEL 1746
Cdd:COG3064 9 AAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1747 AKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE 1826
Cdd:COG3064 76 AKKLAE-----AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1827 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 1906
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1907 RQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAE 1986
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1987 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVV 2047
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1362-1731 |
4.45e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1362 RQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEE 1441
Cdd:pfam13868 13 SKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1442 EirvvrlqlettERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ 1521
Cdd:pfam13868 93 Y-----------EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1522 RALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQrsaevelqskrasfAEKTAQLERTLQEEHvtvtqlreeaer 1601
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------------AERDELRAKLYQEEQ------------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1602 raqqQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQ 1681
Cdd:pfam13868 216 ----ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 40849888 1682 ELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1731
Cdd:pfam13868 292 RRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2170-2354 |
4.70e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.65 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2170 KAQVEQELTTLRLQLEETDHQKsiLDEELQRLKAEVTEAarqrsqVEEELFSV----RVQMEELGKLKARIEAENRALIl 2245
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKR--CQALLQELSAPLEEK------ISQGSYSVpggyQLYLEDREKLVEKYRQVPRKGV- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2246 RDKDNTQRFLEEEA--------------EKMKQVAEEAARLSVAAQEAARL----RQLAEEDLAQQRALAE--KMLKEKM 2305
Cdd:cd16269 167 KAEEVLQEFLQSKEaeaeailqadqaltEKEKEIEAERAKAEAAEQERKLLeeqqRELEQKLEDQERSYEEhlRQLKEKM 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 40849888 2306 QavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLVEETQGFQ 2354
Cdd:cd16269 247 E--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1464-1553 |
4.70e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1464 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALDELKLQAEEAERRLRQ 1543
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 40849888 1544 AEAERARQVQ 1553
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
952-1378 |
4.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 952 RHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKDPAR--ECAQRIAEQQKAQAEVEG 1024
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1025 LGKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEHLKEA 1104
Cdd:COG4717 168 LEAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1105 QAVPATLQELEVTKAslkklRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVeveRWRERVTQLLERWQAVLAQT 1184
Cdd:COG4717 243 ERLKEARLLLLIAAA-----LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1185 DVRQRELEQLGRQLRYYRE-SADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQE-KALLEEIerHGEKVEECQKFAK 1262
Cdd:COG4717 315 ELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1263 QYiNAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET---LRRMEEEERL 1339
Cdd:COG4717 393 QA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGEL 471
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 40849888 1340 AE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE 1378
Cdd:COG4717 472 AEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3375-3410 |
4.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.89e-04
10 20 30
....*....|....*....|....*....|....*.
gi 40849888 3375 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3410
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1107-1519 |
4.94e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1107 VPATLQELEVTKASLKKLRAQAEAQQPVFNTLRDELRGaqevgerlqqrhgerdveverwrervtqLLERWQAVLAQTDV 1186
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAG----------------------------LTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1187 RQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEierhgekveecqkfAKQYIN 1266
Cdd:pfam19220 88 LVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREE--------------AQAAEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1267 AIKDYELQLITYKAQLEPVAspAKKPKVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQ 1343
Cdd:pfam19220 154 ALQRAEGELATARERLALLE--QENRRLQALSEEQAAELAELTRRLAELETQldaTRARLRALEGQLAAEQAERERAEAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1344 RAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLrqssEAEIQ 1423
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL----EADLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1424 AKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqae 1503
Cdd:pfam19220 308 RRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRLKEELQRER--- 384
|
410
....*....|....*.
gi 40849888 1504 AELALrVKAEAEAARE 1519
Cdd:pfam19220 385 AERAL-AQGALEIARE 399
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2718-2751 |
4.99e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.99e-04
10 20 30
....*....|....*....|....*....|....
gi 40849888 2718 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2751
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
919-1491 |
5.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 919 ELHYQAFLRDSQDAGGFGPEDRLvaEREYGSCSRHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLR 997
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQF--SQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLR 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 998 LPLD-------------KDPARECAQRIAEQQKA-QAEVEGLGKgVARLSAEAEKVLAL-----PEPSPAAPTL----RS 1054
Cdd:pfam15921 419 RELDdrnmevqrleallKAMKSECQGQMERQMAAiQGKNESLEK-VSSLTAQLESTKEMlrkvvEELTAKKMTLesseRT 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1055 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvLKTHEEHLKEAQavpatlqelevtkASLKKLRAQAEAQQPV 1134
Cdd:pfam15921 498 VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQH-LKNEGDHLRNVQ-------------TECEALKLQMAEKDKV 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1135 FNTLRDELRG-AQEVGErlqqrHGerdveverwRERVTQLLERWQavlAQTDVRQRELEqlgrqLRYYRESADPLSSWLQ 1213
Cdd:pfam15921 564 IEILRQQIENmTQLVGQ-----HG---------RTAGAMQVEKAQ---LEKEINDRRLE-----LQEFKILKDKKDAKIR 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1214 DAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVEECQkfaKQYINAIKDYELQLITYKAQLEPVASPAKKPK 1293
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1294 VQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAHAQAKA 1373
Cdd:pfam15921 699 MQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA-------------MKVAMGMQKQITAKRGQIDA 745
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1374 qaelearelqrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQL 1450
Cdd:pfam15921 746 ------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQelsTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 40849888 1451 ETTERQRGGAEDELQalraraeeaeaqkRQAQEEAeRLRRQ 1491
Cdd:pfam15921 814 DKASLQFAECQDIIQ-------------RQEQESV-RLKLQ 840
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1667-1810 |
5.26e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEATAATQKRQELEAE 1745
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1746 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAE-EAKRQRQLAE 1810
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNElEIAKAKELADiEATKFERIVE 795
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1674-1934 |
5.59e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1674 RQREL------AEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqheataatqkrQELEAelA 1747
Cdd:COG0497 142 AQRELldafagLEELLEEYREAY----RAWRALKKELEELRADEAERARELDLLRFQL--------------EELEA--A 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1748 KVRAEMEVLLaskaraEEEsrstseksKQRLEAeAGRFRELAEEAarLRALAEEakrqrqlaEEDAARQRAEAERVLtEK 1827
Cdd:COG0497 202 ALQPGEEEEL------EEE--------RRRLSN-AEKLREALQEA--LEALSGG--------EGGALDLLGQALRAL-ER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1828 LAAISE-----ATRLkTEAEIALKEKEAEnerLRRLAEDEAFQRRRLEEqaaqhkadIEERLAQLRKaseseLERQKGL- 1901
Cdd:COG0497 256 LAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSLEFDPERLEE--------VEERLALLRR-----LARKYGVt 318
|
250 260 270
....*....|....*....|....*....|...
gi 40849888 1902 VEDTLRQRRQVEEEIMALKASFEKAAAGKAELE 1934
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELA 351
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1332-1448 |
5.76e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1332 RMEEEERLAEQQRAEERERLAEVEA---ALEKQ-RQLAEAHAQAKAQAELEARELQRRMQEEV------TRREEAAVDAQ 1401
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKlkeELEEKkEKLQEEEDKLLEEAEKEAQQAIKEAKKEAdeiikeLRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 40849888 1402 QQKRSIQEELQHLRQSSeaEIQAKAQQVEAAERSRMRIEEEIRVVRL 1448
Cdd:PRK00409 604 VKAHELIEARKRLNKAN--EKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2292-2629 |
6.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2292 QQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLveETQGFQRTLEAERQRQLEMSAEA 2371
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2372 ERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDQDAERLREAIAELEREKEKL 2451
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2452 KQEAKLLQLKSEEMQTVQQEQILQETQ----------------------------------ALQKSFLSEKDSLLQRERF 2497
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2498 IEQEKAKLEQLFQDEVAKAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQrleqqrqqQEKLLA 2577
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--------IAALLA 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 40849888 2578 EENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKALPNGRDALDGPSMEA 2629
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE 429
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1813-2024 |
6.30e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1813 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 1892
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1893 SELERQKGLVEDTLR--QRRQVEEEIMALKASFEKAAAGKA---------ELELELGRIRSNAEDTMRSKELAEQEAARQ 1961
Cdd:COG4942 97 AELEAQKEELAELLRalYRLGRQPPLALLLSPEDFLDAVRRlqylkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1962 RQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQ 2024
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1421-1570 |
6.44e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1421 EIQAKAQQVEAAERSrMRIEEEIRvvrlqlETTERQRggAEDELQALRARAEEAEAQ-KRQAQEEAERLRRQVQDESQRK 1499
Cdd:PTZ00491 658 EITTKSQEAAARHQA-ELLEQEAR------GRLERQK--MHDKAKAEEQRTKLLELQaESAAVESSGQSRAEALAEAEAR 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1500 R-QAEAEL--------ALRVKAEAEAAREKQRALQALDELKLQAE---EAERRLRQAEAERARQVQVAL--ET--AQRSA 1563
Cdd:PTZ00491 729 LiEAEAEVeqaelrakALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATKFERIVEALgrETliAIARA 808
|
....*..
gi 40849888 1564 EVELQSK 1570
Cdd:PTZ00491 809 GPELQAK 815
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2168-2599 |
6.46e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.90 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2168 RQKAQVEQELTTLRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2244
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2245 LRDKDNTQRFLEEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2323
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2324 QKELAQEQARRLQEDKEQMAQQLVEE--TQGFQ----RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2397
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERmsAKGLQmelsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2398 QAEEIG----------EKLHRTELATQEKVTLVQTleiqRQQSDQDAERLREAIAELEREKEKLKQEAKLL--------- 2458
Cdd:pfam07111 427 AVARIPslsnrlsyavRKVHTIKGLMARKVALAQL----RQESCPPPPPAPPVDADLSLELEQLREERNRLdaelqlsah 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2459 -----------QLKSEEMQTV----QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ-LFQDEVAKAKQLQEE 2522
Cdd:pfam07111 503 liqqevgrareQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2523 QQRQQQQMEQEKQELVASMEEARRRQREAEEGVR----RKQEELQRLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAL 2598
Cdd:pfam07111 583 VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRqiqhRATQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLML 662
|
.
gi 40849888 2599 A 2599
Cdd:pfam07111 663 A 663
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2225-2523 |
6.47e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2225 QMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2304
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2305 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMS 2382
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2383 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlks 2462
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 2463 EEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLQEEQ 2523
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1359-1580 |
6.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1359 EKQRQLAEAHAQ-AKAQAELEArelqrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQS-SEAEIQAKAQQVEAAERSR 1436
Cdd:COG3883 20 AKQKELSELQAElEAAQAELDA------LQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1437 MRIEEEIRVVRL--------------QLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1502
Cdd:COG3883 94 ALYRSGGSVSYLdvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1503 EAELAlrvkaeaeaarEKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1580
Cdd:COG3883 174 EAQQA-----------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2679-2715 |
7.11e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 2679 RYLKGGSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA 2715
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1162-1402 |
7.12e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1162 EVERWRERVTQLLERWQAVLAQTDVRQREL------EQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAARE 1235
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1236 QLRQ-----EKALLEEIERHGEKVEECQKFAKQyinAIKDYELQLITYKAQLEPVASPAK---------KPKVQSGSESV 1301
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1302 IQEYVDLRTRYSELTTL--TSQYIKFISETLRRMEE--------EERLAEQQRAEERERLAEVEAAL---EKQRQLAEAH 1368
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSqeREEEAEVFLEAEQKLEElrrrrqekESEEFEKLRQKQQEAELELEELKkkrEERRKLLEEE 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 40849888 1369 AQAKAQAELEAR----ELQRRMQEEVTRREEAAVDAQQ 1402
Cdd:pfam02029 297 EQRRKQEEAERKlreeEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1684-1957 |
7.37e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 45.23 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1684 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1760
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1761 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1820
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1821 ErvLTEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASES 1893
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1894 ELERQKGLVEDTLRQRrqVEEEIMAlkasfekaaagKAELELELGRIRsnaedtmrsKELAEQE 1957
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEETEDA-----------KNKLEWQLKKTL---------QEIAELE 278
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2161-2328 |
7.49e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2161 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSVRVQMEEL----------- 2229
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALrsylspnspqv 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2230 GKLKARIEAenralilrdkdntqrfLEeeaekmKQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAV 2308
Cdd:COG3524 252 RQLRRRIAA----------------LE------KQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAAL 309
|
170 180
....*....|....*....|
gi 40849888 2309 QEAtrlKAEAEllQQQKELA 2328
Cdd:COG3524 310 EQA---RIEAA--RQQRYLA 324
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1670-1865 |
7.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1670 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1746
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1747 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAE-AGRFRELAEEAARLRALAEEAKRQRQLAE 1810
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQiAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1811 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1865
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1740-1925 |
7.63e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1740 QELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1819
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDE------------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1820 AERvLTEKLAAISEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQK 1899
Cdd:COG1579 75 IKK-YEEQLGNVRNNKEYE-----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*.
gi 40849888 1900 GLVEDTLRQRRQVEEEIMALKASFEK 1925
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPP 174
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1723-1946 |
7.64e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1723 EELARLQHEATAATQKRQELEaelaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLralaeEA 1802
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRK----KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ----KKQAEEAAKQ-----AA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1803 KRQRQlAEEDAARQRAEAervlteKLAAISEATRLKTEAEIALKEKEA-ENERLRRLAEDEAfQRRRLEEQAAQHKADIE 1881
Cdd:PRK09510 129 LKQKQ-AEEAAAKAAAAA------KAKAEAEAKRAAAAAKKAAAEAKKkAEAEAAKKAAAEA-KKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 1882 ERLAQLRKASESELERQKGLVEdtlrQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAED 1946
Cdd:PRK09510 201 KKAEAEAKKKAAAEAKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2284-2514 |
7.72e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.32 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2284 QLAEEDLAQQRALAEKMLKEKmqavqeatrlkaEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2363
Cdd:COG4487 18 SLYADIVKQRRAEFEKELAER------------LADAAKREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2364 QLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQsdqdaerlreaiaE 2443
Cdd:COG4487 86 ALAVAEEKEK---ELAALQEALAEKDAKLAELQAKELELLKKERELEDAKRE---AELTVEKERDE-------------E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 2444 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQetqalqksflsekdsllQRERFIEQEKAKLEQLFQDEVA 2514
Cdd:COG4487 147 LDELKEKLKKEEEEKQLAEKSLKVAEYEKQLK-----------------DMQEQIEELKRKKEQGSTQLQG 200
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1394-1806 |
7.89e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1394 EEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSrmrIEEEIRVVrlqlettERQRGGAEDELQALRARAEE 1473
Cdd:pfam02029 4 EEEA--ARERRRRAREERRRQKEEEEPSGQVT-ESVEPNEHN---SYEEDSEL-------KPSGQGGLDEEEAFLDRTAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1474 AEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQ 1553
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIA---DEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1554 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVtvtqlreeaerraqqqaeaerareeaereleRWQLKANEALRL 1633
Cdd:pfam02029 148 EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKI-------------------------------KKEKKVKYESKV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1634 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAeeqavrqrelaeqelekQRQLAEGTAQQRLAAEQELIRLRaeteq 1713
Cdd:pfam02029 197 FLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLS-----------------QSQEREEEAEVFLEAEQKLEELR----- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1714 geQQRQLLEEElarlqhEATAATQKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRfRELAEEAA 1793
Cdd:pfam02029 255 --RRRQEKESE------EFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK-RRMKEEIE 323
|
410
....*....|...
gi 40849888 1794 RLRALAEEaKRQR 1806
Cdd:pfam02029 324 RRRAEAAE-KRQK 335
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1331-1587 |
8.01e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.91 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAELEarelqrrmqeevtrREEAAVDAQQQKRSIQE 1409
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1410 ELQhLRQSSEAEIQAKAQQVEAAERSR----MRI--------------EEEIRVVRLQLETTERQ---RGGAEDEL-QAL 1467
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARvdleAKIeslkeelaflkknhEEEVRELQAQVSDTQVNvemDAARKLDLtSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1468 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA-LDELKLQAEEAERRLRQAEA 1546
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIeLQSLKKQKASLERQLAETEE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 40849888 1547 ERARQvqvaLETAQRSaeveLQSKRASFAEKTAQLERTLQE 1587
Cdd:pfam00038 253 RYELQ----LADYQEL----ISELEAELQETRQEMARQLRE 285
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2295-2517 |
8.41e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2295 ALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAE-RQRQLEMSAEAER 2373
Cdd:COG3883 12 AFADPQIQAKQKELSE---LQAELEAAQAELDALQAELEELNEEYNE-LQAELEALQAEIDKLQAEiAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2374 LKLRMAEMSRAQARAEEDAQRFrkQAEEIGEKLHRteLATQEKVTLVQTLEIQRQQSDQdaERLREAIAELEREKEKLKQ 2453
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLL--GSESFSDFLDR--LSALSKIADADADLLEELKADK--AELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 2454 EAKLLQLKSEEMQTVQQEQilqetQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2517
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQ-----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1696-1851 |
8.43e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1696 QRLAAEQELIRlRAETEQGEQQRQLlEEELARLQHEATAATQKRQELEAELAkvraEMEVLLASKARAEEESRSTSEKSK 1775
Cdd:PRK00409 495 KRLGLPENIIE-EAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1776 QRLEAEAgrfrelaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1851
Cdd:PRK00409 569 EEAEKEA--------QQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1314-1553 |
8.72e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 45.75 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1314 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAELEarELQRRMQE-EVTR 1392
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRAEAQQMLS--QLQQMLENlQAGQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1393 REEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQAL 1467
Cdd:pfam13779 594 PQQQQQQGQSEMQQAMDELGDLLReqqqlLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1468 RARAEEAEAQKRQAQEEAERLRRQVQ-DESQRKRQA-----EAELALRVKAEAEAAREKQRALQALdelklqaEEAERRL 1541
Cdd:pfam13779 674 GDLAERQQALRRRLEELQDELKELGGkEPGQALGDAgramrDAEEALGQGDLAGAVDAQGRALEAL-------RKGAQQL 746
|
250
....*....|..
gi 40849888 1542 RQAEAERARQVQ 1553
Cdd:pfam13779 747 AEAMQQQQGQGQ 758
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1875-2293 |
9.11e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.50 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1875 QHKADIEERLAQlRKASESELERQKGLVEDTLRQ---RRQVEEEIMALKASFEKAAAGKAELElELGRIRSNAEDTMRSK 1951
Cdd:pfam17380 279 QHQKAVSERQQQ-EKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQE-RMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1952 ElaeqeaaRQRQLaaeeeqrrreaeervqrslaaeeEAARQRKVALE-----EVERLKAKvEEARRLRERAEQESARQLQ 2026
Cdd:pfam17380 357 E-------RKREL-----------------------ERIRQEEIAMEisrmrELERLQME-RQQKNERVRQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2027 LAQEAAQKRLQAEEKAHAFVvqqreeelqqtlqqeqnmlerlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERl 2106
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQI--------------------------------------------------RAEQEEARQ- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2107 kqsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQaadaEMEKHKKFAEQTLRQKAQVEQElttLRLQLEE 2186
Cdd:pfam17380 435 ------------------REVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELEKE---KRDRKRA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2187 TDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvqMEELGKlkaRIEAENRALILRDKDNTQRFLEEE---AEKMK 2263
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRKLLEKE-------MEERQK---AIYEEERRREAEEERRKQQEMEERrriQEQMR 559
|
410 420 430
....*....|....*....|....*....|
gi 40849888 2264 QVAEEAARLSVAAQEAARLRQLAEEDLAQQ 2293
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2147-2454 |
9.45e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2226
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EELGKLKArieaenralILRDKdntqrFLEEEAEKmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2306
Cdd:pfam15905 132 LELTRVNE---------LLKAK-----FSEDGTQK---------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2307 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2386
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2387 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQE 2454
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1084-1769 |
9.72e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1084 IRSTQGAEEVLKTHEEHLKEAQAVPATLQE-LEVTKASLKKLRAQAEAQqpvFNTLRDELRGAQEVG-ERLQQRHGERDV 1161
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEeRQETSAELNQLLRTLDDQ---WKEKRDELNGELSAAdAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1162 EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEK 1241
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1242 AL-LEEIERHGEKVE-ECQKFAKQYINAIKDYELQLITYKAQL-----EPVASPAKKPKVQSGSESVIQEYVDLRTRYSE 1314
Cdd:pfam12128 407 DRqLAVAEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELklrlnQATATPELLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1315 LTTLTSqyikfisetlrrmeeEERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQA------------------ 1375
Cdd:pfam12128 487 VERLQS---------------ELRQARKRRDQASEALRQASRRLEERQSaLDELELQLFPQAgtllhflrkeapdweqsi 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1376 -ELEARELQRR--MQEEVTrreEAAVDAQQQKRSIQEELQHLR----QSSEAEIQAKAQQVE----AAERSRMRIEEEIR 1444
Cdd:pfam12128 552 gKVISPELLHRtdLDPEVW---DGSVGGELNLYGVKLDLKRIDvpewAASEEELRERLDKAEealqSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1445 VVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAE---LALRVKAEAEAAREK 1520
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAnERLNSLEAQlkqLDKKHQAWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1521 QRALQALDELKLQAEEAER-----RLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEEHVTVTQL 1595
Cdd:pfam12128 709 KREARTEKQAYWQVVEGALdaqlaLLKAAIAARRSGAKAELKALETWYKRDLASLGVD-PDVIAKLKREIRTLERKIERI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1596 REEAERRAQQQAEAErareeaerelERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQ 1675
Cdd:pfam12128 788 AVRRQEVLRYFDWYQ----------ETWLQ---RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1676 RELAEQELEKQRQLAEGTAQQRLAAEQElirlRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1755
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDANSE----QAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLA 929
|
730
....*....|....
gi 40849888 1756 LLASKARAEEESRS 1769
Cdd:pfam12128 930 ETWESLREEDHYQN 943
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1671-2582 |
9.95e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1671 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVR 1750
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1751 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1822
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1823 VLTEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASESELERQK 1899
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1900 GLVEDTLRQRRQVEEEIMALK---ASFEKAAAG-KAELELELGRIRSNAEDTMRSKE-LAEQEAARQRQLAAEEEQRRRE 1974
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKfviKELQQLEGSsDRILELDQELRKAERELSKAEKNsLTETLKKEVKSLQNEKADLDRK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1975 AEervqrSLAAEEEAARQRKVALEEVERL-KAKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAF-----VVQ 2048
Cdd:TIGR00606 517 LR-----KLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKskeinQTR 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2049 QREEELQQTLQQEQNMLERLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLR 2128
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFIT 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2129 KEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA 2208
Cdd:TIGR00606 671 QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK-STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2209 ARQRSQVEEELFSVRVQMEELGKLKARIEAENRA--LILRDKDNTQRFLEEEAEKMKQVAEEAARL-----SVAAQEAAR 2281
Cdd:TIGR00606 750 RNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2282 LRQLAEEDL---AQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQedkeQMAQQLVEETQGFQRTLE 2358
Cdd:TIGR00606 830 EKQEKQHELdtvVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIR 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2359 AERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT-LEIQRQQSDQDAERL 2437
Cdd:TIGR00606 903 EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTV 982
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2438 REAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQETQALQKsfLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAK 2517
Cdd:TIGR00606 983 NAQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRK--RENELKEVEEEL-----KQHLKEMGQMQVLQMK 1053
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2518 QLQeeqqrqqqqmeqekQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAEENQR 2582
Cdd:TIGR00606 1054 QEH--------------QKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1055-1589 |
1.04e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1055 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKthEEHLKEAQAVPATLQELEVTKASLKKLRAQAEAQQPV 1134
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1135 FNTLRDELRgaQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ-LGRQLRYYRESADPLSSWLQ 1213
Cdd:pfam02463 472 DLLKETQLV--KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1214 DAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVEecQKFAKQYINAIKDYE-LQLITYKAQLEPVASPAK-- 1290
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL--KSIAVLEIDPILNLAqLDKATLEADEDDKRAKVVeg 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1291 ------------KPKVQSGSESVIQEYVDLRTRYSELTTLTS---QYIKFISETLRRMEEEERLAE-----------QQR 1344
Cdd:pfam02463 628 ilkdteltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSeltKELLEIQELQEKAESELAKEEilrrqleikkkEQR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1345 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA 1424
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1425 KAQQVEAAERS------RMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDES 1496
Cdd:pfam02463 788 VEEEKEEKLKAqeeelrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEE 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1497 QRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1576
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
570
....*....|...
gi 40849888 1577 KTAQLERTLQEEH 1589
Cdd:pfam02463 948 KEKEENNKEEEEE 960
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1303-1443 |
1.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1303 QEYVDLRTRYSELTTLtsqyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAREL 1382
Cdd:COG1579 38 DELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1383 QrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEI 1443
Cdd:COG1579 114 E--LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1341-1442 |
1.07e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.49 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1341 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaelEARELQRRMQEEVTRREEaaVDAQQQKRSIQEELQHLRQSSEA 1420
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 40849888 1421 EIQAKAQQVEAAERSRMRIEEE 1442
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1415-1594 |
1.07e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.72 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1415 RQSSEAEIQAKAQQVEA-AERSRMRIE-EEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERlRRQV 1492
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1493 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSK-- 1570
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTei 212
|
170 180
....*....|....*....|....
gi 40849888 1571 RASFAEKTAQLERTLQEEHVTVTQ 1594
Cdd:pfam00529 213 RAPVDGTVAFLSVTVDGGTVSAGL 236
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1329-1505 |
1.12e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1329 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---------LAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVD 1399
Cdd:PRK12678 45 GMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRaaraaaaarQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1400 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEirvvrlqlETTERQRGGAEDELQALRARAEEAEAQKR 1479
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREER 196
|
170 180
....*....|....*....|....*.
gi 40849888 1480 QAQEEAERLRRQVQDESQRKRQAEAE 1505
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRD 222
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1472-1551 |
1.16e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.33 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LDELKLQAEEAERRLRQA 1544
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 40849888 1545 EAERARQ 1551
Cdd:PRK11448 218 RKEITDQ 224
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1609-2038 |
1.19e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.39 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1609 AERAREEAERELERWQLKANEALRLRLQAEevaqqkSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1688
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLA------WLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1689 LAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1766
Cdd:COG3903 561 LREGRrwLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1767 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1846
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1847 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKA 1926
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1927 AAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2006
Cdd:COG3903 801 AAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAA 880
|
410 420 430
....*....|....*....|....*....|..
gi 40849888 2007 VEEARRLRERAEQESARQLQLAQEAAQKRLQA 2038
Cdd:COG3903 881 AAALLAAAAAAAAAAAAAAAAAAALAAAAAAA 912
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1387-1535 |
1.20e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 45.05 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1387 QEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAeiqAKAQQVEaaersrmrIEEEIRVVRLQLETTERQRGGAEDELQ- 1465
Cdd:pfam05911 680 TEENKRLKEEFEQLKSEKENLEVELASCTENLES---TKSQLQE--------SEQLIAELRSELASLKESNSLAETQLKc 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1466 ------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAE-LALRVKAEAEAAREKQRALQALDELKLQAE 1535
Cdd:pfam05911 749 maesyeDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKcLELQEQLERNEKKESSNCDADQEDKKLQQE 825
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1331-1501 |
1.21e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1331 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEARELQRRMQEEVTRREEAAVDAQQQKRSIQEE 1410
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPE-AAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1411 LQHLRQSSEAEIQAKAQQVEAAERSRMRieeeiRVVRLQLETTERQRGGaEDELQALRARAEEAEAQKRQAQEEAERLRR 1490
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 40849888 1491 QVQDESQRKRQ 1501
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1449-1912 |
1.23e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1449 QLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR--VKAEAEAAREKQRALQA 1526
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1527 LDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehVTVTQLREEAERRAQQQ 1606
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA--RAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1607 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1686
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1687 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1766
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1767 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1846
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1847 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1912
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2282-2456 |
1.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2282 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAER 2361
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2362 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAI 2441
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 40849888 2442 AELEREKEKL-KQEAK 2456
Cdd:PRK12704 172 AVLIKEIEEEaKEEAD 187
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1334-1589 |
1.24e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1334 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEA----------------------RELQRRMQEEVT 1391
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELkpsgqggldeeeafldrtakreERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1392 RREEAAVDAQQQKRSIQEELQHlRQSSEAEIQAKAQQVeaaERSRMRIEEEirvvrlqlETTERQRGGAEDELQALRARA 1471
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKEN-NEEEENSSWEKEEKR---DSRLGRYKEE--------ETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAEAQKRQAQEEAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREK-------QRALQALDELKLQAEEAERRLRQ 1543
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 40849888 1544 AEAERARQVQVaLETAQRSAEVELQSKRASFAE----KTAQLERTLQEEH 1589
Cdd:pfam02029 233 SQEREEEAEVF-LEAEQKLEELRRRRQEKESEEfeklRQKQQEAELELEE 281
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2196-2404 |
1.33e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 44.45 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2196 EELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKM-----KQVAEEAA 2270
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2271 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLV 2347
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 2348 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2404
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1710-1842 |
1.34e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1710 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1789
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1790 EEAARLRA-------------LAEEAKRQRQLAEEDAARQRAEAERVlTEKLAAISEATRLKTEAE 1842
Cdd:pfam05262 287 QIEIKKNDeealkakdhkafdLKQESKASEKEAEDKELEAQKKREPV-AEDLQKTKPQVEAQPTSL 351
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1325-1541 |
1.40e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.51 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1325 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR-REEAAVDAQQQ 1403
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKgNEELAREALAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1404 KRSIQeelqhlrqsseaeiqakaQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQE 1483
Cdd:pfam04012 92 KKSLE------------------KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1484 EAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQaLDELKLQAEEAERRL 1541
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1460-1527 |
1.54e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.65 E-value: 1.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1460 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR-----KRQAEAELA-LRVKAEAEAAREKQRALQAL 1527
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAErILEQAKAEIEQEKEKALAEL 115
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
29-132 |
1.54e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 29 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 86
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 40849888 87 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 132
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1472-1589 |
1.59e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1472 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQ 1551
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 40849888 1552 VQVALETAQRSAEVELQSKRASFAEKTAQL-ERTLQEEH 1589
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2198-2411 |
1.59e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2198 LQRLKAEVTEAARQRSQVEEElfsvrvQMEELGKLKARIEAENRALilrdkdNTQRFLEEEAEKMkqvAEEAARLSVAAQ 2277
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL------EKERLAAQEQKKQ---AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2278 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLVEETQGFQRT 2356
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2357 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2411
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1628-1850 |
1.60e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.85 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1628 NEALRLRLQ-AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--LAEGTAQQRLAAEQEl 1704
Cdd:COG5283 9 DKPFKSALEsAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQalDQAGIDTRQLSAAQR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1705 iRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVRAEME-----VLLASKARAEEESRSTSEKSKQRLE 1779
Cdd:COG5283 88 -RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR-LAGAGAAAAaigaaLAASVKPAIDFEDAMADVAATVDLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1780 AEAGRFRELAEEA----ARLRALAEE-AKRQRQLAEEDAARQRAEAervLTEKLAAISEATRLKTE--AEIALKEKEA 1850
Cdd:COG5283 166 KSSEQFKALGKQArelsAQTPQSADDiAAGQAALAQAGVSAEDILA---FTPTAAKLATAFDTDAEeaAEIAAKILNA 240
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1709-1836 |
1.68e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1709 AETEQGEQQRQLLEEELARLQHEATAATQKR-QELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQRLEAEAGRFRE 1787
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1788 LAEEAARLRALAEEAKRQRQLA--EEDAAR-------------QRAEAERVLT-------------EKLAAISEATR 1836
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEvtEEDIAEvvsrwtgipvgklLEGEREKLLNleeelhervigqdEAVEAVADAIR 566
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1228-1490 |
1.69e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1228 ANSQAAREQLRQEkalLEEIE-----RHGEKVEECQ-------------KFAKQYINAIKDYELQLITYKAQLEPVASPA 1289
Cdd:PRK10929 19 AATAPDEKQITQE---LEQAKaaktpAQAEIVEALQsalnwleerkgslERAKQYQQVIDNFPKLSAELRQQLNNERDEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1290 KKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEA 1367
Cdd:PRK10929 96 RSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1368 HAQAK---AQAELEARELQ-----------------RRMQEEVTRREEAAVDAQQQkrSIQEELQHLRQsSEAEiqakaq 1427
Cdd:PRK10929 170 LAQAQltaLQAESAALKALvdelelaqlsannrqelARLRSELAKKRSQQLDAYLQ--ALRNQLNSQRQ-REAE------ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1428 qvEAAERSRMRIEEEIRVVRLQLETTERQRggaedEL-QALRARAEEAE---AQKRQAQEEAERLRR 1490
Cdd:PRK10929 241 --RALESTELLAEQSGDLPKSIVAQFKINR-----ELsQALNQQAQRMDliaSQQRQAASQTLQVRQ 300
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1666-1847 |
1.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1666 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEATAATQKRQELEA 1744
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1745 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1823
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 40849888 1824 LTEKLAAISEATRLKTEAEIALKE 1847
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1710-1932 |
1.73e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1710 ETEQGEQQRQLLEEELARLQ-----------HEATAATQKRQELEAELAKVRAEMEV-----LLASKARAEEESRSTSEK 1773
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHgaeiskleeenREKEKALPKNDDMTIEEAKRRAAAAAkakaaALAKQKREGTEEVTEEEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1774 SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--AARQRAEAERVLTEKLAAISEATRLKTEAEIAL---KEK 1848
Cdd:PRK07735 91 AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAkaAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKakaKAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1849 EAENERLRRLAEDEAFQRRRLEEQAAQH-KADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEE-IMALKASFEKA 1926
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTEEeKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKaIAAAKAKAAAA 250
|
....*.
gi 40849888 1927 AAGKAE 1932
Cdd:PRK07735 251 ARAKTK 256
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1444-1595 |
1.75e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.98 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1444 RVVRLQLETTERQRGGAEDELQALRA-----RAEEAEAQKrQAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAR 1518
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGqiqqlRTELQELEA-QQQEEAESSREQLQE---LEEQLATERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1519 EKQRALQALDELKLQAEEAERRLRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVTVT 1593
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVL 198
|
..
gi 40849888 1594 QL 1595
Cdd:pfam09787 199 QL 200
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1321-1515 |
1.76e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1321 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEevtrreeaavda 1400
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1401 QQQKRSIQEELQHLRQSSEAEIQAKAQQvEAAERSRMRIEEEiRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQ 1480
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 40849888 1481 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1515
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1537-1738 |
1.80e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1537 AERRLRQAEAERARQVQVAlETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvtqlreeaerRAQQQAEAERAREEA 1616
Cdd:COG2268 199 RDARIAEAEAERETEIAIA-QANREAEEAELEQEREIETARIAEAEAELAKK-------------KAEERREAETARAEA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1617 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1696
Cdd:COG2268 265 EAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKR 344
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 40849888 1697 RLAAeqelirlrAETEQGEQQRQL-LEEELARLQHEATAATQK 1738
Cdd:COG2268 345 ALAE--------AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1407-1742 |
1.85e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1407 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAE 1486
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1487 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVE 1566
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1567 LQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1646
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1647 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1726
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*.
gi 40849888 1727 RLQHEATAATQKRQEL 1742
Cdd:COG4372 324 LAKKLELALAILLAEL 339
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1871-2044 |
1.89e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.09 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1871 EQAAQHKADIEERLAQLRKASESELERQKGLVED-TLRQRRQVEEEIMALKASfEKAAAgKAELELELGRIRSNAEdtmr 1949
Cdd:COG2268 192 RKIAEIIRDARIAEAEAERETEIAIAQANREAEEaELEQEREIETARIAEAEA-ELAKK-KAEERREAETARAEAE---- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1950 sKELAEQEAARQRQLAAEEeqrrreaeervqrslaaeEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQ 2029
Cdd:COG2268 266 -AAYEIAEANAEREVQRQL------------------EIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
170
....*....|....*.
gi 40849888 2030 -EAAQKRLQAEEKAHA 2044
Cdd:COG2268 327 aEAEAIRAKGLAEAEG 342
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2163-2341 |
1.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2163 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRSQVEEELFSVRVQME-ELGKLKARIEAENR 2241
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2242 ALilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2321
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|
gi 40849888 2322 QQQKELAQEQARRLQEDKEQ 2341
Cdd:COG3206 364 RELYESLLQRLEEARLAEAL 383
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1321-1499 |
1.94e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1321 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTR---REEAA 1397
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKarqRQELQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1398 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLeTTERQRGGAEDELQALRARAEEAEAQ 1477
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRELEKQIEEREEQRAAEREEELEEG 317
|
170 180
....*....|....*....|..
gi 40849888 1478 KRQAQEEAERLRRqVQDESQRK 1499
Cdd:pfam13868 318 ERLREEEAERRER-IEEERQKK 338
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2163-2411 |
1.98e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2163 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSVRVQMEELGK 2231
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2232 LKARIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedlaQQRALAEKMlkEKMQAVQ 2309
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2310 EATRLKAE--AELLQQQKELaqeqarrlqEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2387
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL---------RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....
gi 40849888 2388 AEEDAQRFRKQAEEIGEKLHRTEL 2411
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSL 404
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2252-2464 |
2.03e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2252 QRFleeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQ 2331
Cdd:PRK05035 453 ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2332 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLRMAEMSRAQAR-AEEDAQRFRKQ 2398
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 2399 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQLKSEE 2464
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1667-1807 |
2.05e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 43.43 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA-- 1744
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1745 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1807
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1341-1444 |
2.06e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.24 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1341 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARElqrrmQEEVTRREEAAVDAQQQKRS-IQEELQHLRQSSE 1419
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAAAA-----AEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40849888 1420 ----------------AEIQAkaqQVEAAERSRMRIEEEIR 1444
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2168-2494 |
2.09e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 44.51 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2168 RQKAQVEQELTTLRLQ-LEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVrVQMEE---LGKLKARIEAEN-RA 2242
Cdd:pfam15964 285 QHEAVLAQTHTNVHMQtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQA-VQMTEeanFEKTKALIQCEQlKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2243 LILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELL 2321
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2322 QQQKELAQEQAR-RLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMS-AEAERLKL-------RMAEMSRAQARAEEDA 2392
Cdd:pfam15964 442 SQEMDVTKVCGEmRYQLNQTKMKK---DEAEKEHREYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREEC 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2393 QRFrkqAEEIGEKLHRTELATQEKVTLVQTL----EIQRQQSDQDAERLREAIAELEREKE------------------K 2450
Cdd:pfam15964 519 LKL---TELLGESEHQLHLTRLEKESIQQSFsneaKAQALQAQQREQELTQKMQQMEAQHDktvneqyslltsqntfiaK 595
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 40849888 2451 LKQEAKLLQLKSEEMQTVQQEQILQETQalQKSFLSEKDSLLQR 2494
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQ--EKEYLQDRLEKLQK 637
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1464-1563 |
2.15e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1464 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALDelklqaEEAERR 1540
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 40849888 1541 LRQAEAERARQVQVALETAQRSA 1563
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2755-2791 |
2.16e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.16e-03
10 20 30
....*....|....*....|....*....|....*..
gi 40849888 2755 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2791
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1670-1813 |
2.24e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1670 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1749
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1750 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1813
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1378-1516 |
2.28e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1378 EARELQRRMqEEVTRREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1457
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1458 GGAEDELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1516
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2167-2464 |
2.31e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2167 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIeaenralil 2245
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2246 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2325
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2326 ELAQEQARRLQEDKEQMAQQLVEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2403
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2404 EKLHR--TELAT--QEKVTLVQTL-EIQRQQS---------------------------DQDAERLREAIAELEREKEKL 2451
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRNMEmlngqsvcpvcgttlgeeksnhiinhyNEKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 40849888 2452 KQEAKllQLKSEE 2464
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1624-1919 |
2.39e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1624 QLKANEALRLRLQAEEVAQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLA-EGTAQQRLAA 1700
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDE---MMEEERERALEEEEEKEEERKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1701 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1780
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEER-EEDERILEYLKEKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1781 EAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE 1849
Cdd:pfam13868 183 EREIARLRAQqekaqdekaerDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEE 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1850 AEN--ERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 1919
Cdd:pfam13868 263 FERmlRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3674-3712 |
2.46e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*....
gi 40849888 3674 YLYGTGSVAGVYLPGSRQTLTIYQALKKGLLSAEVARLL 3712
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2255-2393 |
2.47e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2255 LEEEA------EKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQ 2324
Cdd:PTZ00491 675 LEQEArgrlerQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAE 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 2325 KELAQEQARRLQEDKEQmaQQLVEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2393
Cdd:PTZ00491 752 AELEKLRKRQELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2337-2473 |
2.61e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2337 EDKEQMAQQLVEETQgfqRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigeklhrtELAT--- 2413
Cdd:COG1842 22 EDPEKMLDQAIRDME---EDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE--------DLAReal 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2414 QEKVTL---VQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLL--QLKSEEMQTVQQEQI 2473
Cdd:COG1842 91 ERKAELeaqAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEAL 155
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2329-2517 |
2.63e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 42.34 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2329 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHR 2408
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE--RELKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2409 TELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL-LQLKSEEMQTVQQEQ---ILQETQALQKSF 2484
Cdd:pfam15665 91 EAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkHRQEIQELLTTQRAQsasSLAEQEKLEELH 170
|
170 180 190
....*....|....*....|....*....|...
gi 40849888 2485 LSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2517
Cdd:pfam15665 171 KAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
41-131 |
2.64e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.75 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 41 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 113
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 40849888 114 DDIADGNPKLTLGLIWTI 131
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2322-2456 |
2.67e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2322 QQQKELAQEQARRLQEDKEQMAQQLVEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2395
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 40849888 2396 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDQDAERLREAIAelereKEKLKQEAK 2456
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1365-1553 |
2.76e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.74 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1365 AEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIR 1444
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1445 vvRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AELALRVKAEAEAAREKQRA 1523
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDRRDRREQGDRREERGRRD 222
|
170 180 190
....*....|....*....|....*....|
gi 40849888 1524 LQALDELKLQAEEAERRLRQAEAERARQVQ 1553
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
30-138 |
2.77e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.74 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 30 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 100
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 40849888 101 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 138
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1987-2471 |
2.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1987 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahAFVVQQREEELQQTLQQEQNMLE 2066
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2067 RLRSEaeaarraaeeaeeareqaereaaqsRKQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2146
Cdd:COG4717 150 ELEER-------------------------LEELRELEE--------------------ELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2147 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA-EVTEAARQRSQVEEELFSVRVQ 2225
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2226 MEELGKLKARIE---AENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQ---LAEEDLAQQRALAEK 2299
Cdd:COG4717 265 GGSLLSLILTIAgvlFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2300 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAqQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2379
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2380 EMSRAQarAEEDAQRFRKQAEEIGEKL--HRTELATQEkvtlvqtLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKL 2457
Cdd:COG4717 424 ALDEEE--LEEELEELEEELEELEEELeeLREELAELE-------AELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490
....*....|....
gi 40849888 2458 LQLKSEEMQTVQQE 2471
Cdd:COG4717 495 LKLALELLEEAREE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1873-2049 |
2.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1873 AAQHKADIEERLAQLRKasesELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKE 1952
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1953 LAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL-----------EEVERLKAKVEEARRLRERAEQES 2021
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 40849888 2022 ARQLQL--AQEAAQKRLQAEEKAHAFVVQQ 2049
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1352-1564 |
3.10e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.87 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1352 AEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEvtRREEAAVDAQQQKRSIQEEL---QHLRQSSEAEIQAKAQQ 1428
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPRQNNRRDRNE--RRDTRDNRTRREGRENREENrrnRRQAQQQTAETRESQQA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1429 VEAA-ERSRMRIEEEIRvvrlqletTERQRGGAEDELQA-LRARAEEAEAQKRQAQEEAERlRRQVQdesQRKRQAEAEL 1506
Cdd:PRK10811 660 EVTEkARTQDEQQQAPR--------RERQRRRNDEKRQAqQEAKALNVEEQSVQETEQEER-VQQVQ---PRRKQRQLNQ 727
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1507 ALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1564
Cdd:PRK10811 728 KVRIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEENNA 785
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1677-1873 |
3.20e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1677 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1755
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1756 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAER----VLTEK 1827
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKlrnqLTSKS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 40849888 1828 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 1873
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1708-1845 |
3.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 43.32 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1708 RAETEQGEQqrqlleEELARLQHEA-TAATQKrqelEAELAKVRAEMEVLLASKARAEEESRST--------SEKSKQRL 1778
Cdd:PRK12472 191 RAETLAREA------EDAARAADEAkTAAAAA----AREAAPLKASLRKLERAKARADAELKRAdkalaaakTDEAKARA 260
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40849888 1779 EAeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKlaaiSEATRLKTEAEIAL 1845
Cdd:PRK12472 261 EE---RQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKK----AETAKAATDAKLAL 320
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3009-3046 |
3.65e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 3.65e-03
10 20 30
....*....|....*....|....*....|....*...
gi 40849888 3009 LRGTSVIAGVWLEEAGQKLSIYEALRRDLLQPEVAVAL 3046
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2245-2418 |
3.65e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2245 LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2324
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2325 KELAQEQAR--------RLQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFR 2396
Cdd:pfam05262 257 AKNLPKPADtsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|..
gi 40849888 2397 kqaEEIGEKLHRTELATQEKVT 2418
Cdd:pfam05262 331 ---EPVAEDLQKTKPQVEAQPT 349
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2175-2456 |
3.74e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2175 QELTTLRLQLEETDHQKSILDEELQRLKaevteaaRQRSQVEEELFSVRVQMEEL-GKLKARIEAENRALILRDKDNtqr 2253
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK-------EKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELN--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2254 fleEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKEL 2327
Cdd:COG1340 71 ---EKVKELKEERDELnEKLNELREELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2328 AQE-QARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA----QARAEEDAQRFRKQAEEI 2402
Cdd:COG1340 146 EKElEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadelRKEADELHKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 2403 gEKLHRTELATQEKVTLVQTlEIQRQQSDQDAERLREAIAELEREKEKLKQEAK 2456
Cdd:COG1340 226 -DELHEEIIELQKELRELRK-ELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2227-2344 |
3.78e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2227 EELGKLKARIEAENRALILRDKDNTQrfLEEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2306
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 40849888 2307 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2344
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1460-1703 |
3.98e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1460 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqralqaLDELKLQAEEAER 1539
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAE-----------IDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1540 RLRQAEA---ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEA 1616
Cdd:COG3883 80 EIEERREelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1617 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1696
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
....*..
gi 40849888 1697 RLAAEQE 1703
Cdd:COG3883 240 AAAAASA 246
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1430-1547 |
4.02e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1430 EAAERSRMRIE---EEIRVVRLQLETTERQRGGAEDElqalraraeeaeaQKRQAQEEAERLRRQVQDESQRKRQAEAel 1506
Cdd:COG0542 397 EAAARVRMEIDskpEELDELERRLEQLEIEKEALKKE-------------QDEASFERLAELRDELAELEEELEALKA-- 461
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 40849888 1507 alRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAE 1547
Cdd:COG0542 462 --RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| antiphage_ZorA_2 |
NF033915 |
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel ... |
1697-1900 |
4.03e-03 |
|
anti-phage ZorAB system protein ZorA; Proteins of this subfamily are putative H+ channel proteins, but it has been reported that they are also involved in anti-phage defense.
Pssm-ID: 411476 [Multi-domain] Cd Length: 383 Bit Score: 42.83 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1697 RLAAEQELIRLRAETEQGEQQRQLLEEELA-RLQHEATAATQKRQE-LEAELAKVRAEMEVLLASkaraeeesrSTSEKS 1774
Cdd:NF033915 201 RIPAEQSLVHIAEYSKESKEALQELHERIGdRLQESLNGMSEAMQTaLTDALNNIMAPAIQTLVS---------TTSQQS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1775 KQRLEAEAGRFRElaeeaarlrALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRlkteaeialKEKEAENER 1854
Cdd:NF033915 272 TQVLESLVGNFMD---------GMTSAGREQGLQMQQ-AAADVNAAVSGMSERLNQLFNSLS---------EQQGRQMER 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 40849888 1855 LRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKG 1900
Cdd:NF033915 333 AQQQSSTFETQLQRLSGSANERQAQLEQRFEELMSGLTEQLQTQLG 378
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2280-2455 |
4.04e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2280 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLVEETQG 2352
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2353 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDQ 2432
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREPV 333
|
170 180
....*....|....*....|...
gi 40849888 2433 dAERLREAIAELEREKEKLKQEA 2455
Cdd:pfam05262 334 -AEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1325-1387 |
4.08e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 43.71 E-value: 4.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1325 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAELEARELQRRMQ 1387
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1334-1517 |
4.13e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1334 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQH 1413
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1414 LRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQRggaedELQALRARAEEAEAQKRQAQEEAErlrrqv 1492
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*
gi 40849888 1493 QDESQRKRQAEAELAlRVKAEAEAA 1517
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1667-1824 |
4.27e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEA 1744
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1745 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1820
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....
gi 40849888 1821 ERVL 1824
Cdd:COG1842 207 EDEL 210
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2148-2421 |
4.28e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2148 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVR 2223
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2224 VQMEELGKL-----KARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2296
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2297 AEKMLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK--EQMAQQLVEETQGFQRTLEAERQRQLEMSAEAER 2373
Cdd:pfam13868 213 EEQERKERQKEREEAeKKARQRQELQQAREEQIELKERRLAEEAerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 40849888 2374 LKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2421
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1187-1510 |
4.35e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1187 RQRELEQLGRQlryyRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEI----ERHGEKVEECQKFAK 1262
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1263 QYINAIKDYElqlitykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiSETLRRMEEEERLAE 1341
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1342 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAR-ELQRRMQEEVTRREEAAVDAQQQ--KRSIQEELQHLRQSS 1418
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKyESKVFLDQKRGHPEVKSQNGEEEvtKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1419 EAEIQAKAQQVEAAERSRmrieEEIRVVRLQLETTE----RQRGG-AEDELQALRARAEE-----AEAQKRQAQEEAERL 1488
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKL----EELRRRRQEKESEEfeklRQKQQeAELELEELKKKREErrkllEEEEQRRKQEEAERK 308
|
330 340
....*....|....*....|....*...
gi 40849888 1489 ------RRQVQDESQRKRQAEAELALRV 1510
Cdd:pfam02029 309 lreeeeKRRMKEEIERRRAEAAEKRQKL 336
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1335-1965 |
4.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1335 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAELEARELQRRMQ---EEVTRREEAAVDAQQQKRSI 1407
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQadlEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1408 QEELQhlRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQ-----LETTERQRGGAEDELQALRARAEEAEAQKRQAQ 1482
Cdd:PRK04863 378 QEENE--ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEAT 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1483 EEAERLRRQVQDESQRKRQAE--AELALRVKAEAEAAREKQRALQALDELKLQAEEAER----RLRQAEAERARQVQVAL 1556
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1557 ETAQRSAEVELQSK--RASFAEK-TAQLERTLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWqLKANEALRl 1633
Cdd:PRK04863 536 ERLLAEFCKRLGKNldDEDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA- 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1634 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKaEEQAVRQRELAEQ----------ELEKQRQLAE------------ 1691
Cdd:PRK04863 614 RLREQSGEEFEDSQDVTEYMQQLLERERELTVER-DELAARKQALDEEierlsqpggsEDPRLNALAErfggvllseiyd 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1692 --------------------------GTAQQRLAAEQELIRLRAETEQGEQQ---RQLLEEELAR--LQHEATAATQ--- 1737
Cdd:PRK04863 693 dvsledapyfsalygparhaivvpdlSDAAEQLAGLEDCPEDLYLIEGDPDSfddSVFSVEELEKavVVKIADRQWRysr 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1738 -------KRQELEAELAKVRAEMEVLLASKARAEEESRSTsekskQRLEAEAGRFrelaeeAARLRALAEEAKRQRQLAE 1810
Cdd:PRK04863 773 fpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQKL-----QRLHQAFSRF------IGSHLAVAFEADPEAELRQ 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1811 edAARQRAEAERvlteKLAAISEATRLKTEAEIALKEKEAENERLR---RLAEDEAFQRRRLE-----EQAAQHKADIE- 1881
Cdd:PRK04863 842 --LNRRRVELER----ALADHESQEQQQRSQLEQAKEGLSALNRLLprlNLLADETLADRVEEireqlDEAEEAKRFVQq 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1882 --------ERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAElelelgrirsNAEDtMRSKEL 1953
Cdd:PRK04863 916 hgnalaqlEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE----------DAAE-MLAKNS 984
|
730
....*....|..
gi 40849888 1954 AEQEAARQRQLA 1965
Cdd:PRK04863 985 DLNEKLRQRLEQ 996
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1718-2030 |
4.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1718 RQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1797
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1798 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1877
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1878 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELELGRIRSNAEDTMRSKELAEQE 1957
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1958 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2030
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1369-1520 |
4.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1369 AQAKAqaeLEARELQRRMQEEVtrREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEE------- 1441
Cdd:PRK12704 29 AEAKI---KEAEEEAKRILEEA--KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkle 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1442 EIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDEsqrkrqAEAELALRVKA 1512
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEE------ARHEAAVLIKE 177
|
....*...
gi 40849888 1513 EAEAAREK 1520
Cdd:PRK12704 178 IEEEAKEE 185
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1326-1427 |
4.54e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1326 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAKA-----QAELEARELQRRMQ----EEVT 1391
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEVakiqmQQKIMEKEAEKKISeiedEMHL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 40849888 1392 RREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAQ 1427
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1792-1936 |
4.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1792 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 1871
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1872 QAAQ------HKADIEERLAQLRKASESELERQKGLVEDTLRQR--RQVEEEIMALKASFEKAAAGKAELELE 1936
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1630-1959 |
4.86e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1630 ALRLRLQAEEVAQQKS-LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1708
Cdd:pfam07888 29 AELLQNRLEECLQERAeLLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1709 AETEQGEQQRQLLEEELAR------LQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekSKQRLEAEA 1782
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHearireLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQ----LQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1783 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARqraeaervLTEKLAAiseATRLKTEAEIALKEKEAENERLRRLAEDE 1862
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITT--------LTQKLTT---AHRKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1863 AFQRRRLEEQAAQ--------HKADIEE-----RLAQLRKASESELERQKGLVEdTLRQRRQVE--------EEIMALKA 1921
Cdd:pfam07888 254 EGLGEELSSMAAQrdrtqaelHQARLQAaqltlQLADASLALREGRARWAQERE-TLQQSAEADkdrieklsAELQRLEE 332
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 40849888 1922 SFEKAAAGKAELELELGRIR--SNAEDTMRSKELAEQEAA 1959
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKdcNRVQLSESRRELQELKAS 372
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2221-2401 |
4.97e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2221 SVRVQMEE----LGKLKARIEAENRA-LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEED 2289
Cdd:PRK11637 62 SVRQQQQQraslLAQLKKQEEAISQAsRKLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQGEHTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2290 LAQQRALAEKMLKEKMQA----VQEAtRLKAEAELLQQQKELAQEqaRRLQEDKEQMAQQLVEETQGFQRTLE---AERQ 2362
Cdd:PRK11637 142 LQLILSGEESQRGERILAyfgyLNQA-RQETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEqarNERK 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 2363 RQL---------------EMSAEAERLKLRMAEMSR-AQARAEE---DAQRFRKQAEE 2401
Cdd:PRK11637 219 KTLtglesslqkdqqqlsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1241-1512 |
5.23e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1241 KALLEEIERH------GEK---VEECQKFAKQ---YIN-----AIKDYELQLITYKAqlEPVASPAKKPKVQSGSESVIQ 1303
Cdd:PLN03188 970 KRVQDELEHYrnfydmGERevlLEEIQDLRSQlqyYIDsslpsARKRNSLLKLTYSC--EPSQAPPLNTIPESTDESPEK 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1304 EYVDLRTRYSELTtltSQYIKFISETLRRMEEEERLAEQQRAE--ERERLAEveaALEKQRQLA-EAHAQAKAQ-AELEA 1379
Cdd:PLN03188 1048 KLEQERLRWTEAE---SKWISLAEELRTELDASRALAEKQKHEldTEKRCAE---ELKEAMQMAmEGHARMLEQyADLEE 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1380 RELQ-----RRMQEEVTRREEAAVDAqqqkrSIQEELQHLRQSSEAEIQA-KAQQveaaERSRMRIEEEIRVVRLQLETT 1453
Cdd:PLN03188 1122 KHIQllarhRRIQEGIDDVKKAAARA-----GVRGAESKFINALAAEISAlKVER----EKERRYLRDENKSLQAQLRDT 1192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1454 ER--QRGG--------AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1512
Cdd:PLN03188 1193 AEavQAAGellvrlkeAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
2-163 |
5.32e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.01 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2 AHLLTSGPPpdeQDFIQAYEEVREKYKDERDRVQKKTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---S 78
Cdd:COG5069 350 AHLFNTHPG---QEPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 79 LPREKGR-------MRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsg 144
Cdd:COG5069 425 HKLVKKQpasgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD----- 498
|
170
....*....|....*....
gi 40849888 145 qsEDMTAKEKLLLWSQRMV 163
Cdd:COG5069 499 --GCGLSDSDLCAWLGSLG 515
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1667-1902 |
5.36e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEATAATQKRQEleae 1745
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1746 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEagrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1824
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1825 TEKLAAIS-EATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasESELERQKGLV 1902
Cdd:pfam05911 140 KSRLESCEkEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1424-1861 |
5.49e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1424 AKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAE 1503
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1504 AELALRVKAEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1583
Cdd:COG3064 85 AAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1584 TLQEEHVTVTQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREAR 1663
Cdd:COG3064 165 AAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1664 RRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELE 1743
Cdd:COG3064 245 LGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1744 AELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV 1823
Cdd:COG3064 325 GALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLR 404
|
410 420 430
....*....|....*....|....*....|....*...
gi 40849888 1824 LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAED 1861
Cdd:COG3064 405 LDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVA 442
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1196-1408 |
5.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1196 RQLRYYRESADPLSSWLQD-AKSRQEQIQAvpianSQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINA---IKDY 1271
Cdd:COG3206 164 QNLELRREEARKALEFLEEqLPELRKELEE-----AEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1272 ELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQR 1344
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1345 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQRRMQEE-------VTRREEAAVDAQQQKRSIQ 1408
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3414-3445 |
5.67e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.67e-03
10 20 30
....*....|....*....|....*....|..
gi 40849888 3414 KLLSAEKAVTGYKDPYSGSTISLFQAMKKGLV 3445
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1324-1583 |
5.82e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1324 KFISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEARELQR-RMQEEVTRREEAAV 1398
Cdd:pfam05667 250 KRIAEQLRsaalAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1399 DAQQQK--RSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaedelQALRARA-EEAE 1475
Cdd:pfam05667 330 QQQREEelEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ--------YKVKKKTlDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1476 aqkrQAQEEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalDELKLQAEEAERRLRQAEAERaRQ 1551
Cdd:pfam05667 398 ----DAEENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EK 462
|
250 260 270
....*....|....*....|....*....|..
gi 40849888 1552 VQVALEtaqrsaevELQSKRASFAEKTAQLER 1583
Cdd:pfam05667 463 IKEVAE--------EAKQKEELYKQLVAEYER 486
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1138-1506 |
6.01e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1138 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLgrqLRYYRESADPLSSWLQDAKS 1217
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1218 RQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKV-------EECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK 1290
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1291 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSqyiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1368
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1369 AQAKAQAELEARELQrrMQEEVTRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEiRVVRL 1448
Cdd:pfam07888 266 QRDRTQAELHQARLQ--AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 40849888 1449 QLETT-ERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1506
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2368-2616 |
6.07e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2368 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELERE 2447
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2448 KEKLKQE-AKLLQlkseEMQTVQQEQILQetqalqksFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLQEEQQRQ 2526
Cdd:COG4942 99 LEAQKEElAELLR----ALYRLGRQPPLA--------LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2527 QQQMEQEKQELVASMEEARRRQREAEEGVRRKQEELQRLEQQRQQQEKLLAE---ENQRLRERLQRLEEEhrAALAHSEE 2603
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAE--AAAAAERT 243
|
250
....*....|...
gi 40849888 2604 IATSQAAATKALP 2616
Cdd:COG4942 244 PAAGFAALKGKLP 256
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1359-1490 |
6.11e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1359 EKQRQLAEAHAQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKAQQVEAAERSR 1436
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1437 MRIEEEIRVVRLQLETTERQRGGAEDELQalraraeeaEAQKRQAQEEAERLRR 1490
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1358-1564 |
6.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1358 LEKQRQLAEAHAQAKAQAELEARELQRRMQEEvtRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrm 1437
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1438 rieeeirvvrlqLETTERQRGGAEdelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEAELALRVKAEAEaa 1517
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 40849888 1518 rekqraLQALDELKLQAEEAerrlrQAEAERARQVQVAlETAQRSAE 1564
Cdd:PRK12705 157 ------EEKAQRVKKIEEEA-----DLEAERKAQNILA-QAMQRIAS 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2166-2590 |
6.51e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2166 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQ----RLkAEVTEAARQRSQVEeelfsvRVQmEELGKLKARIEAENR 2241
Cdd:COG3096 297 ARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdHL-NLVQTALRQQEKIE------RYQ-EDLEELTERLEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2242 ALilrdkdntqrflEEEAEkmkQVAEEAARLSVAAQEAARLR-QLAEE----DLAQQRALAekmlkekmqaVQEATRLKA 2316
Cdd:COG3096 369 VV------------EEAAE---QLAEAEARLEAAEEEVDSLKsQLADYqqalDVQQTRAIQ----------YQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2317 EAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTL--EAERQRQLEMSAEAerLKLRMAEMSRAQA--RAEEDA 2392
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvADAARRQFEKAYEL--VCKIAGEVERSQAwqTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2393 QRFRKQAEEIGEklhrtelatqekvtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQeakllQLKSEEMQTVQQEQ 2472
Cdd:COG3096 502 RRYRSQQALAQR---------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQ-----QLDAAEELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2473 --ILQETQALQKSFLSEKDSLLQRERfiEQEKAKLEQLFQDEVA--KAKQLQEEQQRQQQQMEQEKQELVASMEEARRRQ 2548
Cdd:COG3096 562 leAQLEELEEQAAEAVEQRSELRQQL--EQLRARIKELAARAPAwlAAQDALERLREQSGEALADSQEVTAAMQQLLERE 639
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 40849888 2549 REAEegvrrkqeelqrleqqrqQQEKLLAEENQRLRERLQRL 2590
Cdd:COG3096 640 REAT------------------VERDELAARKQALESQIERL 663
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1801-1962 |
6.51e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1801 EAKRQRQLAEEDAARQRAEAERvLTEKlaAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQRRRLEEQAAQ 1875
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAER-ETEI--AIAQANREAEEAELEqereiETARIAEAEAELAKKKAEERREAETARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1876 HKADIEErlAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKASFEKAAAGKAELELElgrirsnaedtmrskELAE 1955
Cdd:COG2268 266 AAYEIAE--ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AEAE 328
|
....*..
gi 40849888 1956 QEAARQR 1962
Cdd:COG2268 329 AEAIRAK 335
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1432-1762 |
6.61e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1432 AERSRMRIEEEIRVVRLQLETterqrggAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRvk 1511
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMM-------EEERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKLQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1512 aEAEAAREKQRALQALDELKLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvt 1591
Cdd:pfam13868 99 -EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAE--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1592 vtqlreeaERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQ---QKSLAQADAEKQKEEAEREARRRGKA 1668
Cdd:pfam13868 175 --------REEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERkerQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1669 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelaRLQHEATAATQKRQELEAELAK 1748
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE---REEQRAAEREEELEEGERLREE 323
|
330
....*....|....
gi 40849888 1749 VRAEMEVLLASKAR 1762
Cdd:pfam13868 324 EAERRERIEEERQK 337
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1678-1963 |
7.13e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1678 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1757
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1758 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKR-QRQLAEE---DAARQRAEAErvlteklaaise 1833
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQRgERILAYFgylNQARQETIAE------------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1834 atrlkteaeialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLvedtlrqrrqve 1913
Cdd:PRK11637 175 ---------------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTL------------ 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 40849888 1914 eeiMALKASFEKAAAGKAELELELGRIRSN-AEDTMRSKELAEQEA-------ARQRQ 1963
Cdd:PRK11637 222 ---TGLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1579-1936 |
7.26e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1579 AQLERTLQEEHVTVtqlreeaERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1658
Cdd:pfam07888 34 NRLEECLQERAELL-------QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1659 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1738
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1739 RQELEAELAKVRAemevLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE------ED 1812
Cdd:pfam07888 187 LRSLSKEFQELRN----SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglgeelSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1813 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA----ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLR 1888
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 40849888 1889 KAsESELERQKglvEDTLRQRRQVEEEIMALKASFEKAAAGKAELELE 1936
Cdd:pfam07888 343 KL-EVELGREK---DCNRVQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1365-1516 |
7.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 42.55 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1365 AEAHAQAKAQAELEARElqrrmqeevtrREEAAVDAQQQKRSIQEElqhlrqssEAEIQAKAQQVEAAERSRMRIEEEIR 1444
Cdd:PRK12472 182 AEALAAAPARAETLARE-----------AEDAARAADEAKTAAAAA--------AREAAPLKASLRKLERAKARADAELK 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 40849888 1445 VV--RLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1516
Cdd:PRK12472 243 RAdkALAAAKTDEAKARAEERQQKAAQQAAEAATQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDA 316
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1400-1536 |
7.45e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 41.51 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1400 AQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLET-TERQRGGAEDELQALRARAEEAEAQK 1478
Cdd:pfam12037 51 MKKQEQTRQAELQ-------AKIKEYEAAQEQLKIERQRVEYEERRKTLQEETkQKQQRAQYQDELARKRYQDQLEAQRR 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40849888 1479 RQA-----QEEAERLRRQVQDESQRKRQAEAELALR-------VKAEAE--AAREKQRALQALDELKLQAEE 1536
Cdd:pfam12037 124 RNEellrkQEESVAKQEAMRIQAQRRQTEEHEAELRreterakAEAEAEarAKEERENEDLNLEQLREKANE 195
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1621-1916 |
7.55e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1621 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE-QELEKQRQLAEGTAQ---- 1695
Cdd:pfam15558 42 QKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEdQENQRQEKLERARQEaeqr 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1696 -----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASKARAEEESRST 1770
Cdd:pfam15558 122 kqcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQA-RKVLVDCQAKAEELLRRL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1771 S-EKSKQRLEAE-----AGRFRELAEEAA-------RLRALAEEAKRQRQLAEEDAARqraEAERVLTEKLAAISEATRL 1837
Cdd:pfam15558 201 SlEQSLQRSQENyeqlvEERHRELREKAQkeeeqfqRAKWRAEEKEEERQEHKEALAE---LADRKIQQARQVAHKTVQD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1838 KTE-AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEI 1916
Cdd:pfam15558 278 KAQrARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKK---EQRSEQISREKEATLEEARKTARASFHMREKVREET 354
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1398-1544 |
7.79e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1398 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEDELQALRARAEEAEAQ 1477
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 40849888 1478 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALDELKLqaEEAERR------LRQA 1544
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1517-1571 |
7.94e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 7.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 40849888 1517 AREKQRALQaldelKLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1571
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2228-2623 |
8.19e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2228 ELGKLKARIE--AENRALILRDKDNTQRFLEEEAEKMKQ---VAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2302
Cdd:PRK02224 214 ELAELDEEIEryEEQREQARETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2303 EKMQAVQEATRLKAEAELLQQQKElaqeqarRLQEDKEQMaqqlveetqgfQRTLEAERQRQLEMSAEAERLKLRMAEMS 2382
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARRE-------ELEDRDEEL-----------RDRLEECRVAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2383 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQ--L 2460
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2461 KSEEMQTVQQEQILQE------TQALQKSflSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLqeeqqrqqqqmeqek 2534
Cdd:PRK02224 436 RTARERVEEAEALLEAgkcpecGQPVEGS--PHVETIEEDRERVEELEAELEDL-EEEVEEVEER--------------- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2535 qelVASMEEARRRQREAEEgvrrkqeelqrLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIATSQAAATKA 2614
Cdd:PRK02224 498 ---LERAEDLVEAEDRIER-----------LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
....*....
gi 40849888 2615 LPNGRDALD 2623
Cdd:PRK02224 564 EEEAEEARE 572
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1460-1583 |
8.36e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1460 AEDELQALRARAEEAEAQKRQAQEEAERLRRQVQdesqrKRQAEAELALRVKAEA---EAAREKQ--------------R 1522
Cdd:pfam04012 34 MQSELVKARQALAQTIARQKQLERRLEQQTEQAK-----KLEEKAQAALTKGNEElarEALAEKKslekqaealetqlaQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40849888 1523 ALQALDELKLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1583
Cdd:pfam04012 109 QRSAVEQLRKQLAALETKIQQLKAKK-NLLKARLKAAKAQEAVQTSLGSLSTSSATDSFER 168
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1769-2044 |
8.55e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 41.89 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1769 STSEKSKQRLEAEAG-RFRELAEEaarlRALAEEAKRQRQLAEEDAARQRAeaervlTEKLAAISeATRLKTEAEIALKE 1847
Cdd:PRK07735 1 MDPEKDLEDLKKEAArRAKEEARK----RLVAKHGAEISKLEEENREKEKA------LPKNDDMT-IEEAKRRAAAAAKA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1848 KEAENERLRRLAEDEAFQRrrlEEQAAQHKAdieerlAQLRKASESELERQKglvEDTLRQRRQVEEEIMALKASFE-KA 1926
Cdd:PRK07735 70 KAAALAKQKREGTEEVTEE---EKAKAKAKA------AAAAKAKAAALAKQK---REGTEEVTEEEKAAAKAKAAAAaKA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1927 AAGKAELELELGRIRSNAEDTMRSKELAEQEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 2006
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAA 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 40849888 2007 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2044
Cdd:PRK07735 218 LAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARAKT 255
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1338-1505 |
8.59e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 42.33 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1338 RLAEQQRAEERERLAEVEAALEKQRQlaeahaqakAQAELEARELQRRMQEEvtRREeaavdAQQQKRSIQEELQhlrQS 1417
Cdd:PRK10811 644 RQAQQQTAETRESQQAEVTEKARTQD---------EQQQAPRRERQRRRNDE--KRQ-----AQQEAKALNVEEQ---SV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1418 SEAEIQAKAQQVEaAERSRMRIEEEIRVvrLQLETTERQRGGAEDELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1497
Cdd:PRK10811 705 QETEQEERVQQVQ-PRRKQRQLNQKVRI--EQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDE 781
|
....*...
gi 40849888 1498 RKRQAEAE 1505
Cdd:PRK10811 782 ENNAENRD 789
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
34-136 |
8.68e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.59 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 34 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRHRQVKLV 109
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 40849888 110 NIRNDDIADGNPKLTLGLIWTIILHFQ 136
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1438 |
8.72e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1179 AVLAQTDVR---QRELEQLGRQLRYYRESADPLSSWLQDAKSRQEQIQAVPIANSQAAREQLRQEKALLEEIERHGEKVE 1255
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1256 ECQKFAKQYINAIKDYELQLitYKAQLEPvaspakKPKVQSGSESVIQEYvdlrtRYSELTTLTSQYIKFISETLRRMEE 1335
Cdd:COG4942 94 ELRAELEAQKEELAELLRAL--YRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1336 EERLAEQQRAEERERLAEVEAALEKQRqlaeahaQAKAQAELEARELQRRMQEEVTRREEAAVDAQQQKRSIQEELQHLR 1415
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 40849888 1416 QSSEAEIQAKAQQVEAAERSRMR 1438
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1328-1455 |
8.92e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.02 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1328 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAELEAREL-QRRMQEEVTRREEAAVDAQQQKR 1405
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 40849888 1406 SIQEELQHLRQSSEAeiqAKAQQVEAAErsRMRIEEEIRVVRLQLETTER 1455
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1361-2055 |
8.94e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1361 QRQLAEA---HAQAKAQAELEARELQRRMQEEVTRREeAAVDAQQQKRSIQEELQHLRQSSEAEIQA-KAQQVEAAERSR 1436
Cdd:pfam15921 91 QRRLNESnelHEKQKFYLRQSVIDLQTKLQEMQMERD-AMADIRRRESQSQEDLRNQLQNTVHELEAaKCLKEDMLEDSN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1437 MRIEEeIRVVRLQLEtterqrgGAEDELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEAELALrVKAEA 1514
Cdd:pfam15921 170 TQIEQ-LRKMMLSHE-------GVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISY-LKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1515 EAAREKQRALQA--LDELKLQAEEAERRLRQAEAERARQVQVALETAQ--RSAEVELQSKRASFAEKT----AQLERTLQ 1586
Cdd:pfam15921 241 FPVEDQLEALKSesQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASsaRSQANSIQSQLEIIQEQArnqnSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1587 EEHVTVTQLreeaerraqqqaeaerareeaereleRWQLKanealrlrlQAEEVAQQKSlaqadaekqkeeaerearrrg 1666
Cdd:pfam15921 321 DLESTVSQL--------------------------RSELR---------EAKRMYEDKI--------------------- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1667 kaeEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1746
Cdd:pfam15921 345 ---EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1747 AKVRAEMEVLLASKARAEEESRSTSEkskQRLEAEAGRFRELaEEAARLRALAEEAKRQ-RQLAEEDAARQRA--EAERV 1823
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQGQME---RQMAAIQGKNESL-EKVSSLTAQLESTKEMlRKVVEELTAKKMTleSSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1824 LTEKLAAISEATRlkteaeiALKEKEAENERLRrlaedeafQRRRLEEQAAQHKADIEERLAQLRKASESeLERQKGLVE 1903
Cdd:pfam15921 498 VSDLTASLQEKER-------AIEATNAEITKLR--------SRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1904 DTLRQRRQVEEEIMALKASFEKAAAG----KAELELELGRIRSNAEDTmrsKELAEQEAARQRQLAaeeeqrrreaeerv 1979
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAmqveKAQLEKEINDRRLELQEF---KILKDKKDAKIRELE-------------- 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1980 qrslaaeeeaARQRKVALEEVERLKAKVEEARRLRERAEQESarqlQLAQEAAQKRLQAEEKAHAFVVQQR-----EEEL 2054
Cdd:pfam15921 625 ----------ARVSDLELEKVKLVNAGSERLRAVKDIKQERD----QLLNEVKTSRNELNSLSEDYEVLKRnfrnkSEEM 690
|
.
gi 40849888 2055 Q 2055
Cdd:pfam15921 691 E 691
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2168-2346 |
9.17e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.78 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2168 RQKAQVEQELTTlRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEeelfsVRVQMEELGKLKARIEAENRALILR- 2246
Cdd:COG2268 201 ARIAEAEAERET-EIAIAQANREAEE-AELEQEREIETARIAEAEAELA-----KKKAEERREAETARAEAEAAYEIAEa 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2247 --DKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQ 2322
Cdd:COG2268 274 naEREVQRQLEIAEREREIELQEKEAEREEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKL 353
|
170 180
....*....|....*....|....
gi 40849888 2323 QQKELAQEQARRLQEDKEQMAQQL 2346
Cdd:COG2268 354 GDAAILLMLIEKLPEIAEAAAKPL 377
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1668-1768 |
9.45e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1668 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1747
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 40849888 1748 KvRAEMEVLLaskarAEEESR 1768
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1328-1432 |
9.47e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.84 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 1328 ETLRRMEEEERLAEQQRAEERERLAEV---EAALEKQRQLAEAHAQAKAQAELE------ARELQRRMQEEVTRREEA-- 1396
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEkyqEWLQRKARQQTKKREESHKQKAAEsaskslAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 40849888 1397 -AVDAQQQKRsiQEELQHLRQSSEAEIQAKAQQVEAA 1432
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4270-4300 |
9.57e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.57e-03
10 20 30
....*....|....*....|....*....|.
gi 40849888 4270 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4300
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2169-2511 |
9.59e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2169 QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENralilrDK 2248
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2249 DNTQRFLEEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2325
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2326 ELAQEQarrlQEDKEQMAQQLVEETQGFQRTLEAERQRQlEMSAEAERLKlrmaemsraqaraeedaqrfrKQAEEIGEK 2405
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40849888 2406 LHRTELATQEKVtlVQTLEIQRQQSDQDAERLREAIAELEREKEKLKQEAKLLQlkseemqtvqqEQILQETQALQKsFL 2485
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ-----------RELEEKQNEIEK-LK 376
|
330 340
....*....|....*....|....*.
gi 40849888 2486 SEKDSLLQRERFIEQEKAKLEQLFQD 2511
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| |
