|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
41-145 |
2.47e-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: 248.86 E-value: 2.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 41 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 41322919 121 RNDDIADGNPKLTLGLIWTIILHFQ 145
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
38-156 |
1.78e-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: 241.47 E-value: 1.78e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 117
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322919 118 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 156
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
37-154 |
6.23e-72 |
|
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: 237.19 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 37 QDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21236 11 KDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
|
90 100 110
....*....|....*....|....*....|....*...
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 154
Cdd:cd21236 91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
158-263 |
1.05e-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: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 41322919 238 PEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
159-263 |
3.36e-66 |
|
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: 219.96 E-value: 3.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 41322919 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
38-155 |
2.01e-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: 212.59 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 117
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 41322919 118 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 155
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
159-263 |
3.00e-57 |
|
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: 194.43 E-value: 3.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 41322919 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
157-263 |
1.79e-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: 177.93 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 157 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 236
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 41322919 237 DPEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
43-146 |
1.20e-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: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 43 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 41322919 122 NDDIADGNPKLTLGLIWTIILHFQI 146
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 ... |
37-142 |
5.01e-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: 168.31 E-value: 5.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 37 QDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQV 115
Cdd:cd21246 10 ADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRV 89
|
90 100
....*....|....*....|....*..
gi 41322919 116 KLVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21246 90 HLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
159-259 |
9.05e-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: 161.43 E-value: 9.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 41322919 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-259 |
3.68e-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: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 36 EQDERDRVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRH 112
Cdd:COG5069 2 EAKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 113 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGR 191
Cdd:COG5069 82 KGVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 192 LFNAIIHRHKPLLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 259
Cdd:COG5069 159 AFSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
37-142 |
1.16e-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: 158.61 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 37 QDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLrHRQV 115
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 41322919 116 KLVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
39-146 |
2.45e-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: 157.54 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 39 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 114
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 41322919 115 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
159-259 |
6.17e-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: 156.40 E-value: 6.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 41322919 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
39-146 |
9.36e-44 |
|
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: 156.19 E-value: 9.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 39 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 111
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 41322919 112 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
158-263 |
4.01e-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: 148.24 E-value: 4.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 41322919 238 PEDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
146-261 |
7.16e-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: 147.89 E-value: 7.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1314-1893 |
3.37e-40 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 164.72 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1314 QEYVDLRTHYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---LAEAHAQAKAQAERE 1389
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1390 AKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG 1469
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1470 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1549
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1550 RRLR--QAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQeehvavAQLREEAERRAQQQAEAERAREEA 1627
Cdd:COG1196 449 EEEAelEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE------AEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1628 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1707
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1708 RLAAEQELIRLRAETEQGEqqrqLLEEELARLQREAAAATQKRqeLEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1787
Cdd:COG1196 603 LVASDLREADARYYVLGDT----LLGRTLVAARLEAALRRAVT--LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1788 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1867
Cdd:COG1196 677 AEAELE----ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
570 580
....*....|....*....|....*.
gi 41322919 1868 RLAEDEAFQRRRLEEQAAQHKADIEE 1893
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
38-142 |
6.16e-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: 146.32 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
37-142 |
2.19e-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: 144.43 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 37 QDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQV 115
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 41322919 116 KLVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
41-142 |
1.07e-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: 141.37 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 41 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 119
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 41322919 120 IRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
39-146 |
1.57e-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: 141.12 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 39 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
155-259 |
1.82e-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: 140.91 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 155 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 41322919 235 LLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
43-144 |
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 41322919 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 41322919 121 RNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
155-259 |
6.71e-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: 139.42 E-value: 6.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 155 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 41322919 235 LLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1351-1973 |
1.12e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 156.64 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAEReAKELQQRMQEevvRREEAAVdaqQQKRSIQEELQQLrqss 1429
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAER-YRELKEELKE---LEAELLL---LKLRELEAELEEL---- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1430 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1509
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEE-------LELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1510 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALEtaQRSAEAELQSKRASFAEKT 1589
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1590 AQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEA 1669
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1670 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQREAAAA 1746
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1747 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAkRQRQLAEEDAAR 1826
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL-LGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1827 QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSEL 1906
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1907 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSnaEDTLRsKEQAELEAARQR 1973
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD--LEELE-RELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1681-2249 |
3.49e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 154.71 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEE---DAARQRAEAERVLAE 1837
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLE----ELEEELAELEEELEELEEELEELEEeleEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1838 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKgLVEDTL 1917
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1918 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 1997
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1998 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQE 2072
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2073 QSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQA 2152
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2153 EQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFS 2232
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|....*..
gi 41322919 2233 VRVQMEELSKLKARIEA 2249
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
158-259 |
3.53e-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: 137.30 E-value: 3.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 41322919 238 PEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
38-146 |
1.03e-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: 135.82 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 38 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1441-2049 |
2.36e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 152.40 E-value: 2.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1441 EAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASR 1520
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1521 VKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEH 1600
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1601 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1680
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLAskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL--AEEAKRQRQLAEEDAARQRAEAERVLAEK 1838
Cdd:COG1196 490 AARLLLLLE--AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1839 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLR 1918
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1919 QRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 1998
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1999 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2049
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1478-2113 |
4.48e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 151.24 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1478 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaevelasrVKAEAEAAREKQRALQALEE-------LRLQAEE 1547
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKEleaelllLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1548 AERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1627
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1628 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1707
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE-----------AELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1708 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQ 1787
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1788 RLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAiGEATRLKTEAEIALKEKEAENERLR 1867
Cdd:COG1196 468 LLEEAA----LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA-GLRGLAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1868 RLAEDEAFQRRRLEEQAAQhkadIEERLAQLRkasdseLERQKGLVEDTLRQRRQVEEEILALKASFekAAAGKAELELE 1947
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAA----AIEYLKAAK------AGRATFLPLDKIRARAALAAALARGAIGA--AVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1948 LGRIRSNAEDTL--RSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2025
Cdd:COG1196 611 ADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2026 ERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2105
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
....*...
gi 41322919 2106 QSRRQVEE 2113
Cdd:COG1196 771 RLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1339-2051 |
8.84e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.45 E-value: 8.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1418
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1419 Q----EELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGELQALRA--RAEEAEAQKRQA 1492
Cdd:PTZ00121 1192 ElrkaEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfeEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1493 QEEAERLRRQVQ-DESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQ 1571
Cdd:PTZ00121 1271 AIKAEEARKADElKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK-KKAEEAKKAAEAAK 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1572 rsAEAELQSKRASFAEKTAQLERSLQEEHvavaqlreeaerraqqqaeaerareeaerelerwQLKANEAlrlRLQAEEV 1651
Cdd:PTZ00121 1350 --AEAEAAADEAEAAEEKAEAAEKKKEEA----------------------------------KKKADAA---KKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1652 AQQKSLAQaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQR-QLAEGTAQQRLAAEqELIRLRAETEQGEQQRQ 1730
Cdd:PTZ00121 1391 KKADEAKK------------------KAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKAD-EAKKKAEEAKKADEAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1731 LLEEelarlQREAAAATQKRQEL-EAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEaEAGRFRELAEEAARLRAl 1809
Cdd:PTZ00121 1452 KAEE-----AKKAEEAKKKAEEAkKADEAKKKAE-------EAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKK- 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1810 AEEAKRQRQLAEEDAARQRAEA----ERVLAEKLAAIGEATRL--KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1883
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKAeeKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1884 AAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRrqveEEILALKASFEKAAAGKAELELELGRIRS-----NAEDT 1958
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1959 LRSKEQA--ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQES 2032
Cdd:PTZ00121 1674 KKKAEEAkkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDE 1753
|
730
....*....|....*....
gi 41322919 2033 ARQLQLAQEAAQKRLQAEE 2051
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEE 1772
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
162-263 |
1.18e-35 |
|
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: 132.55 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 41322919 241 VDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
143-259 |
4.92e-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: 131.71 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 143 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 222
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 223 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
42-147 |
8.32e-34 |
|
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: 127.95 E-value: 8.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 118
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1705-2337 |
8.33e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.92 E-value: 8.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1705 AQQRL-AAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEEsrstse 1783
Cdd:COG1196 177 AERKLeATEENLERLEDILGE-------LERQLEPLERQAEKA-ERYRELKEELKELEAELLLLKLRELEAELE------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1784 kskqrleaeagrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1863
Cdd:COG1196 243 --------------ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1864 ERLRRLAEDEA---FQRRRLEEQAAQHKADIEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAG 1940
Cdd:COG1196 309 ERRRELEERLEeleEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1941 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 2020
Cdd:COG1196 388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2021 ARRLRERAEQESARQLQLAQEAAQKR---LQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2097
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLlllLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2098 VQA---------------EREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2162
Cdd:COG1196 548 LQNivveddevaaaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2163 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSK 2242
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2243 LKARIEAENRALILRDKDNTQRFLQEEAEKMKQvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK----MQA 2318
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLA 786
|
650
....*....|....*....
gi 41322919 2319 VQEATRLKAEAELLQQQKE 2337
Cdd:COG1196 787 IEEYEELEERYDFLSEQRE 805
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
43-146 |
6.71e-33 |
|
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: 124.71 E-value: 6.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 120
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 41322919 121 RNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
158-256 |
1.59e-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: 123.69 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 41322919 238 PEDVDVPQPDEKSIITYVS 256
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
43-146 |
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 41322919 43 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 41322919 122 NDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
159-259 |
1.87e-32 |
|
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: 123.67 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 41322919 239 EDVDVPQPDEKSIITYVSSLY 259
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
38-142 |
5.43e-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: 5.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 38 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTIIL 142
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
146-261 |
3.29e-31 |
|
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: 120.33 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 146 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 226 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 261
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
162-263 |
5.25e-31 |
|
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: 119.29 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 41322919 241 VDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
162-264 |
1.53e-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: 118.11 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 41322919 240 DVDVPQPDEKSIITYVSSLYDAMPR 264
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
158-256 |
1.94e-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: 118.01 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 41322919 238 PEDVDVPQPDEKSIITYVS 256
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
39-148 |
2.13e-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: 118.07 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 39 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 114
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 41322919 115 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 148
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
164-259 |
4.15e-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: 116.68 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 164 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 242
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 41322919 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
42-144 |
5.94e-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: 116.43 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
894-971 |
1.36e-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: 114.24 E-value: 1.36e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 894 LAWQSLRRDVQLIRSWSLATFRTLKPEEQRQALHSLELHYQAFLRDSQDAGGFGPEDRLMAEREYGSCSHHYQQLLQS 971
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1677-2460 |
2.53e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 130.26 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1756
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEE--ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1757 LAKvRAEmevllasKARAEEESRSTSEKSKqrleaeagrfrelAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlA 1836
Cdd:PTZ00121 1174 DAK-KAE-------AARKAEEVRKAEELRK-------------AEDARK----AEAARKAEEERKAEEARKAEDAKK--A 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1837 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeqaAQHKADIEERLAQLRKASdselERQKGLVEDT 1916
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-----AAIKAEEARKADELKKAE----EKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1917 LRQRRQVEEeilalkasfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAA 1996
Cdd:PTZ00121 1298 AEEKKKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1997 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2073
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2074 SvlDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQsaeeqaqaraqaqaaaekLRKEAEQEAARRAQAE 2153
Cdd:PTZ00121 1446 A--DEAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE------------------AKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2154 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQrlKAEATEAARQRSQVEEELFSV 2233
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2234 RVQMEELSKL-KARIEAENRALILRDKDNTQRFLQEEAEKMKqvAEEAARlsvaAQEAARLRQLAEEDLAQQRALAEKML 2312
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2313 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLAEETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2392
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2393 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvTLVQTLEIQRQQSDHDAERLREAIAELEREKE 2460
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK-KKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
144-261 |
5.65e-29 |
|
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: 114.41 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 144 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 223
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322919 224 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1314-2027 |
1.71e-28 |
|
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: 127.09 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1314 QEYVDLRTHYSELT-TLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaqAKAQAEREAKE 1392
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL-------EVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1393 LQQRMQEEVVRREeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAE 1472
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1552
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1553 RQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL- 1631
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSg 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1632 ---------------ERWQLKANEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1686
Cdd:TIGR02168 518 lsgilgvlselisvdEGYEAAIEAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1687 RELA------------------------------EQELEKQRQL-----------------------AEGTAQQRLAAEQ 1713
Cdd:TIGR02168 598 EGFLgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1714 ELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRL 1789
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1790 EAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRL 1869
Cdd:TIGR02168 758 ELEAEI-EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1870 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAGKAELELELG 1949
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1950 RIRSNAE--DTLRSKEQAELEAARQR------QLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLK----AK 2017
Cdd:TIGR02168 912 ELRRELEelREKLAQLELRLEGLEVRidnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAA 991
|
810
....*....|
gi 41322919 2018 VEEARRLRER 2027
Cdd:TIGR02168 992 IEEYEELKER 1001
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
162-261 |
3.19e-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: 111.22 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 240
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 41322919 241 VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1538-2168 |
3.82e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.43 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1538 LEELRLQAEEAERRLRQAEVERARQVQVALeTAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqq 1617
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAEL----------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1618 aeaerareeaerelerwqlkanEALRLRLQAEEvaqqkslaqaeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQ 1697
Cdd:COG1196 270 ----------------------EELRLELEELE---------------------------LELEEAQAEEYELLAELARL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1698 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevLLASKARAEEE 1777
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLEAEAELAEA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1778 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1857
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1858 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKA 1937
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1938 AAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK 2017
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2018 VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEAR 2097
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 2098 VQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2168
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1106-1816 |
5.28e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.05 E-value: 5.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1106 RAHEEQLKEAQAVpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLl 1185
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1186 erwqavlaqtdvrQRELEQLGRQLRYYRESadplgawLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKV 1265
Cdd:COG1196 294 -------------LAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1266 EECQrfakqyinaikdyelqlvtykaqlepvaspakkpkvqsgsesviqeyvdlrthyselttltsqyikfisETLRRME 1345
Cdd:COG1196 340 EELE---------------------------------------------------------------------EELEEAE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1346 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQL 1425
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1426 RQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvQD 1505
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE---GF 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1506 ESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1585
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1586 AEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA----NEALRLRLQAEEVAQQKSLAQAE 1661
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGS 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1662 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR 1741
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1742 EAAAATQ-------KRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAK 1814
Cdd:COG1196 747 LLEEEALeelpeppDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEAR 811
|
..
gi 41322919 1815 RQ 1816
Cdd:COG1196 812 ET 813
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1351-2413 |
9.63e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.55 E-value: 9.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERLAEVEAalEKQRQLAE-AHAQAKAQAE--REAKELQQRMQEEVVRRE---EAAVD-----AQQQKRSIQ 1419
Cdd:NF041483 85 ADQLRADAERELRDARA--QTQRILQEhAEHQARLQAElhTEAVQRRQQLDQELAERRqtvESHVNenvawAEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1420 EELQQLRQSSEAEiqakARQAEAAERSRlrieeeirVVRLQLEAteRQRGGAEGElqalRARAEeAEAQKRQAQEEAERL 1499
Cdd:NF041483 163 SQARRLLDESRAE----AEQALAAARAE--------AERLAEEA--RQRLGSEAE----SARAE-AEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1500 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaeEAERRLRQAEVERARQVQVALETAqrsaeaelq 1579
Cdd:NF041483 224 LNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA--------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1580 SKRASFAEKT-AQLERSLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1657
Cdd:NF041483 293 AKQLASAESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKA 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1658 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQGEQQRQLLEEEL 1736
Cdd:NF041483 370 ARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVELQEEARRLRGEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1737 ARLQREAAAATQK-----RQELEAELAKVRAEMEVLLAsKARAE-EESRSTSEKSKQRLEAEAGR----FRELAE----- 1801
Cdd:NF041483 450 EQLRAEAVAEGERirgeaRREAVQQIEEAARTAEELLT-KAKADaDELRSTATAESERVRTEAIErattLRRQAEetler 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1802 ---EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLRRL 1869
Cdd:NF041483 529 traEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIRRE 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1870 AEDEAfqrRRLEEQAAqhkadieERLAQLRKASDSELERQKGLVEDTLRQRRqVEEEILALKASFEKAAagkaelelELG 1949
Cdd:NF041483 609 AAEET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------EAE 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1950 RIRSNAEDTlRSKEQAELEAARQRqlaaeeerrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRERAE 2029
Cdd:NF041483 670 RLKSEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERERAR 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2030 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEaarraaeeaeearvQAEREAAQSRR 2109
Cdd:NF041483 735 EQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQE--------------QAEEEIAGLRS 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2110 QVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVEQElt 2189
Cdd:NF041483 801 AAEHAAERTRTEAQEEADRVRSDAYAERERASEDAN------------RLRREAQEETEAAKALAERTVSE-AIAEAE-- 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2190 tlRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR----VQMEELSKLKARIEAENRALILRDKDNTQRF 2265
Cdd:NF041483 866 --RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2266 LQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKmqavqEATRLKAEAELLQQQKELAQEQA 2343
Cdd:NF041483 944 ARAEAERVRADAAAQAEqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEA-----ERVKAEAAAEAERLRTEAREEAD 1018
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2344 RRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfRKQAEEI 2413
Cdd:NF041483 1019 RTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA--RKEAERI 1086
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1722-2606 |
1.22e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.48 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1722 TEQGEQQRQLLEEELARLQREAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFREL-- 1799
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1800 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1877
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1878 RRLEEQaaqHKADIEERLAQLRKASDSelerqkglvedtlrqrRQVEEeilalkasfekaaAGKAELELELGRIRsNAED 1957
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1958 TLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2037
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2038 LAQEAAQKRLQAEEKAHAFAVQQKEQELQQTlqqeqsvldqlrgeaeaarraaeeaeearVQAEREAAQSRRQVEEAERL 2117
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKK-----------------------------ADAAKKKAEEAKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2118 KQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2197
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2198 TDHQknlldEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARiEAENRALILRDKDNtqrfLQEEAEKMKQVA 2277
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADE----AKKKAEEAKKKA 1499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2278 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeQM 2353
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK-NM 1578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2354 AQQLAEETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtlvqt 2433
Cdd:PTZ00121 1579 ALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK----- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2434 leiqrqqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDSLLQRErfiEQEK 2513
Cdd:PTZ00121 1647 ---------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---AEEA 1701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2514 AKLEQL---FQDEVAKAQqlreEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEE 2590
Cdd:PTZ00121 1702 KKAEELkkkEAEEKKKAE----ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
890
....*....|....*.
gi 41322919 2591 NQRLREQLQLLEEQHR 2606
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRR 1793
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
42-144 |
2.25e-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: 109.11 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
146-261 |
2.63e-27 |
|
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: 109.40 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
42-147 |
1.18e-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: 107.81 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1399-2116 |
1.19e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1399 EEVVrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQAL 1478
Cdd:PTZ00121 1030 EELT--EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTE 1107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1479 RARAEEaEAQKRQAQEEAERLRRqvqdeSQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQ-AEEAERRLRQAEV 1557
Cdd:PTZ00121 1108 TGKAEE-ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAA 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1558 ERARQVQVALETaqRSAEaelQSKRASFAEKtAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1637
Cdd:PTZ00121 1182 RKAEEVRKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1638 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELI 1716
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKKaDAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1717 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE-----A 1791
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADelkkaA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1792 EAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVlAEKLAAIGEATRLKTEAEIALKEKEAENErLRRLA 1870
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKK-AEEAKKKAEEAKKADEAKKKAEEAKKADE-AKKKA 1492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1871 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGR 1950
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKK 1571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1951 IRSNAEDTLRSKEQA-ELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEE----ARR 2023
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAkKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEkkKVEQLKKKEAEekkkAEE 1651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2024 LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAERE 2103
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
730
....*....|...
gi 41322919 2104 AAQSRRQVEEAER 2116
Cdd:PTZ00121 1732 AEEAKKEAEEDKK 1744
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
146-261 |
1.47e-26 |
|
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: 107.50 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
37-146 |
1.65e-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: 107.15 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 37 QDERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHR 113
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 41322919 114 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1484-2466 |
4.83e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.16 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1484 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAE--AEAAREKQRALQALEELRLQAE-EAERRLR 1553
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1554 QAEVERARQVQVA---LETAQRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeAERAREEAERE 1630
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEAI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1631 LERWQLKANEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrl 1709
Cdd:NF041483 213 LRRARKDAERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE-- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1710 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKS 1785
Cdd:NF041483 288 AKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1786 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLK 1849
Cdd:NF041483 368 KAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLR 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1850 TEAEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASDSEL 1906
Cdd:NF041483 447 GEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETL 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1907 ERQKGLVEdtlRQRRQVEEEILALKASFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEaarqrq 1974
Cdd:NF041483 527 ERTRAEAE---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD------ 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1975 laaeeerrrreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESARqlqLAQEAAQKRLQAEEKA 2053
Cdd:NF041483 598 ---------------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAER---LRTEAAADASAARAEG 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2054 HAFAVQQKEQELQQTLQQEQSVLDqlrgeaeaarraaeeaEEARVQAEREAAQSRRQVEEAERLKQSAEEQAqaraqaqa 2133
Cdd:NF041483 654 ENVAVRLRSEAAAEAERLKSEAQE----------------SADRVRAEAAAAAERVGTEAAEALAAAQEEAA-------- 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2134 aaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRL 2212
Cdd:NF041483 710 ------------------------RRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRR 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2213 KAEATEAARQRSQ-VEEELFSVRVQM-EELSKLkaRIEAENRAlilrdkDNTQRFLQEEAEKMKqvAEEAARLSVAAQEA 2290
Cdd:NF041483 766 ATELVSAAEQTAQqVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDA 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2291 ARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA 2370
Cdd:NF041483 836 NRLRREAQEETEAAKALAERTVSE---AIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2371 ERQRQL--EMSAEAERLKLRV-AEMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEKVTLVQTLEIQRQQSDH-- 2443
Cdd:NF041483 913 AQADRLigEATSEAERLTAEArAEAERLRDEARAEAERVRADAAAQAEQLiaEATGEAERLRAEAAETVGSAQQHAERir 992
|
1050 1060
....*....|....*....|....*
gi 41322919 2444 -DAERLR-EAIAELEREKEKLQQEA 2466
Cdd:NF041483 993 tEAERVKaEAAAEAERLRTEAREEA 1017
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1101-1854 |
1.58e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 117.55 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHE-EQLKEAQAVPATLPELEATKASLKKlRAQ----AEAQQPTFDALR-DELRGAQEVGERLQQRHGERDVEV 1174
Cdd:PTZ00121 1136 AEDARKAEEaRKAEDAKRVEIARKAEDARKAEEAR-KAEdakkAEAARKAEEVRKaEELRKAEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1175 ERWR----ERVAQLLERWQAVLAQTD-VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVR--EQ 1247
Cdd:PTZ00121 1215 EEARkaedAKKAEAVKKAEEAKKDAEeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1248 LR--QEQALLEEIERHGEKVEECQRFAKQYINAIKDYELqlVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSE 1325
Cdd:PTZ00121 1295 AKkaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEA-----EAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1326 LTTLTSQYIKFISETLRRMEEEERLAEQ--QRAEERERLAEVEAALEKQRQLAEaHAQAKAQAEREAKELQQRmQEEVVR 1403
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEakKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKK-AEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1404 REEAAVDAQQQKRSiqEELQQlrqsseaeiqaKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGElQALRARAE 1483
Cdd:PTZ00121 1446 ADEAKKKAEEAKKA--EEAKK-----------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKK 1511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1484 EAEAQKRQAQEEAERLRRqvqdeSQRKRQAEvelasrvkaEAEAAREKQRAlqalEELRlQAEEAERRLRQAEVERARQV 1563
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKK-----AEEAKKAD---------EAKKAEEKKKA----DELK-KAEELKKAEEKKKAEEAKKA 1572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1564 QVALETAQRSAE--AELQSKRASFAEKTAQLERSLQEEHVAvaqlreeaerraqqqaeaerareeaerelerwqlKANEA 1641
Cdd:PTZ00121 1573 EEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAK----------------------------------KAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1642 lrlRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRElaeqELEKQRQLAEGTAQQRLAAEQELIRLRAE 1721
Cdd:PTZ00121 1619 ---KIKAEELKKAEEEKKKVEQLK------------KKEAEEKKKAE----ELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1722 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakVRAEMEVllaskARAEEESRSTSEKSKQRLEAEAGRFRELAE 1801
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE---KKKAEEL-----KKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1802 EAARLRALAEEAKRQRQLAEEdaarQRAEAERVLAEKLAAIGEATRLKTEAEI 1854
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
46-143 |
2.19e-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: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 46 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 121
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 41322919 122 NDDIADGnPKLTLGLIWTIILH 143
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
164-259 |
2.76e-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: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 164 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 242
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 41322919 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
146-261 |
3.84e-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: 103.23 E-value: 3.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 146 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSV 225
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 226 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1681-2519 |
1.18e-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: 114.38 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1840
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1841 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrkaSDSELERQKGLVEDTLRQR 1920
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1921 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdtlrsKEQAELEAARQRQLaaeeerrrreaeervqkSLAAEEEA 2000
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2001 ARQRKAALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA-QKRLQA------EEKAHAFAVQQ 2060
Cdd:TIGR02168 487 LQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlGGRLQAvvvenlNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2061 KEQELQQTLQQEQSVLDQ-LRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEE-------AERLKQSAEEQAQARAQAQ 2132
Cdd:TIGR02168 567 QNELGRVTFLPLDSIKGTeIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2133 AAAEKLRKEAEQEAARRAQAEQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRL 2212
Cdd:TIGR02168 647 IVTLDGDLVRPGGVITGGSAKTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2213 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEnralilrdkdntqrfLQEEAEKMKQVAEEAARLSVAAQEAAR 2292
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2293 LRQLAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleae 2371
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2372 rqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA 2451
Cdd:TIGR02168 849 -----ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2452 IAELEREKEKLQQEAKLLQlkseemQTVQQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2519
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
158-264 |
1.35e-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: 101.21 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 158 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 234
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 41322919 235 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 264
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1403-2248 |
1.97e-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: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1403 RREEAavdaQQQKRSIQEELQQL---RQSSEAEIQAKARQAEAAERSRlRIEEEIRvvrlqleaterqrggaEGELQALR 1479
Cdd:TIGR02168 173 RRKET----ERKLERTRENLDRLediLNELERQLKSLERQAEKAERYK-ELKAELR----------------ELELALLV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1480 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLR--QAEV 1557
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1558 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLErSLQEEHVAVAQLREeaerraqqqaeaerareeaerelERWQLK 1637
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLE-ELKEELESLEAELE-----------------------ELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1638 ANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaQQRLAAEQELIR 1717
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE---AELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1718 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGR 1795
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1796 FRELAEEAARLRALAEEAKRQR--QLAEEDAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDE 1873
Cdd:TIGR02168 525 LSELISVDEGYEAAIEAALGGRlqAVVVENLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1874 AFQR--RRLEEQAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILALKASFEKAAAG----KAELELE 1947
Cdd:TIGR02168 599 GFLGvaKDLVKFDPKLRKALSYLLGGVLVVDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1948 LGRI-RSNAEDTLRSK-EQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2025
Cdd:TIGR02168 670 SSILeRRREIEELEEKiEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2026 ERAEQESARQLQLAQEAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAA 2105
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2106 QSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVE 2185
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 2186 QELTTLRLQLEETDHQKNLLDEELQRLKAEA---TEAARQRSQVEEELFSVRVQMEELSKLKARIE 2248
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIdnlQERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
162-262 |
2.02e-24 |
|
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: 100.62 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 241
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 41322919 242 DVPQPDEKSIITYVSSLYDAM 262
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
43-146 |
2.23e-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: 100.44 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 43 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 118
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1855-2519 |
2.78e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1855 ALKEKEAENERLRRLaEDEAF----QRRRLEEQAAQ------HKADIEERLAQLRKASDSELERQKGLVEdtlRQRRQVE 1924
Cdd:COG1196 177 AERKLEATEENLERL-EDILGelerQLEPLERQAEKaeryreLKEELKELEAELLLLKLRELEAELEELE---AELEELE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1925 EEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR 2004
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2005 KAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQkeqelqqtlqqeqsvldqlrgeae 2084
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL------------------------ 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2085 aarraaeeaeearVQAEREAAQSRRQVEEAERLKQSAeeqaqaraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAAD 2164
Cdd:COG1196 389 -------------LEALRAAAELAAQLEELEEAEEAL-----------------------------------LERLERLE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2165 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2244
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2245 ARIEAENRA-LILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2323
Cdd:COG1196 501 ADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2324 RLKAEAELLQQQKELAQEQARRL----QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARA 2399
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2400 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTV 2479
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 41322919 2480 QQEQLLQETQALQQSFLSEKDSLLQRERfIEQEKAKLEQL 2519
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERE-LERLEREIEAL 779
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
160-259 |
4.87e-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: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 160 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 41322919 240 D-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1101-1901 |
2.87e-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: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAvpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1180
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1181 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1260
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1261 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQyikfISET 1340
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1341 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER-------------------EAKE--LQQRMQE 1399
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegyeAAIEaaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1400 EVVRREEAAVDAQQ---QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQ 1476
Cdd:TIGR02168 550 VVVENLNAAKKAIAflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKLRKALSYLLG 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1477 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevelASRVKAEAEAAREKQRalQALEELRLQAEEAERRLR--Q 1554
Cdd:TIGR02168 624 GVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILERR--REIEELEEKIEELEEKIAelE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1555 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERW 1634
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1635 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1714
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1715 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEA 1791
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1792 EAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLa 1870
Cdd:TIGR02168 934 LEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL- 1005
|
810 820 830
....*....|....*....|....*....|.
gi 41322919 1871 edeafqrrrleeqaAQHKADIEERLAQLRKA 1901
Cdd:TIGR02168 1006 --------------TAQKEDLTEAKETLEEA 1022
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
159-263 |
3.62e-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: 97.17 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 41322919 239 EDVDVPQPDEKSIITYVSSLYDAMP 263
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
159-259 |
3.91e-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: 96.73 E-value: 3.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 41322919 239 EDVDVPQ-PDEKSIITYVSSLY 259
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1016-1584 |
3.49e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1016 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1095
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1096 RGTQGAEEVLRAHEEQLKEAQAvpATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1175
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1176 RWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqAVREQLRQEQALL 1255
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1256 EEIERHGEKVEEcqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqyik 1335
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1336 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrreEAAVDAQQQK 1415
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI----GAAVDLVASD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1416 RSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1495
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1496 AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE--TAQRS 1573
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdlEELER 767
|
570
....*....|.
gi 41322919 1574 AEAELQSKRAS 1584
Cdd:COG1196 768 ELERLEREIEA 778
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
159-257 |
4.16e-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: 93.84 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 41322919 238 PEDVDVPQPDEKSIITYVSS 257
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
42-147 |
4.96e-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: 94.77 E-value: 4.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
42-147 |
5.29e-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: 94.76 E-value: 5.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 42 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
793-859 |
6.25e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.94 E-value: 6.25e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 793 QLKPRhpAHPMRGRLPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVLSSSGSEAAVPSVCFLVP 859
Cdd:pfam17902 1 PLKQR--RSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1103-2386 |
7.47e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 101.83 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1103 EVLRAheeQLKEAQAVPATLPELEAT----KASLKKLRAQAEAQQPTFDALRdELRGAQEVGERLQQRHGERDVeverwr 1178
Cdd:NF041483 46 EVLRA---KLHEARRSLASRPAYDGAdigyQAEQLLRNAQIQADQLRADAER-ELRDARAQTQRILQEHAEHQA------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1179 ervaqlleRWQAVLAQTDV--RQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQ----LRQEQ 1252
Cdd:NF041483 116 --------RLQAELHTEAVqrRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQalaaARAEA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1253 ALLEEIERH--GEKVEECQRFAKQYI-NAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvDLRTHYSELTTL 1329
Cdd:NF041483 188 ERLAEEARQrlGSEAESARAEAEAILrRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESD-----QARRQAAELSRA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1330 TSQyikfisetlrRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqAKAQAEREAKELQQRMQEEVVRREEAav 1409
Cdd:NF041483 263 AEQ----------RMQEAEEALREARAEAEKVVAEAKEAAAKQLASAES---ANEQRTRTAKEEIARLVGEATKEAEA-- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1410 daqqqkrsIQEELQQLRQSSEAEiqAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGElQALRARAEEAEAQK 1489
Cdd:NF041483 328 --------LKAEAEQALADARAE--AEKLVAEAAEKARTVAAED--------TAAQLAKAARTAE-EVLTKASEDAKATT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1490 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRLQAEEAE--RRLRQAEVER----AR 1561
Cdd:NF041483 389 RAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAktVELQEEARRLRGEAEqlRAEAVAEGERirgeAR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1562 QVQVA-LETAQRSAEAELQSKRASFAE----KTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQl 1636
Cdd:NF041483 469 REAVQqIEEAARTAEELLTKAKADADElrstATAESERVRTEAIERATTLRRQAEET-----------------LERTR- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1637 kaNEALRLRLQAEEVAQqkslAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAegTAQQRLA-AEQEL 1715
Cdd:NF041483 531 --AEAERLRAEAEEQAE----EVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLT--AAEEALAdARAEA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1716 IRLRAET-EQGEQQRQLLEEELARLQREAAAATQK-RQELEAELAKVRAEME---VLLASKARAE-EESRSTSEKSKQRL 1789
Cdd:NF041483 603 ERIRREAaEETERLRTEAAERIRTLQAQAEQEAERlRTEAAADASAARAEGEnvaVRLRSEAAAEaERLKSEAQESADRV 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1790 EAEAGRFRE-LAEEAAR-LRALAEEAKRQRQLAEE--DAARQRAEAERVLA-----EKLA--------AIGEATRLKTEA 1852
Cdd:NF041483 683 RAEAAAAAErVGTEAAEaLAAAQEEAARRRREAEEtlGSARAEADQERERAreqseELLAsarkrveeAQAEAQRLVEEA 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1853 E------IALKEKEAENER-----LRRLAEDEAFQRRrleeQAAQHKADIEERLAQL---RKASDSELERQKGlVEDTLR 1918
Cdd:NF041483 763 DrratelVSAAEQTAQQVRdsvagLQEQAEEEIAGLR----SAAEHAAERTRTEAQEeadRVRSDAYAERERA-SEDANR 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1919 QRRQVEEEILALKASFEKAAAG--------KAELELELGRIRSNAEDTLRSKEQ--------AELEAARQRQLAAEEERR 1982
Cdd:NF041483 838 LRREAQEETEAAKALAERTVSEaiaeaerlRSDASEYAQRVRTEASDTLASAEQdaartradAREDANRIRSDAAAQADR 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1983 RREAEERVQKSLAAE--EEAARQRKAALEEVERLKAK--------VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2052
Cdd:NF041483 918 LIGEATSEAERLTAEarAEAERLRDEARAEAERVRADaaaqaeqlIAEATGEAERLRAEAAETVGSAQQHAERIRTEAER 997
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2053 AHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaq 2132
Cdd:NF041483 998 VKAEAAAEAERLRTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA----- 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2133 aaaeklrkeaeqeaarraqaeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTlrlqleetdhqknlLDEELQRL 2212
Cdd:NF041483 1073 --------------------------DTMVGAARKEAERIVAEATVEGNSLVEKARTD--------------ADELLVGA 1112
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2213 KAEATeAARQRSQveeelfsvrvqmeelsKLKARIEAENRALilrdkdnTQRFLQEEAEKMKQVAEEAARLSVAAQEaar 2292
Cdd:NF041483 1113 RRDAT-AIRERAE----------------ELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE--- 1165
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2293 lrQLAEEDLAQQRALAE---KMLKEKMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLAEETqgfQRTLE 2369
Cdd:NF041483 1166 --QLAEAEAKAKELVSDansEASKVRIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELD 1237
|
1370
....*....|....*..
gi 41322919 2370 AERQRQLEMSAEAERLK 2386
Cdd:NF041483 1238 VLVRRREDINAEISRVQ 1254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2076-2688 |
7.81e-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: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2076 LDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERlkqsaeeqaqaraQAQAAAEKLRKEAEQEAARRAQAEQA 2155
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2156 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRV 2235
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2236 QMEELsklkARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2315
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2316 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtLEAERQRQLEMSAEAERLklrvaemsRA 2395
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLLEAEADYEGF--------LE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2396 QARAEEDAQRFRKQAEEIGEKLHRTELAtqEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2475
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAY--EAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2476 MQTVQQEQLLQETQALQQSFLSEKDSLLQReRFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEA 2555
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYY-VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2556 RRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATK------TLPNG 2629
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEReelleeLLEEE 745
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2630 RDALDGPAAEAEPEHSFDGLRRKVSA--QRLQEAG---ILSAEELQRLAQGHTTVDElaRREDV 2688
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERleREIEALGpvnLLAIEEYEELEERYDFLSE--QREDL 807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1101-1901 |
3.04e-20 |
|
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: 99.75 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHE--EQLKEAQAVPATLpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDveverwr 1178
Cdd:TIGR02168 209 AEKAERYKElkAELRELELALLVL-RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1179 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQALLEEi 1258
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE-LAELEEKLEELKEELESLEA- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1259 erhgeKVEECQrfakqyiNAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDlrthySELTTLTSQYIKFIS 1338
Cdd:TIGR02168 359 -----ELEELE-------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE-----ARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevVRREEAAvdAQQQKRSI 1418
Cdd:TIGR02168 422 EIE---ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQ--LQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1419 QEELQQLRQSSEAEIQAKArqaeaaerSRLRIEEEIRVVRLQLEATERQRGGAE----GELQALRARAEEAEAQKRQAQE 1494
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALLK--------NQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1495 EAERLRR-------------QVQDESQRKRQAEVE--LASRVKAEAEAarekQRALQALEELRLQAEEAERRLRQAEVER 1559
Cdd:TIGR02168 567 QNELGRVtflpldsikgteiQGNDREILKNIEGFLgvAKDLVKFDPKL----RKALSYLLGGVLVVDDLDNALELAKKLR 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1560 ARQVQVALET-----------AQRSAEAELQSKRASFAE---KTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1625
Cdd:TIGR02168 643 PGYRIVTLDGdlvrpggvitgGSAKTNSSILERRREIEEleeKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1626 EAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTA 1705
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1706 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKS 1785
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1786 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE--- 1862
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidn 940
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 41322919 1863 -NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1901
Cdd:TIGR02168 941 lQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
163-260 |
3.74e-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: 88.56 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 163 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 241
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 41322919 242 DVPQPDEKSIITYVSSLYD 260
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1331-2061 |
4.53e-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: 99.28 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1331 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVD 1410
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1411 AQQQKRSIQEELQQLRQSSEAEIQA-----KARQAEAAERSRLRIEEE--IRVVRLQLEATERQRGGAEGELQALRARAE 1483
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESskqeiEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1484 EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQALEELRLQAEEAE-RRLRQAEVERA 1560
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleIKREAEEEEEEELEKLQEKLEQLEEELLAKkKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1561 RQVQVALETAQR-SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1639
Cdd:pfam02463 391 KLKEEELELKSEeEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1640 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELI 1716
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1717 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG-R 1795
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIlK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1796 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAF 1875
Cdd:pfam02463 631 DTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1876 QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA 1955
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1956 EDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ 2035
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740
....*....|....*....|....*....
gi 41322919 2036 LQLAQE---AAQKRLQAEEKAHAFAVQQK 2061
Cdd:pfam02463 871 ELLLKEeelEEQKLKDELESKEEKEKEEK 899
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
159-259 |
5.19e-20 |
|
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: 88.17 E-value: 5.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 238
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 41322919 239 EDVDV--PQPDEKSIITYVSSLY 259
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1339-1898 |
8.34e-20 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 98.45 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQR------AEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDA 1411
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQ-----------SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATE-----------RQRG 1469
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaalraeaaALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1470 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELrLQAEEAE 1549
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEL-IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1550 RRLRQAeVERA----------------------------RQVQVALETAQRSAEAELQSKRASFAEK--------TAQLE 1593
Cdd:COG4913 474 ERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1594 RSLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKSLAQAEAE 1663
Cdd:COG4913 553 AELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1664 KQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQ 1740
Cdd:COG4913 633 LEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1741 REAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1820
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1821 EEDAARQRAEAERVLAE--------------KLAAIGE-ATRLKTEAEIALKEKEAENERLRRLAEDEAFQrrRLEEQAA 1885
Cdd:COG4913 779 RARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIEFVA--DLLSKLR 856
|
650
....*....|...
gi 41322919 1886 QHKADIEERLAQL 1898
Cdd:COG4913 857 RAIREIKERIDPL 869
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
159-258 |
3.17e-19 |
|
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: 85.61 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 41322919 239 ED-VDVPQPDEKSIITYVSSL 258
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
155-260 |
3.42e-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: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 155 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 234
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 41322919 235 LLDPEDV-DVPQPDEKSIITYVSSLYD 260
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
162-258 |
4.66e-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: 85.06 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 162 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 237
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 41322919 238 PEDVDVPQPDEKSIITYVSSL 258
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1305-1953 |
8.34e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1305 VQSGSESVIQEYVDLRTHySELTTLTSQyIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQ 1374
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLH-ERLNGLESE-LAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1375 laeahaqAKAQAEREAKELQQRMQEEVVRREEaavdaqqqkrsIQEELQQLRQSSE---AEIQAKARQAEAAERSRLRIE 1451
Cdd:PRK02224 266 -------TIAETEREREELAEEVRDLRERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1452 EEIRVVRLQLEATERQRGGAEGELQALRARAEEaeaqkrqAQEEAERLRRQVQdesqrkrqaevelasrvkaEAEAAREK 1531
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-------LREEAAELESELE-------------------EAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1532 QRAlqALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSaeAELQSKRASFAEKTAQLERSLQEEHVAVAQlreeae 1611
Cdd:PRK02224 382 RRE--EIEELEEEIEELRERFGDAPVDLG-------NAEDFL--EELREERDELREREAELEATLRTARERVEE------ 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1612 rraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAE 1691
Cdd:PRK02224 445 ---------------------------AEALLEAGKCPECGQP---------------VEGSPHVETIEEDRERVEELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1692 qELEKQRqLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1771
Cdd:PRK02224 483 -ELEDLE-EEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1772 ARAEEEsrstSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTE 1851
Cdd:PRK02224 561 AEAEEE----AEEAREEVAELNSKLAELKERIESLERIRT------LLAAIADAEDEIER---LREKREALAE---LNDE 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1852 AEIALKEKeaeNERLRRLAEDeaFQRRRLEE------QAAQHKADIEERLAQLRKASDsELERQKGLVE------DTLRQ 1919
Cdd:PRK02224 625 RRERLAEK---RERKRELEAE--FDEARIEEaredkeRAEEYLEQVEEKLDELREERD-DLQAEIGAVEneleelEELRE 698
|
650 660 670
....*....|....*....|....*....|....*
gi 41322919 1920 RR-QVEEEILALKASFEKAaagkAELELELGRIRS 1953
Cdd:PRK02224 699 RReALENRVEALEALYDEA----EELESMYGDLRA 729
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
44-144 |
1.19e-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: 84.17 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 44 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 119
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 41322919 120 IRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1789-2622 |
1.27e-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: 94.74 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1789 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLAEKLAAIGEATRlKTEAE 1853
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1854 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILAL 1930
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1931 KASFEKAAAGKAELELELgrirsnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2010
Cdd:TIGR02168 308 RERLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2011 VERLKAKVEEARR--LRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEqelqqtlqqeqsvLDQLRGEAEAARR 2088
Cdd:TIGR02168 381 LETLRSKVAQLELqiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2089 AAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQAraqaqaaaeklrkeaeqeaarraqaeqaaLRQKQAADAEME 2168
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-----------------------------LQARLDSLERLQ 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2169 KHKKFAEQTLRQKAQVEQELTTLR---LQLEETDHQ-----KNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL 2240
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSGLSGILgvlSELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2241 SKLKARIEAENRALILRDKDNTQRFLqeeaekmKQVAEEAARLSVAAQeaARLRQLA-EEDLAQQRALAEKMLKEKMQAV 2319
Cdd:TIGR02168 579 DSIKGTEIQGNDREILKNIEGFLGVA-------KDLVKFDPKLRKALS--YLLGGVLvVDDLDNALELAKKLRPGYRIVT 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2320 QEATRL--------------------KAEAELLQQQKELAQEQARRLQ---EDKEQMAQQLAEETQGFQRTLEAERQRQL 2376
Cdd:TIGR02168 650 LDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2377 EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELE 2456
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2457 REKEKLQQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAQQLREEQQR 2536
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEE 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2537 QQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEqhrAALAHSEEVT 2616
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIE 964
|
....*.
gi 41322919 2617 ASQVAA 2622
Cdd:TIGR02168 965 DDEEEA 970
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
45-142 |
3.64e-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: 82.77 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 45 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 120
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 41322919 121 RNDDI-ADGNPKLTLGLIWTIIL 142
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1888-2689 |
3.76e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.28 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1888 KADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAEL 1967
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1968 EAARQrqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQEAAQKRl 2047
Cdd:PTZ00121 1137 EDARK------------------------AEEARKAEDAKRVEIAR---KAEDARKAEEARKAEDAKKAEAARKAEEVR- 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2048 QAEEKAHAFAVQQKEQELQQTLQQEqsvLDQLRgeaeaarraaEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQA 2127
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERK---AEEAR----------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2128 RAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEETDHQKnll 2205
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKA--- 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2206 dEELQRlKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAenralilrDKDNTQRfLQEEAEKMKQVAEEAARLSV 2285
Cdd:PTZ00121 1332 -DAAKK-KAEEAKKAAEAAKAEAE-----AAADEAEAAEEKAEA--------AEKKKEE-AKKKADAAKKKAEEKKKADE 1395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2286 AAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAEllqqQKELAQEQARRLQEDKEqmaqqlAEETQgfQ 2365
Cdd:PTZ00121 1396 AKKKAEEDKKKADE------------LKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKK------ADEAK--K 1451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2366 RTLEAERQRQLEMSAEAERlklrVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvQTLEIQRQQSDHDA 2445
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAK----KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKA 1524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2446 ERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQALQQSFLSEKD---SLLQRERFIEQEKAKLEQLF-- 2520
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMkl 1600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2521 --QDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL 2598
Cdd:PTZ00121 1601 yeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2599 QLLEEQHR----AALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRlQEAGILSAEELQRLAQ 2674
Cdd:PTZ00121 1681 KKAEEDEKkaaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKI 1759
|
810
....*....|....*
gi 41322919 2675 GHTTVDELARREDVR 2689
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1357-1901 |
8.69e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.90 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1357 EERERLAEVEAALEKQRQLAEAHAQAkaqaeREAKElqqrmQEEVVRREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAK 1436
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-----QIELLEPIRELAERYAAARERLAELEYLR--AALRLWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1437 ARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDESQ 1508
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1509 RKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQV------ALETAQRSAEAELQSKR 1582
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleaeiaSLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1583 ASFAEKTAQLERSLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL--------QAE 1649
Cdd:COG4913 447 DALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppehyaAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1650 EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAETEQG- 1725
Cdd:COG4913 503 RWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAITRAGq 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1726 --------------------------EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1779
Cdd:COG4913 583 vkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1780 STS--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRL 1848
Cdd:COG4913 663 VASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1849 KTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1901
Cdd:COG4913 743 ARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1339-2107 |
1.01e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.81 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEerlAEQQRAEERERLAEV-----EAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1413
Cdd:NF041483 524 ETLERTRAE---AERLRAEAEEQAEEVraaaeRAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALADARA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1414 Q----KRSIQEELQQLRQSSEAEIQAKARQAE----------AAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQAL 1478
Cdd:NF041483 601 EaeriRREAAEETERLRTEAAERIRTLQAQAEqeaerlrteaAADASAARAEGENVAVRLRSEAaAEAERLKSEAQESAD 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1479 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAAREKQRALQALEELrlqAEEAERRLRQAEVE 1558
Cdd:NF041483 681 RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGS---ARAEADQERERAREQSEEL---LASARKRVEEAQAE 754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1559 RARQVQvalETAQRSAEAelqskrASFAEKTAQLERSlqeehvAVAQLREEAERraqqqaeaerareeaerelerwqlka 1638
Cdd:NF041483 755 AQRLVE---EADRRATEL------VSAAEQTAQQVRD------SVAGLQEQAEE-------------------------- 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 nEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQrlaAEQELIRL 1718
Cdd:NF041483 794 -EIAGLRSAAEHAAER--TRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERTVSE---AIAEAERL 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1719 RAETEQGEQQ-------------------RQLLEEELARLQREAAA-----ATQKRQELEAELAKVRAEMEVLLASKARA 1774
Cdd:NF041483 868 RSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAqadrlIGEATSEAERLTAEARAEAERLRDEARAE 947
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1775 EEESRSTSEKSKQRLEAEAgrfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEi 1854
Cdd:NF041483 948 AERVRADAAAQAEQLIAEA------TGEAERLRAEAAETVGS---AQQHAERIRTEAERVKAE---AAAEAERLRTEAR- 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1855 alkekeAENERLRRLAEDEAFQRRRleEQAAQHKADIEERLAQLRK-ASDSELERQKGLVE-----DTLRQRRQVEEEIL 1928
Cdd:NF041483 1015 ------EEADRTLDEARKDANKRRS--EAAEQADTLITEAAAEADQlTAKAQEEALRTTTEaeaqaDTMVGAARKEAERI 1086
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1929 ALKASFE------KAAAGKAELELELGR----IRSNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEE 1998
Cdd:NF041483 1087 VAEATVEgnslveKARTDADELLVGARRdataIRERAEE-LRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE 1165
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1999 EAARQRKAALEEVERLK--------AKVEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQelqqtlq 2070
Cdd:NF041483 1166 QLAEAEAKAKELVSDANseaskvriAAVKKAEGLLKEAEQKKA---ELVREAEKIKAEAEAEAKRTVEEGKRE------- 1235
|
810 820 830
....*....|....*....|....*....|....*..
gi 41322919 2071 qeqsvLDQLrgeaeAARRAAEEAEEARVQAEREAAQS 2107
Cdd:NF041483 1236 -----LDVL-----VRRREDINAEISRVQDVLEALES 1262
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
159-258 |
5.29e-17 |
|
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: 79.51 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 238
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 41322919 239 ED-VDVPQPDEKSIITYVSSL 258
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 ... |
1485-2367 |
6.31e-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: 88.88 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1485 AEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1564
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1565 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL 1644
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1645 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1724
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1725 GEQQRQLLeEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA 1804
Cdd:pfam02463 403 EEKEAQLL-LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1805 RLRALAEEAKRQRQlaEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1884
Cdd:pfam02463 482 LQEQLELLLSRQKL--EERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1885 AQHKADIEERLAQLRKASDSeLERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1964
Cdd:pfam02463 560 VEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1965 AELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2044
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2045 KRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQ 2124
Cdd:pfam02463 719 AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2125 AQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNL 2204
Cdd:pfam02463 799 QEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEE 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2205 LDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAarls 2284
Cdd:pfam02463 879 LEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENN---- 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2285 vaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF 2364
Cdd:pfam02463 955 --------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
...
gi 41322919 2365 QRT 2367
Cdd:pfam02463 1027 VSI 1029
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
163-260 |
7.95e-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: 79.15 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 163 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 241
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 41322919 242 DVPQPDEKSIITYVSSLYD 260
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1413-2356 |
1.22e-16 |
|
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: 88.20 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1413 QQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEA----- 1487
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1488 QKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAR------EKQRALQALEELRLQAEEAERrlrQAEVERAR 1561
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEL---EAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1562 QVQVALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwqlka 1638
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAkleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL--------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 nEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQELIR 1717
Cdd:TIGR02169 367 -EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1718 LRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAEAG 1794
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHG 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1795 RFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRLAE 1871
Cdd:TIGR02169 526 TVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1872 DEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELeRQKGLVEDTLRQRRQVEEEILALKAS--FEKAAAgkaeleLELG 1949
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRMVTLEGelFEKSGA------MTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1950 RIRSNAEDTLRSKEQAELEAARQRqlaaeeerrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLRERAE 2029
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2030 Q-----ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAeeaeearvqAEREA 2104
Cdd:TIGR02169 716 RkigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---------NDLEA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2105 AQSRRQVEEAERLKQSAEeqaqaraqaqaaaeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQV 2184
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLE--------------EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2185 EQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENraliLRDKDNTQR 2264
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSELKAK 925
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2265 fLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2344
Cdd:TIGR02169 926 -LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERK 1003
|
970
....*....|..
gi 41322919 2345 RLQEDKEQMAQQ 2356
Cdd:TIGR02169 1004 AILERIEEYEKK 1015
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
161-272 |
2.02e-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: 78.11 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 41322919 241 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 272
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1598 |
3.39e-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: 86.65 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 963 HHYQQLLQSLeqgAQEESRCQRCISELKDIRLQLEA-CETRTVHRLRLPLDKEPARECAQRIAEQQK-AQAEVEGLGKGV 1040
Cdd:TIGR02168 284 EELQKELYAL---ANEISRLEQQKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEeLKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1041 ARLSAE-AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSlSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVP 1119
Cdd:TIGR02168 361 EELEAElEELESRLEELEEQLETLRSKVAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1120 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQ----T 1195
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNqsglS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1196 DVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQampLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQY 1275
Cdd:TIGR02168 520 GILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAA---KKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1276 INAIKDYELQLVTYKAQLEPVASP---------------AKKPKVQSGSESVIQEYVDLRTHYS--------ELTTL-TS 1331
Cdd:TIGR02168 597 IEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGVitggsaktNSSILeRR 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1332 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAE----AHAQAKAQAEREAKElQQRMQEEVVRREEA 1407
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAE-VEQLEERIAQLSKE 755
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1408 AVDAQQQKRSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEA 1487
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEE-----------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1488 QKRQAQEEAERLRRQVQDESQRKRQAEVELASrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAEVERArQVQVAL 1567
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERA-SLEEAL 889
|
650 660 670
....*....|....*....|....*....|.
gi 41322919 1568 ETAqRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:TIGR02168 890 ALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1336-1823 |
3.51e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.97 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1336 FISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQ-RMQEEVVRREEAAVDAQQQ 1414
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1415 KRSIQEELQQLRQSSEA------EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG-GAEGELQALRARAEEAEA 1487
Cdd:COG4717 127 LLPLYQELEALEAELAElperleELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1488 QKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVAL 1567
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELE-AAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1568 ETAqrsAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQ 1647
Cdd:COG4717 286 LAL---LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1648 AEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQ 1727
Cdd:COG4717 363 LQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1728 qrqlLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1807
Cdd:COG4717 430 ----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALK 496
|
490
....*....|....*.
gi 41322919 1808 ALAEEAKRQRQLAEED 1823
Cdd:COG4717 497 LALELLEEAREEYREE 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
966-1875 |
4.35e-16 |
|
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: 86.28 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 966 QQLLQSLEQGAQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1045
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1046 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRGTQG----AEEVLRAHEEQLKEAQ 1116
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1117 AVPATL-PELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1195
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1196 dvRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAmpladsqavreqlrqeqalleEIERHGEKVEECQRFAKQY 1275
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1276 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQR 1355
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1356 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKelqQRMQEEVVRREEAAVDAQQQKRS-------------IQEEL 1422
Cdd:TIGR02169 511 AVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAG---NRLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEA----------EIQAKARQA-----------EAAERSRlRIEEEIRVVRLQLEATERQ---RGGA-EGELQA 1477
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGGSrAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1478 LRARAEEAEAQKRQAQEEA-ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEE----LRLQAEEAERRL 1552
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeekLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1553 RQAEVERarqvqvaletaqrsaeAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelE 1632
Cdd:TIGR02169 747 SSLEQEI----------------ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------S 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1633 RWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAE 1712
Cdd:TIGR02169 792 RIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELE 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1713 QELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStsekskqrLEAE 1792
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDP 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1793 AGRFRELAEEAARLRALAEEAKR-QRQLAEEDAARQRA--EAERVLAEKLAAIGEATRLKTEAEiALKEKEAENERLRRL 1869
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRvEEEIRALEPVNMLAiqEYEEVLKRLDELKEKRAKLEEERK-AILERIEEYEKKKRE 1018
|
....*.
gi 41322919 1870 AEDEAF 1875
Cdd:TIGR02169 1019 VFMEAF 1024
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
164-259 |
6.24e-16 |
|
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: 76.63 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 164 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 242
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 41322919 243 VPQPDEKSIITYVSSLY 259
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
161-260 |
8.61e-16 |
|
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: 76.16 E-value: 8.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 41322919 241 VDV--PQPDEKSIITYVSSLYD 260
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
161-264 |
1.40e-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: 75.47 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 41322919 241 VDV--PQPDEKSIITYVSSLYDAMPR 264
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1374-1744 |
1.68e-15 |
|
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: 84.02 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1374 QLAEAHAQAKAQAEREAKELQQRMQEEVVRreeaavdaqQQKRSIQEELQQLRQSSEAEiqaKARQAEA-------AERS 1446
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1447 RLRIEEEIRVVRLQLEatERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEVELASRVK-AEA 1525
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1526 EAAREKQRALQALEELRLQAEEA-ERRLRQAEVERARqvqvaletaqrsaeaELQSKRASFAEKTAQLERSLQEEhvava 1604
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1605 qlreeaerraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQa 1683
Cdd:pfam17380 470 ---------------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE- 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1684 vrQRELAEQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1744
Cdd:pfam17380 534 --RRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
41-140 |
2.60e-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: 74.87 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 41 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 115
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 41322919 116 KLVNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4042-4080 |
3.70e-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: 3.70e-15
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 4042 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4080
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
35-143 |
3.75e-15 |
|
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: 74.24 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 35 DEQDERdrvqkkTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQ 104
Cdd:cd21219 2 GSREER------AFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCN 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322919 105 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 143
Cdd:cd21219 69 YAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1014-1588 |
5.09e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.66 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1014 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1093
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1094 VIRGTQGAEEvlraheEQLKEaqavpatlpELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1173
Cdd:COG4913 331 QIRGNGGDRL------EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1174 VERWRERVAQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVRE--QLRQE 1251
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGEliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1252 QALLEE-IER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqeyvdlrth 1322
Cdd:COG4913 473 EERWRGaIERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1323 ysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EVEAALEK--QRQLAEAH------AQAKAQAE 1387
Cdd:COG4913 539 --KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1388 REAKELQQRMQeEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAErsrlrIEEEIRvvrlQLEAterq 1467
Cdd:COG4913 617 AELAELEEELA-EAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAE-----LEAELE----RLDA---- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1468 rggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL-ASRVKAEAEAAREKQRALQALEELRlqAE 1546
Cdd:COG4913 683 ---SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERF--AA 757
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 41322919 1547 EAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEK 1588
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1690-2476 |
5.25e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 82.57 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1690 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQREA-AAATQKRQELEAELAKVRAEMEV 1766
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1767 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLaekLAAIGE 1844
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1845 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRleeQAAQHKADIEERLAQlrkasdselerqkglVEDTLRQRRQVE 1924
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARR---QAAELSRAAEQRMQE---------------AEEALREARAEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1925 EEILAlkasfekaaagkaelelelgrirsnaedtlrskeQAELEAARQrqlaaeeerrrreaeervqksLAAEEEAARQR 2004
Cdd:NF041483 282 EKVVA----------------------------------EAKEAAAKQ---------------------LASAESANEQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2005 -KAALEEVERLKAK-VEEARRLRERAEQESArqlQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrge 2082
Cdd:NF041483 307 tRTAKEEIARLVGEaTKEAEALKAEAEQALA---DARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTK---- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2083 aeaarraaeeaeearvQAEREAAQSRRQVEEAERLkqsaeeqaqaraqaqaaaeklRKeaeqeaarRAQAEQAALRQKQA 2162
Cdd:NF041483 380 ----------------ASEDAKATTRAAAEEAERI---------------------RR--------EAEAEADRLRGEAA 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2163 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEElQRLKAEATEAARQR-----SQVEEELFSVRVQM 2237
Cdd:NF041483 415 DQAEQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEG-ERIRGEARREAVQQieeaaRTAEELLTKAKADA 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2238 EELSKL------KARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAAR--LSVAAQEAARLRQLAEEDLAQQRAla 2308
Cdd:NF041483 494 DELRSTataeseRVRTEAIERATTLRRQaEETLERTRAEAERLRAEAEEQAEevRAAAERAARELREETERAIAARQA-- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2309 ekmlkekmQAVQEATRLKAEAELLQQQKELAQEQARrlqEDKEQMAQQLAEETQGfQRTLEAERQRQLEMSAEAERLKLR 2388
Cdd:NF041483 572 --------EAAEELTRLHTEAEERLTAAEEALADAR---AEAERIRREAAEETER-LRTEAAERIRTLQAQAEQEAERLR 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2389 ---VAEMSRAQARAEEDAQRFRKQAEEIGEKLH----------RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2455
Cdd:NF041483 640 teaAADASAARAEGENVAVRLRSEAAAEAERLKseaqesadrvRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETL 719
|
810 820
....*....|....*....|.
gi 41322919 2456 EREKEKLQQEAKLLQLKSEEM 2476
Cdd:NF041483 720 GSARAEADQERERAREQSEEL 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2241-2756 |
1.33e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.14 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2241 SKLKARI-EAENR-----------ALILRDKDNTQRFLQEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRAL 2307
Cdd:COG1196 168 SKYKERKeEAERKleateenlerlEDILGELERQLEPLERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2308 AEKMLKEkmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqRTLEAERQRQLEM------SAE 2381
Cdd:COG1196 244 LEAELEE---LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA---ELARLEQDIARLEerrrelEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2382 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2461
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2462 LQQEAKLLQ------LKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVA-KAQQLREEQ 2534
Cdd:COG1196 398 LAAQLEELEeaeealLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElLEEAALLEA 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2535 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2614
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2615 VTASQVAATKTLPNGRDALDGPAAEAEPEhsfdgLRRKVSAQRLQEAGILSAEELQRLAQGHTTVDELARREDVRhyLQG 2694
Cdd:COG1196 558 VAAAAIEYLKAAKAGRATFLPLDKIRARA-----ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL--VAA 630
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2695 RSSIAGLLLKATNEKLSVyAALQRQLLSPGTALILLEAQAASGFLLDPVRNRRLTVNEAVKE 2756
Cdd:COG1196 631 RLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3723-3761 |
1.39e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.39e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3723 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3761
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1101-2049 |
1.46e-14 |
|
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: 81.27 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAVpatLPELEATKASLKKLRAQAEaqqpTFDALRDELRGAqEVGERLQQrhgerdveverWRER 1180
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAE----RYQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1181 VAQLlerwQAVLAQTDVRQRELEQLGRQLRyyrESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIER 1260
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1261 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTHYSELttltsqyikfiset 1340
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1341 lrrmeeeerlaeqqraeeRERLAEVEAALEKQRQlaeahaqaKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsiqE 1420
Cdd:TIGR02169 370 ------------------RAELEEVDKEFAETRD--------ELKDYREKLEKLKREINELKRELDRLQEELQRLS---E 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1421 ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqrggAEGELQALRARAEEAEAQKRQAQEEAERLR 1500
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKK------------------QEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1501 RqvqdesqRKRQAEVELAsRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQS 1580
Cdd:TIGR02169 483 K-------ELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNVVV 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1581 KRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQqkslaqa 1660
Cdd:TIGR02169 555 EDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVE------- 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1661 eaekqkeeaereARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA------EQELIRLRAETEQGEQQRQLLEE 1734
Cdd:TIGR02169 628 ------------DIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfsrsePAELQRLRERLEGLKRELSSLQS 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1735 ELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1811
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1812 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1890
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1891 IEERLAQLRKAsDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELE 1968
Cdd:TIGR02169 856 IENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELS 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1969 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQ 2044
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....*
gi 41322919 2045 KRLQA 2049
Cdd:TIGR02169 1015 KKREV 1019
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
618-807 |
1.47e-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: 75.95 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 618 LHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQ 697
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 698 AALQTQWSWMLQLCCCIEAHLKENAAYFQFFSDVREAEGQLQKLQEALRrkySCDRSATVTRLEDLLQDAQDEKEQLNEY 777
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 41322919 778 KGHLSGLAKRAKAVVQLKPRHPAHPMRGRL 807
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2805-2843 |
1.48e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.48e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 2805 LLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEMNRVL 2843
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1635-2478 |
2.07e-14 |
|
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: 80.88 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1635 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1710
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1711 --AEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1788
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1789 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLAEKLAaigeatrLKTEAEIALKEKEAENERLRR 1868
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINE-------LEEEKEDKALEIKKQEWKLEQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1869 LAEDEAFQRRRLEEQAAQHkADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAELELEL 1948
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEY-DRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1949 GRIrsnaedtlRSKEQAELEAARQRQLAAEEERRRREAEERVQksLAAEEEAARqrkAALEEVERLKAKVEEARRLRERA 2028
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRLNNVVVEDDAVAKEAIE--LLKRRKAGR---ATFLPLNKMRDERRDLSILSEDG 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2029 EQESARQLqlaqeaaqkrLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR------------GEAEAARRAAEEAEE 2095
Cdd:TIGR02169 598 VIGFAVDL----------VEFDPKyEPAFKYVFGDTLVVEDIEAARRLMGKYRmvtlegelfeksGAMTGGSRAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2096 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2175
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2176 QTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLkaEATEAARQRSQVEEELFSVRvqmEELSKLKARIEAENRALi 2255
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLE---EEVSRIEARLREIEQKL- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2256 lrdkdNTQRFLQEEAEKMKQVAEEaARLSVAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQ 2335
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKE 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2336 KELAQEQARRLQEDKEQMAQQlaeetqgfqrtLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGE 2415
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQ-----------IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-----EEELSLE 954
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2416 KLHRTELATQEKvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2478
Cdd:TIGR02169 955 DVQAELQRVEEE---IRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
161-262 |
2.45e-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: 72.04 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 41322919 241 -VDVPQPDEKSIITYVSSLYDAM 262
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
44-144 |
2.46e-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: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 44 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 115
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 41322919 116 KLVNIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3464-3502 |
2.71e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 2.71e-14
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3464 LLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEMNRVL 3502
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
159-259 |
3.23e-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: 72.03 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 238
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 41322919 239 ED-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1101-1604 |
3.45e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRaqaeaqqptfDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1180
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1181 VAQLLERWQAVLAQTDVRQRELEQ-------LGRQLRYYRESADPLGAWLQDARRRQEQIQamplADSQAVREQLRQEQA 1253
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESLREDADDLEERAEELREEAAELE----SELEEAREAVEDRRE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1254 LLEEIERHGEKVEEcqRFAKqyinaikdyelqlvtykaqlepvaSPAKKPKVQSGSESVIQEYVDLRTHYSELTTLtsqy 1333
Cdd:PRK02224 385 EIEELEEEIEELRE--RFGD------------------------APVDLGNAEDFLEELREERDELREREAELEAT---- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1334 ikfISETLRRMEEEERLAEQ-------QRAEERERLAEVEAALEKQRQLAEAHAQAKAQaereakelqqrmQEEVVRREE 1406
Cdd:PRK02224 435 ---LRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1407 AAVDAQQQKRSIqEELQQLRQSSEAEIqakARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGELQALRARAEEA 1485
Cdd:PRK02224 500 RAEDLVEAEDRI-ERLEERREDLEELI---AERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1486 EAQKRQAQ--EEAERLRR--QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEA--ERRLRQAEVER 1559
Cdd:PRK02224 576 ELNSKLAElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDK 655
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1560 AR----QVQVALETAQRSAE-AELQSKRASFAEKTAQLErSLQEEHVAVA 1604
Cdd:PRK02224 656 ERaeeyLEQVEEKLDELREErDDLQAEIGAVENELEELE-ELRERREALE 704
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1105-1581 |
3.47e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.43 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1105 LRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRH---GERDVEVERWRERV 1181
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1182 AQlLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAW-LQDARRRQEQIQamplADSQAVREQLRQEQALLEEIER 1260
Cdd:COG4717 153 ER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1261 HGEKVEEcQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISET 1340
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1341 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrrEEAAVDAQQQKRSIQE 1420
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-----LEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1421 ELQQLRQSSEAEIQAKARQAEAAErsrlRIEEEIRVVRLQLEA--TERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1498
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1499 LRRQVQDESQRKRQaevelasrvkaeAEAAREKQRALQALEELRLQAEEAERRLRqaeveRARQVQVALETAQRSAEAEL 1578
Cdd:COG4717 451 LREELAELEAELEQ------------LEEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYREER 513
|
...
gi 41322919 1579 QSK 1581
Cdd:COG4717 514 LPP 516
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1381-2466 |
3.55e-14 |
|
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: 79.83 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1381 QAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQqlrqsSEAEIQAKARQAEAAERSRLRIEEEIrvvrlq 1460
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1461 leaterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEVELASRVKAEAEAAREKQRALQALEE 1540
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1541 LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT-AQLERSLQEEHVAVAQLREEAERRAQQQAE 1619
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1620 AERAREEAERELE--RWQLKANE----ALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK-AEEQAVRQRELAEQ 1692
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLAKKEeelqAALARLEEETAQKNNALKKIRELEAQISELQEDLESERaARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1693 ELEKQRQLAEGT-----AQQRLAA--EQELIRLR----AETEQGEQQRQ-----------LLEEELARLQREAAAATQKR 1750
Cdd:pfam01576 300 ELEALKTELEDTldttaAQQELRSkrEQEVTELKkaleEETRSHEAQLQemrqkhtqaleELTEQLEQAKRNKANLEKAK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1751 QELEAELAKVRAEMEVLLASKaraeeesrSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE--AKRQRQLAEEDAARQR 1828
Cdd:pfam01576 380 QALESENAELQAELRTLQQAK--------QDSEHKRKKLEGQLQELQARLSESERQRAELAEklSKLQSELESVSSLLNE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1829 AEAERV-LAEKLAAIG-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdieeRLA 1896
Cdd:pfam01576 452 AEGKNIkLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1897 QLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLrskeqaeLEAARQRQLA 1976
Cdd:pfam01576 528 DMKK----KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLV 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1977 AEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahaf 2056
Cdd:pfam01576 597 SNLEKKQKKF-----DQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE------ 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2057 avqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqAAAE 2136
Cdd:pfam01576 666 -------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA------------TEDA 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2137 KLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA 2216
Cdd:pfam01576 715 KLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQI 786
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2217 TEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMkQVAEEAARLSVAAQEAARLRQL 2296
Cdd:pfam01576 787 DAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDE 865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2297 AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEA----ER 2372
Cdd:pfam01576 866 LADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESArqqlER 945
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2373 Q------RQLEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDA 2445
Cdd:pfam01576 946 QnkelkaKLQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQA 1025
|
1130 1140
....*....|....*....|.
gi 41322919 2446 ERLREAIAELEREKEKLQQEA 2466
Cdd:pfam01576 1026 EKGNSRMKQLKRQLEEAEEEA 1046
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1069-1598 |
5.94e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.93 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1069 LTLGKLEQVRSLSAiylEKLKTISLVIRGTQGAEEVLRAHEEQlKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDA 1148
Cdd:PRK02224 159 LQLGKLEEYRERAS---DARLGVERVLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1149 LRDElrgAQEVGErlqqRHGERDVEVERWRERVAQLlerwQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARR 1228
Cdd:PRK02224 235 TRDE---ADEVLE----EHEERREELETLEAEIEDL----RETIAET---EREREELAEEVRDLRERLEELEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1229 RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSG 1308
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1309 SESVIQEYVDlrthySELTTLTSQYiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahAQAKAQAER 1388
Cdd:PRK02224 381 DRREEIEELE-----EEIEELRERF-GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE-----RVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 EAKELQQRMQE-EVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---------EIQAKARQAEAAERSRLRIEEEIRVVR 1458
Cdd:PRK02224 450 EAGKCPECGQPvEGSPHVETIEEDRERVEELEAELEDLEEEVEEveerleraeDLVEAEDRIERLEERREDLEELIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1459 LQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS--RVKAEAEAAREKQRALQ 1536
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIE 609
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1537 ALEELR--LQAEEAERRLRQAEV-ERARQVQVALETAqrsAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:PRK02224 610 RLREKReaLAELNDERRERLAEKrERKRELEAEFDEA---RIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1065-1930 |
6.29e-14 |
|
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: 78.96 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1065 SELELTLGKLEQVRslsaiylEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATK--ASLKKLRAQAEAQ 1142
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1143 QPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDVR--QRELEQLGRQLRYYRESadplg 1220
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1221 awLQDARRRQEQIQAmpladsqavreqlrQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1300
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1301 KKPKvqsgsesviQEYVDLRTHYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1380
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1381 QAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ 1460
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1461 LEATERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQaeVELASRVKA------EAEAAREK 1531
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEA--IELLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1532 QRALQALEE-----LRLQAEEAERRLRQA--EVERARQVQVALETAQR--------SAEAELQSKRA-----SFAEKTAQ 1591
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAfkYVFGDTLVVEDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1592 LERSLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQaEEVAQQKSLAQAEAEKQKEEAER 1671
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQ-SELRRIENRLDELSQELSDASRK 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1672 EARRRGKAEEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQreAAAATQKRQ 1751
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSS-LEQEIENVKSELKELEARIEE-------LEEDLHKLE--EALNDLEAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1752 ELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1831
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREI-EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1832 ERVLAEKLAAI----GEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQL--RKASDSE 1905
Cdd:TIGR02169 867 EEELEELEAALrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK-LEALEEELSEIedPKGEDEE 945
|
890 900
....*....|....*....|....*
gi 41322919 1906 LERQKGLVEDTLRQRRQVEEEILAL 1930
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
159-256 |
7.54e-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: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 41322919 238 PEDVDVPQPDEKSIITYVS 256
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1326-2220 |
8.47e-14 |
|
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: 78.68 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1326 LTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEV----EAALEKQRQLAEAHAQAkAQAEREAKELQQRMQEEV 1401
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqEQIAELQAQIAELRAQL-AKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1402 VRREEAavdaQQQKRSIQEELQQLRQSSEAEIQAKARqaeaAERSRLRIEEEIRVVRLQLEATErqrgGAEGELQALRAR 1481
Cdd:pfam01576 257 AQKNNA----LKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1482 AE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsrvkaeaEAAREKQRALQALEELRlQAEEAERRLRQAEVERA 1560
Cdd:pfam01576 325 REqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1561 RQVQVALETAQRSAEAELQSKRASFAEktAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANE 1640
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1641 ALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRA 1720
Cdd:pfam01576 475 ELL----QEETRQKLNLSTRLRQL---------------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1721 ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEAG 1794
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQK 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1795 RFRELaeeaarlraLAEEAKRQRQLAEEdaaRQRAEAERVLAEKLA-----AIGEATRLKTEAEIALKEKEAENERLRRL 1869
Cdd:pfam01576 605 KFDQM---------LAEEKAISARYAEE---RDRAEAEAREKETRAlslarALEEALEAKEELERTNKQLRAEMEDLVSS 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1870 AEDEAFQ-------RRRLEEQAAQHKADIEERLAQLRKASDSEL-------------------------ERQKGLVedtl 1917
Cdd:pfam01576 673 KDDVGKNvhelersKRALEQQVEEMKTQLEELEDELQATEDAKLrlevnmqalkaqferdlqardeqgeEKRRQLV---- 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1918 RQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE 1997
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQS 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1998 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSV 2075
Cdd:pfam01576 829 KESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELL 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2076 LDQLRgeaeaARRAAEEAEEARVQAEREAAQSRRQV-EEAERLKQSAEEQAQARAQAQAAAEKLR-KEAEQEAARRAQAE 2153
Cdd:pfam01576 909 NDRLR-----KSTLQVEQLTTELAAERSTSQKSESArQQLERQNKELKAKLQEMEGTVKSKFKSSiAALEAKIAQLEEQL 983
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2154 QAALRQKQAADA--------------EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQK---NLLDEELQRLKAEA 2216
Cdd:pfam01576 984 EQESRERQAANKlvrrtekklkevllQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEAsraNAARRKLQRELDDA 1063
|
....
gi 41322919 2217 TEAA 2220
Cdd:pfam01576 1064 TESN 1067
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1059-1812 |
1.53e-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: 77.70 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1059 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKTIslvirgtQGAEEVLRAHEEQLKE-AQAVPATLPELEATKASLKKLRA 1137
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSL-------HGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1138 QAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQlgRQLRYYRESAD 1217
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1218 PLGAWLQDARRRQEQI---QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1294
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1295 pvaspAKKPKVQSGSesviqeyvdlrthySELTTLTSQYIKFISETLRRMEEEERLAeqqRAEERERLAEVEAALekQRQ 1374
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAEL--CAA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1375 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE-AAERSRLRIEEE 1453
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGP 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1454 IRVVRLQLEATERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQRKRQAEVELASRVKAEAE 1526
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSeedvYHQLTSERKQRASLKEQMQEIQQSFSILtqcDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1527 AAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK--------RASFAEKTAQLERSLQE 1598
Cdd:TIGR00618 606 AEDMLACEQHA-LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1599 EHVAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArr 1675
Cdd:TIGR00618 685 MQSEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE-- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1676 rgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQREAAAATQKR 1750
Cdd:TIGR00618 762 ----AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRL 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1751 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE 1812
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1709-2477 |
2.22e-13 |
|
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: 77.14 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1709 LAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1788
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1789 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEIAL-KEKEAENERL 1866
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1867 RRL---AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKglvedtlrQRRQVEEEILALKASFEKAAAGKAE 1943
Cdd:pfam01576 162 SEFtsnLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK--------AKRKLEGESTDLQEQIAELQAQIAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1944 LELELgrirsnaedtlrSKEQAELEAARQRqlaaeeerrrreaeervqkslaAEEEAArQRKAALEEVERLKAKVEEarr 2023
Cdd:pfam01576 234 LRAQL------------AKKEEELQAALAR----------------------LEEETA-QKNNALKKIRELEAQISE--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2024 LRERAEQESArqlQLAQEAAQKRLQAEEkahafavqqkeqelqqtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAERE 2103
Cdd:pfam01576 276 LQEDLESERA---ARNKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2104 AAQSRRQVEEAERLKQSAEEqaqaraqaqaaaeKLRKEAEQEAARRAQAeqaaLRQKQAADAEMEKHKKFAEQtlrQKAQ 2183
Cdd:pfam01576 329 VTELKKALEEETRSHEAQLQ-------------EMRQKHTQALEELTEQ----LEQAKRNKANLEKAKQALES---ENAE 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2184 VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALilrDKD--- 2260
Cdd:pfam01576 389 LQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDvss 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2261 ------NTQRFLQEEAekmKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLqq 2334
Cdd:pfam01576 466 lesqlqDTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL-- 540
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2335 qkELAQEQARRLQEDKEQMAQQLAEETQGFQR---------------TLEAERQRQLEMSAEAERLKLR--VAEMSRAQA 2397
Cdd:pfam01576 541 --EALEEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLVSNLEKKQKKFDqmLAEEKAISA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2398 RAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA-------IAELEREKEKLQQEAKLLQ 2470
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknVHELERSKRALEQQVEEMK 698
|
....*..
gi 41322919 2471 LKSEEMQ 2477
Cdd:pfam01576 699 TQLEELE 705
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
159-259 |
2.82e-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: 68.90 E-value: 2.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 238
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 41322919 239 ED-VDVPQPDEKSIITYVSSLY 259
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2175-2470 |
3.46e-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: 76.32 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2175 EQTLRQKAQVEQELTTLRLQLEETDHQKNLlDEELQRLKAEATEAARQRSQVEEELFSV--RVQMEELSKLK-------A 2245
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2246 RIEAENRALILRDKDNTQRFLQEEaekmKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALAEKMLKEKMQAVQEATRL 2325
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEE----RKRELERIRQEEIAMEISRMREL--ERLQMERQQKNERVRQELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2326 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDaQR 2405
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2406 FRKQAEEIGEKLHRTELAT--------QEKVTLVQTLEIQRQQSDHDAERLREaiAELEREKEKLQQEAKLLQ 2470
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEErkqamieeERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEMEERRRIQ 555
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3057-3095 |
4.96e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 4.96e-13
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3057 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEFHEKL 3095
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
62-141 |
6.62e-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: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 62 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 133
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 41322919 134 LGLIWTII 141
Cdd:cd21223 105 LALLWRII 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1678-1894 |
7.96e-13 |
|
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: 73.64 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1757
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1833
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1834 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1894
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-147 |
1.93e-12 |
|
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: 66.88 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 46 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1693-2474 |
2.87e-12 |
|
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: 73.46 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1693 ELEKQRQLAEGTAQQRLAAEQELIRLRAE----TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvll 1768
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1769 askaRAEEESRSTSEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLAEKLAAIGEATRL 1848
Cdd:TIGR00618 251 ----AQEEQLKKQQLLKQLRARIE-----ELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1849 KTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR-RQVEEEI 1927
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1928 LALKASFEKAAAGKAELELELGRIrsNAEDTLRSKEQAELEAAR-QRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2006
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2007 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQlrgeaEAA 2086
Cdd:TIGR00618 467 SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQT-----YAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2087 RRAAEEAEEARVQAEREAAQSRRqvEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEqeaarraqaeqaalRQKQAADAE 2166
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLK--EQMQEIQQSFSILTQCDNRSKEDIPNLQNITV--------------RLQDLTEKL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2167 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQrLKAEATEAARQRsqVEEELFSVRVQMEELSKLKar 2246
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA-LHALQLTLTQER--VREHALSIRVLPKELLASR-- 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2247 ieaenralilrdkdntQRFLQEEAEKMKQVAEEAARLsvaAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK 2326
Cdd:TIGR00618 679 ----------------QLALQKMQSEKEQLTYWKEML---AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2327 AEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRF 2406
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2407 RKQAEEIGEKLHRTELATQEKVTLVQTLeiqRQQSDHDAERLReaiaeleREKEKLQQEAKLLQLKSE 2474
Cdd:TIGR00618 820 NLQCETLVQEEEQFLSRLEEKSATLGEI---THQLLKYEECSK-------QLAQLTQEQAKIIQLSDK 877
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
161-256 |
3.03e-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: 65.87 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 239
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 41322919 240 DVDVPQPDEKSIITYVS 256
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1313-2060 |
3.20e-12 |
|
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: 73.45 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1313 IQEYVDLRTHYSELTTLTSQYikFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKE 1392
Cdd:COG3096 248 IRVTQSDRDLFKHLITEATNY--VAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARE-SD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1393 LQQRMQ--EEVVRREEAAVDAQQQKRSIQEELQQL----RQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLeaTER 1466
Cdd:COG3096 325 LEQDYQaaSDHLNLVQTALRQQEKIERYQEDLEELterlEEQEEVVEEAAEQLAEAEARLE-AAEEEVDSLKSQL--ADY 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1467 QRGgaegeLQALRARAeeaeAQKRQAQEEAERLRRQVQDESQRKRQAEVELAsRVKAEAEAAREKQRALqaleELRLQ-A 1545
Cdd:COG3096 402 QQA-----LDVQQTRA----IQYQQAVQALEKARALCGLPDLTPENAEDYLA-AFRAKEQQATEEVLEL----EQKLSvA 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1546 EEAERRLRQA---------EVERARQVQVALETAQRSAEAELQSKRAS-FAEKTAQLERSLQEEHVAVAQLRE---EAER 1612
Cdd:COG3096 468 DAARRQFEKAyelvckiagEVERSQAWQTARELLRRYRSQQALAQRLQqLRAQLAELEQRLRQQQNAERLLEEfcqRIGQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1613 RAQQQAEAERAREEAERELERWQLKANEAL--RLRLQAEEV---AQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQR 1687
Cdd:COG3096 548 QLDAAEELEELLAELEAQLEELEEQAAEAVeqRSELRQQLEqlrARIKELAARAPAWL------------AAQDALERLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1688 ELAEQELEKQRQLAEgTAQQRLAAEQELIRLRaetEQGEQQRQLLEEELARLQREAAAATQKRQEL-------------- 1753
Cdd:COG3096 616 EQSGEALADSQEVTA-AMQQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALaerlggvllseiyd 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1754 ----------EA------------ELAKVRAEMEVLL-----------------ASKARAEEESRSTSEKSKQRlEAEAG 1794
Cdd:COG3096 692 dvtledapyfSAlygparhaivvpDLSAVKEQLAGLEdcpedlyliegdpdsfdDSVFDAEELEDAVVVKLSDR-QWRYS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1795 RFREL-----AEEAARLRALAEEAKR-QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEnerlRR 1868
Cdd:COG3096 771 RFPEVplfgrAAREKRLEELRAERDElAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQR----RS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1869 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKAsdseLERQKGLVEDTLRQRRQVEEEIL--ALKASFEKAAAGKA--EL 1944
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQLLNKL----LPQANLLADETLADRLEELREELdaAQEAQAFIQQHGKAlaQL 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1945 ELELGRIRSNAE--DTLrskeQAELEAARQRQlaAEEERRRREAEERVQKSLA-AEEEAARQRKAALEEVERLKAKVEEA 2021
Cdd:COG3096 923 EPLVAVLQSDPEqfEQL----QADYLQAKEQQ--RRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQA 996
|
810 820 830
....*....|....*....|....*....|....*....
gi 41322919 2022 RRLRERAeQESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2060
Cdd:COG3096 997 EEARREA-REQLRQAQAQYSQYNQVLASLKSSRDAKQQT 1034
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1717-2271 |
3.45e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1717 RLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1796
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1797 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1870
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1871 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---DSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAEL 1944
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1945 ELELGRIRSNAEDtLRSKE---QAELEAARQR-----------------QLAAEEERRRREAEERVQKS-LAAEEEAARQ 2003
Cdd:PRK02224 411 EDFLEELREERDE-LREREaelEATLRTARERveeaealleagkcpecgQPVEGSPHVETIEEDRERVEeLEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2004 RKAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKahafavQQKEQELQQTLQQEQSVLDQLRGE 2082
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEK------RERAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2083 AEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSaeeqaqaraqaqaaaeklrkeaeQEAARRAQAEQAALRQKQA 2162
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-----------------------LAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2163 ADAEMEKHKKFAEQTLRQ-KAQVEQELTTLRlqLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELS 2241
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE 694
|
570 580 590
....*....|....*....|....*....|.
gi 41322919 2242 KLKARIEA-ENRALILRDkdntqrfLQEEAE 2271
Cdd:PRK02224 695 ELRERREAlENRVEALEA-------LYDEAE 718
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4311-4349 |
4.17e-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: 4.17e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 4311 LLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMVDRI 4349
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
161-260 |
4.54e-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: 65.05 E-value: 4.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 236
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 41322919 237 DPEDVdVPQPDEKSIITYVSSLYD 260
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
161-261 |
6.03e-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: 65.07 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 161 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 240
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 41322919 241 VdVPQPDEKSIITYVSSLYDA 261
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1356-2292 |
6.23e-12 |
|
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: 72.68 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1356 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVvrreeaavdAQQQKRsiQEELQQLRQSSE---AE 1432
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMAREL---------EELSAR--ESDLEQDYQAASdhlNL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1433 IQAKARQAEAAERSRLRIEEeirvVRLQLEATERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQ 1512
Cdd:COG3096 339 VQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1513 AEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAElqskrasfaEKTAQL 1592
Cdd:COG3096 404 ALDVQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQF 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1593 ERSLQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkee 1668
Cdd:COG3096 475 EKAYE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA------------ 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1669 aerearRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQREAAAATQ 1748
Cdd:COG3096 520 ------QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1749 KRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1818
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1819 LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE-----------IALKEKEAENERLRRL----------------AE 1871
Cdd:COG3096 666 PGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYfsalygparhaIVVPDLSAVKEQLAGLedcpedlyliegdpdsFD 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1872 DEAFQRRRLEEQAAQHKADI------------------EERLAQLRKASDSELERQKGLVEDTLRQRRQVE--EEILALK 1931
Cdd:COG3096 746 DSVFDAEELEDAVVVKLSDRqwrysrfpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQafSQFVGGH 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1932 ASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAE------LEAARQR---------QLAAEEERRRREAEERVQKSLAA 1996
Cdd:COG3096 826 LAVAFAPDPEAELA-ALRQRRSELERELAQHRAQEqqlrqqLDQLKEQlqllnkllpQANLLADETLADRLEELREELDA 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1997 EEEAAR---QRKAALEEVERLkakveeARRLRERAEQESARQLQLAQ-EAAQKRLQAEEKAHAFAVQQKE----QELQQT 2068
Cdd:COG3096 905 AQEAQAfiqQHGKALAQLEPL------VAVLQSDPEQFEQLQADYLQaKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2069 LQQEQSVLDQLRgeaeaarraaeeaeEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAA 2147
Cdd:COG3096 979 LGENSDLNEKLR--------------ARLEQAEEARREAREQLRQAqAQYSQYNQVLASLKSSRDAKQQTLQELEQELEE 1044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2148 RRAqaeqaalrqkqAADAEMEkhkkfaEQTLRQKAQVEQELTTLRLqleetdhQKNLLDEELQRLKAEATEAARQRSQVE 2227
Cdd:COG3096 1045 LGV-----------QADAEAE------ERARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAE 1100
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2228 EELFSVRvqmEELSKLKARIEAENRalILRDKD-----NTQRFLQEEAEKMKQVAEE---AARLSVAAQEAAR 2292
Cdd:COG3096 1101 RDYKQER---EQVVQAKAGWCAVLR--LARDNDverrlHRRELAYLSADELRSMSDKalgALRLAVADNEHLR 1168
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3133-3171 |
6.79e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 6.79e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3133 LLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEETSRAL 3171
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2729-2767 |
7.41e-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: 7.41e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 2729 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2767
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1101-1832 |
7.49e-12 |
|
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: 72.29 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQ--RHGERdveVERWR 1178
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEK---IERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1179 ERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLEEI 1258
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1259 ERHGEKVEECQRFAKQYINAIKDYELQLVT-------YKAQ-------LEPVASPAKKPKVQSGSESVIQEYVDLRTHYS 1324
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadaARRQfekayelVCKIAGEVERSQAWQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1325 ELTTLTSQYiKFISETLRRMEEEERLAEQ------QRAEERERLAEVEAALEKQR----QLAEAHAQAKAQAEREAKELQ 1394
Cdd:COG3096 513 RLQQLRAQL-AELEQRLRQQQNAERLLEEfcqrigQQLDAAEELEELLAELEAQLeeleEQAAEAVEQRSELRQQLEQLR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1395 QRMQEeVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaERSRLRIEEEIRVVRLQLEATER---QRGGA 1471
Cdd:COG3096 592 ARIKE-LAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER-EREATVERDELAARKQALESQIErlsQPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1472 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1509
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1510 KRQaEVELASRVKAE---------------AEAAREKQralqaLEELRLQAEE-----AERRLRQAEVER---------A 1560
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1561 RQVQVALETaqrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELER 1633
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1634 WQLKANEALR-LRLQAEEVAQ-QKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1710
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQlEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1711 AEQELI-RLRAETEQGEQQRQLLEEELARLQREAAAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1775
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1776 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1832
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3966-4004 |
9.84e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 9.84e-12
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3966 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 4004
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3799-3837 |
1.04e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.04e-11
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3799 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3837
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1688-2538 |
2.09e-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: 70.97 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1688 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAeME 1765
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1766 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1845
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1846 TRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASDSELER 1908
Cdd:pfam01576 267 REL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEETRS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1909 QKGLVEDTLRQRRQVEEEilaLKASFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAARQRQlaaeeerrrrE 1985
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK----------K 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1986 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARqlqLAQEAAQKRLQaeekahafaVQQKEQEL 2065
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSSLESQ---------LQDTQELL 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2066 QQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQE 2145
Cdd:pfam01576 478 QEETRQKLNLSTRLR------------------QLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2146 AARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLeetDHQKNLL----------DEELQRLKAE 2215
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDL---DHQRQLVsnlekkqkkfDQMLAEEKAI 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2216 ATEAARQRSQVEEE-------LFSVRVQMEELSKLKARIEAENRAL------ILRDKDNTQRFLQEeAEKMKQVAEeaar 2282
Cdd:pfam01576 617 SARYAEERDRAEAEareketrALSLARALEEALEAKEELERTNKQLraemedLVSSKDDVGKNVHE-LERSKRALE---- 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2283 lsvaaQEAARLR-QLAE-EDLAQQRALAEKMLKEKMQAvqeatrLKAEAEL-LQQQKELAQEQARRLQEDKEQMAQQLAE 2359
Cdd:pfam01576 692 -----QQVEEMKtQLEElEDELQATEDAKLRLEVNMQA------LKAQFERdLQARDEQGEEKRRQLVKQVRELEAELED 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2360 ETQgfQRTLEAERQRQLEMsaEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQ 2439
Cdd:pfam01576 761 ERK--QRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLK 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2440 QSDHDAERLREAIAELEREKEKLQQEAKLLQlksEEMQtvqqeqllqetqalqqSFLSEKDSLLQRERFIEQEKAKLEQL 2519
Cdd:pfam01576 837 NLEAELLQLQEDLAASERARRQAQQERDELA---DEIA----------------SGASGKSALQDEKRRLEARIAQLEEE 897
|
890
....*....|....*....
gi 41322919 2520 FQDEVAKAQQLREEQQRQQ 2538
Cdd:pfam01576 898 LEEEQSNTELLNDRLRKST 916
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1473-2051 |
2.18e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAevELASRVKAEAEAAREKQRALQALEELRLQAEEA--ER 1550
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1551 RLRQAEVERARQVQVALETA---QRSAEAELQSKRASFAEKTAQLERSLQEehvavaqlreeaerraqqqAEAERAREEA 1627
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1628 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1702
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1703 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1769
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1770 ----SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1843
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1844 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASDSELERQKGLVE 1914
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1915 ------DTLRQRRqveEEILALKASFEKAAAGKAELElelgriRSNAEDTLR--SKEQAELEAARQRqlaaeeerrrrea 1986
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEqvEEKLDELREERDD------------- 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1987 eerVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2051
Cdd:PRK02224 679 ---LQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1406-1606 |
2.61e-11 |
|
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: 69.02 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1406 EAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEA 1485
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK----ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1486 EAQKRQAQEEAERLRRQVQdesQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL-----RQAEVERA 1560
Cdd:COG4942 96 RAELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLaelaaLRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322919 1561 RQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1606
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2158-2360 |
2.75e-11 |
|
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: 69.02 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2158 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEEL---FSVR 2234
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaelLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2235 VQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2314
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322919 2315 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEE 2360
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1154-1577 |
2.95e-11 |
|
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: 70.37 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1154 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDVR----QRELEQLGR 1207
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRrselERELAQHRA 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1208 QLRYYRESADPLGAWLQDARRRQEQiqAMPLADSQAvreqlrqeQALLEEIERHGEKVEECQRFAKQYINAIkdyelqlv 1287
Cdd:COG3096 858 QEQQLRQQLDQLKEQLQLLNKLLPQ--ANLLADETL--------ADRLEELREELDAAQEAQAFIQQHGKAL-------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1288 tykAQLEPVASPAKKPKVQSgsESVIQEYVDLrthySELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEE--R 1359
Cdd:COG3096 920 ---AQLEPLVAVLQSDPEQF--EQLQADYLQA----KEQQRRLKQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklR 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1360 ERLAEVEAALEKQRQLAEAHAQAKAQAereakelQQRMQEEVVRREEAavdaQQQKRSIQEELQQLrqsseaEIQAKARQ 1439
Cdd:COG3096 991 ARLEQAEEARREAREQLRQAQAQYSQY-------NQVLASLKSSRDAK----QQTLQELEQELEEL------GVQADAEA 1053
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1440 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQ 1512
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRL 1133
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1513 AEVELasrvkaeaeaarekqrALQALEELRLQAEEAERRLRQAeVERARQVQVALETAQRSAEAE 1577
Cdd:COG3096 1134 HRREL----------------AYLSADELRSMSDKALGALRLA-VADNEHLRDALRLSEDPRRPE 1181
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1124-1505 |
3.28e-11 |
|
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: 70.09 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1124 ELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWqavlAQTDVRQRELE 1203
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI----AQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1204 QLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAlleEIERHGEKVEECQRFAKQYINAIKDYE 1283
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1284 LQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrthyselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLA 1363
Cdd:TIGR02168 838 RRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1364 EVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAA 1443
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1444 ERSRLRIEEEI-RVVRLQLEATErqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1505
Cdd:TIGR02168 971 RRRLKRLENKIkELGPVNLAAIE--------EYEELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1426-2052 |
3.56e-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: 70.25 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1426 RQSSEAEIQAKARQAEA--AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1499
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1500 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAeLQ 1579
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1580 SKRASFAEKTAQLERSLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1658
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1659 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1737
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1738 RLQREAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE 1811
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1812 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1891
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1892 EERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEkaaagkAELELELGRIRSN--AEDTLRSKEQAELEA 1969
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKAELKALET 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1970 ARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAA------------LEEVERLKAKVEEARRLRERAEQESARQl 2036
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREiRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARL- 833
|
650
....*....|....*.
gi 41322919 2037 qlaQEAAQKRLQAEEK 2052
Cdd:pfam12128 834 ---IADTKLRRAKLEM 846
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
36-138 |
3.88e-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: 63.21 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 36 EQDERDRVqkktFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIAL 107
Cdd:cd21300 4 EGEREARV----FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAV 77
|
90 100 110
....*....|....*....|....*....|.
gi 41322919 108 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 138
Cdd:cd21300 78 ELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1332-1971 |
8.28e-11 |
|
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: 68.99 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1332 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDA 1411
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQ---SSEAEIQA-KARQAEAAERSRLRIEEEIRVVRLQLE----ATERQRGGAEGELQALRAR-- 1481
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHFRslgsAISKILRELDTEISYLKGRif 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1482 --AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASrVKAEAEAAREKQRALQAleelrlQAEEAERRLRQAEVE 1558
Cdd:pfam15921 242 pvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEITG-LTEKASSARSQANSIQS------QLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1559 RARQVQvALETAQRSAEAELQSKRASFAEKTAQLERSLQeehVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1638
Cdd:pfam15921 315 YMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 NEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EGTAQQRL 1709
Cdd:pfam15921 391 KE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQGQMERQM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1710 AAEQ----ELIRLRAETEQGEQQRQLLEEELARLqreaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESRSTSEKS 1785
Cdd:pfam15921 451 AAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATNAEITKL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1786 KQRLEAEAGRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAEIALKEK 1859
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1860 EAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASDSELERQKGL--VEDTLRQRRQVEEEILALKAS 1933
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDYEVLKRN 682
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 41322919 1934 F----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAAR 1971
Cdd:pfam15921 683 FrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMK 727
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1782-2519 |
8.91e-11 |
|
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: 68.94 E-value: 8.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1782 SEKSKQRLEAEagrfrELAEEAARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 1859
Cdd:TIGR02169 170 RKKEKALEELE-----EVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1860 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAA 1938
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1939 AGKAELELELGRIRSNAEDtlrSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 2015
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2016 AKVEE----ARRLRERAEQESARQLQLAQ-----EAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2086
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAaiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2087 RraaeeaeearvQAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA 2165
Cdd:TIGR02169 479 D-----------RVEKELSKLQRELAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2166 EME-----------------KHKKFAEQTLRQKAQVEQELTTLRLQLEE--TDHQKNLLDEELQRlkAEATEAARQRSQV 2226
Cdd:TIGR02169 548 RLNnvvveddavakeaiellKRRKAGRATFLPLNKMRDERRDLSILSEDgvIGFAVDLVEFDPKY--EPAFKYVFGDTLV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2227 EEELFSVRVQMeelskLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRA 2306
Cdd:TIGR02169 626 VEDIEAARRLM-----GKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL--SSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2307 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLK 2386
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2387 LRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEA 2466
Cdd:TIGR02169 779 EALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2467 KLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDSLLQRERfiEQEKAKLEQL 2519
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRD------LESRLGDLKKER--DELEAQLREL 901
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1359-1884 |
9.48e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 68.73 E-value: 9.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1359 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR 1438
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1439 QAEAAERSRLRIEEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEV 1515
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1516 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERS 1595
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1596 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1675
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1676 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA 1755
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1756 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1835
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 41322919 1836 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1884
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1681-2114 |
1.07e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR--------QLLEEELARLQREAAAATQKRQE 1752
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1753 L--------------EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR----------- 1807
Cdd:COG4913 364 LeallaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1808 ----ALAEEAKRQR----------QLAEEDAARQRAeAERVL-------------AEKLAAIGEATRLKTEAEIALKEKE 1860
Cdd:COG4913 444 alrdALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLggfaltllvppehYAAALRWVNRLHLRGRLVYERVRTG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1861 AENERLRRLAED-------------EAFQRRRLEEQAAQHKADIEERLAQLRKA-------SDSELERQKG--------- 1911
Cdd:COG4913 523 LPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSPEELRRHPRAitragqvKGNGTRHEKDdrrrirsry 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1912 -LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsnaedtlrskeQAELEAARQRQLAAEEERRRREAEERV 1990
Cdd:COG4913 603 vLGFDNRAKLAALEAELAELEEELAEAEERLEAL-------------------EAELDALQERREALQRLAEYSWDEIDV 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1991 QkSLAAEEEAARQRKAALE----EVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQ 2066
Cdd:COG4913 664 A-SAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 41322919 2067 QTLQQEQSVLDQLRGEAEAARRAAEEA--EEARVQAEREAAQSRRQVEEA 2114
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELREnlEERIDALRARLNRAEEELERA 792
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1313-1811 |
1.15e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1313 IQEYVDLRTHYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKE 1392
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1393 LQQRMQeevvrreeAAVDAQQqkrSIQEELQQlrqsSEAEIQAKARQAEAAErsrlRIEEEIRVVRlqlEATERQrggae 1472
Cdd:PRK04863 326 LEQDYQ--------AASDHLN---LVQTALRQ----QEKIERYQADLEELEE----RLEEQNEVVE---EADEQQ----- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 gelqalraraEEAEAQKRQAQEEAERLRRQVQD-----ESQRKR----QAEVELASRVKA-------EAEAAREKQRALQ 1536
Cdd:PRK04863 379 ----------EENEARAEAAEEEVDELKSQLADyqqalDVQQTRaiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1537 A-LEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAeAELQSKRASfaEKTAQLERSLQEEHVAVAQLreeaerraq 1615
Cdd:PRK04863 449 AkEQEATEELLSLEQKLSVAQ-AAHSQFEQAYQLVRKIA-GEVSRSEAW--DVARELLRRLREQRHLAEQL--------- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1616 qqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELE 1695
Cdd:PRK04863 516 ------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1696 KQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQREAAAATQKRQELEAELAKvraemevlLASKA 1772
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LLERE 640
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 41322919 1773 RAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1811
Cdd:PRK04863 641 RELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1529-1881 |
1.25e-10 |
|
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: 67.84 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1529 REKQRALQALEELRLQaEEAERRLRqaEVERARQvqvaLETAQRSAEAELQSKRASFAEKtaqlERSLQEEHvavaqlre 1608
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1609 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1688
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1689 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQREAAAATQKRQ-------ELEAELAKV 1760
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1837
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 41322919 1838 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1881
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1325-1542 |
1.49e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.82 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1325 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAEREA 1390
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1391 KELQQRMQEEVVRRE-EAAVDAQQQKRsiQEELQQlrqssEAEIQAKARQAEAAERSRLRIEEEirvvrlqLEATERQRg 1469
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANA--EREVQR-----QLEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1470 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1542
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1681-1918 |
1.51e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAaatqkrqELEAELAKV 1760
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELA-------RLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1836
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREierlERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1837 EKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKAsdseLERQKGLVEDT 1916
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDA----LAEALGLDEAE 459
|
..
gi 41322919 1917 LR 1918
Cdd:COG4913 460 LP 461
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1678-2055 |
1.52e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE--QQRQLLEEELARLQREAAAATQKRQELEA 1755
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1756 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRA 1829
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1830 EAERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRR 1879
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1880 LEEQAAQHKADIEERLAQLRKASDSELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDT 1958
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1959 LRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQL 2036
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAEL 474
|
410
....*....|....*....
gi 41322919 2037 QLAQEAAQKRLQAEEKAHA 2055
Cdd:COG4717 475 LQELEELKAELRELAEEWA 493
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1516-2051 |
1.53e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 67.96 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1516 ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSAEAELQSKRAS---------- 1584
Cdd:COG3899 713 RRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppasa 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1585 FAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1664
Cdd:COG3899 793 RAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLA 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1665 QKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1744
Cdd:COG3899 873 LAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAA 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1745 AATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1824
Cdd:COG3899 950 AAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALA 1016
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1825 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1904
Cdd:COG3899 1017 AALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAA 1096
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1905 ELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRR 1984
Cdd:COG3899 1097 LAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALA 1176
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1985 EAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2051
Cdd:COG3899 1177 ALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1877-2614 |
1.81e-10 |
|
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: 67.69 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1877 RRRLEEQAA--QHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1954
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1955 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2034
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2035 QLQLAQE---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeaeaarraaeeaeearvQAEREAAQSRRQV 2111
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK------------------LQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2112 EEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2191
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2192 RLQLEEtdhqKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAE 2271
Cdd:pfam02463 457 ELKLLK----DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2272 KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDKE 2351
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQL 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2352 QMAQQLAEETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLV 2431
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2432 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDSLLQRERFIEQ 2511
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2512 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGvrrkqEELQQLEQQRRQQEELLAEEN 2591
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEEL 838
|
730 740
....*....|....*....|...
gi 41322919 2592 qRLREQLQLLEEQHRAALAHSEE 2614
Cdd:pfam02463 839 -ALELKEEQKLEKLAEEELERLE 860
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1101-1602 |
2.41e-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: 67.28 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAVPATL-PELEATKASLKKLRAQAEAqqptfdalrdeLRGAQEVGERLQQRHGERDVEVERWRE 1179
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPA-----------WLAAQDALERLREQSGEALADSQEVTA 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1180 RVAQLLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----RRRQEQIQ 1234
Cdd:COG3096 631 AMQQLLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPARH 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1235 AMPLADSQAVREQLRQEQALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKPKV 1305
Cdd:COG3096 711 AIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLEEL 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1306 QSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQ 1385
Cdd:COG3096 791 RAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLD 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1386 AEREAKELQQRMQEEVV---------RREEAAVD---AQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERSRLRIE 1451
Cdd:COG3096 868 QLKEQLQLLNKLLPQANlladetladRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1452 EEIRVVRLQLEATE--RQR------GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1523
Cdd:COG3096 948 EQQRRLKQQIFALSevVQRrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSS 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1524 EAEAAREKQRALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KRASFAEKTAQLER 1594
Cdd:COG3096 1028 RDAKQQTLQELEQELEELGVQAdAEAEERARirrdelHEELSQNRSRRSQLEKQLTRCEAEMDSlqKRLRKAERDYKQER 1107
|
....*...
gi 41322919 1595 SLQEEHVA 1602
Cdd:COG3096 1108 EQVVQAKA 1115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4387-4425 |
3.16e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.16e-10
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 4387 FLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTAQKL 4425
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1738-2475 |
3.43e-10 |
|
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: 66.92 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1738 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKA-------RAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAL- 1809
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIyrvhrtlRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1810 -------AEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR 1879
Cdd:TIGR00618 133 hdllkldYKTFTRVVLLPQGEFAQflkAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1880 LEEQAAQHKADIEERLAQLRKASDSELERQKGLVE--DTLRQRRQVEEEILALKASFEKAAAGKAELEL---ELGRIRSN 1954
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQkrEAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeRINRARKA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1955 AEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2034
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAQRIHTELQSKMRSRA-----KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2035 QLQLAQeaaqkrlQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA 2114
Cdd:TIGR00618 368 REISCQ-------QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2115 ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ------------------ 2176
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcplcgscihpnparqdi 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2177 -----TLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEA-------ARQRSQVEEELFSVRVQMEEL---- 2240
Cdd:TIGR00618 521 dnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqqsfsilTQCDNRSKEDIPNLQNITVRLqdlt 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2241 ---SKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQE---------AARLRQLAEEDLAQQRA 2306
Cdd:TIGR00618 601 eklSEAEDMLACEQHALLrkLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehALSIRVLPKELLASRQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2307 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEdkeqmaQQLAEETQGFQRTLEAERQRQLEMSAEAER-- 2384
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE------IENASSSLGSDLAAREDALNQSLKELMHQArt 754
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2385 -LKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAtQEKVTLVQTLEIQRQQ-----------SDHDAERLREAI 2452
Cdd:TIGR00618 755 vLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEIGQeipsdedilnlQCETLVQEEEQF 833
|
810 820
....*....|....*....|...
gi 41322919 2453 AELEREKEKLQQEAKLLQLKSEE 2475
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEE 856
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
45-141 |
3.73e-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: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 45 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 110
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 41322919 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
920-1540 |
3.82e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 920 EEQRQALHSLELHYQAFLRDSQDAggfgpeDRLMAEREYgscsHHYQQLLQSLEQGAQEESRCQRcisELKDIRLQLEAC 999
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERL------AELEYLRAA----LRLWFAQRRLELLEAELEELRA---ELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1000 ETRtvhrlrlpldkeparecaQRIAEQQKAQAEVEGLGKGVARLSAeaekvlalpepspaaptLRSELELTLGKLEQVRS 1079
Cdd:COG4913 315 EAR------------------LDALREELDELEAQIRGNGGDRLEQ-----------------LEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1080 LSAIYLEKLKTISLVIRGTqgaeevlrahEEQLKEAQA-VPATLPELEATKASLKKLRAQAEAQqptFDALRDELRGAQE 1158
Cdd:COG4913 360 RRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELRELEA 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1159 VGERLQQRHGERDVEVERWRERVAQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----RYYRE 1214
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppEHYAA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1215 SAdplgAWLQDARRRQE-QIQAMPLADSQAVREQLrQEQALLEEIERhgeKVEECQRFAKQYINAIKDYELqlvtykaql 1293
Cdd:COG4913 501 AL----RWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLDF---KPHPFRAWLEAELGRRFDYVC--------- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1294 epVASPAkkpkvqsgsesviqeyvDLRTHYSELTT--LTSQyikfiSETLRRMEEEERL---------AEQQRAEERERL 1362
Cdd:COG4913 564 --VDSPE-----------------ELRRHPRAITRagQVKG-----NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAEL 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1363 AEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmqEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEA 1442
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1443 AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE--AERLRRQVQDESQRKRQAEVElASR 1520
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAVERELRENLE-ERI 775
|
650 660
....*....|....*....|
gi 41322919 1521 VKAEAEAAREKQRALQALEE 1540
Cdd:COG4913 776 DALRARLNRAEEELERAMRA 795
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
35-144 |
4.31e-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: 60.29 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 35 DEQDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYL 110
Cdd:cd21222 8 DEAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 41322919 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21222 88 EDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
522-711 |
4.96e-10 |
|
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: 62.46 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 522 LRYLQDLLAWVEENQHRVDGAEWGVDLPSVEAQLGSHRGLHQSIEEFRAKIERARSDEGQLSPATRGAY---RDCLGRLD 598
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 599 LQYAKLLNSSKARLRSLE---SLHSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKEL 675
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 41322919 676 QNAGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 711
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1102-1292 |
6.71e-10 |
|
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: 62.08 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1102 EEVLRAHEEQLKEAQaVPATLPELEATKASLKKLRAQAEAQQPTFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1181
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1182 AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLGAWLQDArrrQEQIQAMPLADS-QAVREQLRQEQALLEEIER 1260
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEK---EAALASEDLGKDlESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|..
gi 41322919 1261 HGEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1292
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1351-1549 |
6.88e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEE-RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREeaavdAQQQKrsiQEELQQLRQSS 1429
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1430 EAEIQAKARQAEAAERSRlRIEEEIRvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDESQR 1509
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322919 1510 KRQAEV-ELASRVKAEAEAAREKQRALQALEELRLQAEEAE 1549
Cdd:PRK09510 218 KAAAEAkAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1697-1911 |
9.29e-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: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1697 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEE 1776
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1777 ESRSTSEKSKQRLEA--EAGRFRELA--------EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1846
Cdd:COG4942 98 ELEAQKEELAELLRAlyRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1847 RLKTEAEIALKE----KEAENERLRRLAEDEAFQRRRLEEQAAQhKADIEERLAQLRKASDSELERQKG 1911
Cdd:COG4942 178 ALLAELEEERAAlealKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAERTPA 245
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1103-1880 |
1.30e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1103 EVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEvGERLQQRHGERDVEVERWRERva 1182
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLEELEER-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1183 qlLERWQAVLAQTDVRQRELEqlgRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLRQEQALLE----EI 1258
Cdd:PRK04863 364 --LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLCGlpdlTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1259 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRTHYSELTT 1328
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1329 LTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AEVEAALEKQRQLAEAHAQAKAQA-------EREAKELQ 1394
Cdd:PRK04863 518 LRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1395 QRMQEEVVRREE--AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATErQRGGAE 1472
Cdd:PRK04863 593 ARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS-QPGGSE 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 GE-LQALRARA--------------EEA-------------------EAQKRQAQE-----------------------E 1495
Cdd:PRK04863 672 DPrLNALAERFggvllseiyddvslEDApyfsalygparhaivvpdlSDAAEQLAGledcpedlyliegdpdsfddsvfS 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1496 AERLRRQV-QDESQRK----RQAEVELASRvkaeaeAAREKQralqaLEELRLQAEEAERRLRQAEVERaRQVQVALETA 1570
Cdd:PRK04863 752 VEELEKAVvVKIADRQwrysRFPEVPLFGR------AAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQAF 819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1571 QR------------SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlKA 1638
Cdd:PRK04863 820 SRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----DR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--------------LAEGT 1704
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafaltevvqrrahFSYED 975
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1705 AQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQREAAAATQKRQELEAELAK--VRAEMEVL 1767
Cdd:PRK04863 976 AAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPADSGAE 1055
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1768 LASKARAEE---------ESRSTSEKSKQRLEAE----AGRFRELAEEAARLRALAEEAKRQRQLAeEDAARQRAEAERV 1834
Cdd:PRK04863 1056 ERARARRDElharlsanrSRRNQLEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRL 1134
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1835 LAEKLAAiGEATRLKTEAEI---ALKEKEAENERLR---RLAEDEAFQRRRL 1880
Cdd:PRK04863 1135 HRRELAY-LSADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRPERKV 1185
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2268-2709 |
1.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2268 EEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLK-AEAELLQQQKELAQ--EQAR 2344
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARkaEEAR 1170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2345 RLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlRVAEMSRAQ--ARAEE--DAQRFRKQAEEIGEKLHRT 2420
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEdaKKAEAvkKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2421 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKllqlKSEEMQTVQQEQLLQETQalQQSFLSEKD 2500
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK----KAEEKKKADEAKKKAEEA--KKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2501 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvaSMEEARRRQHEAEEGVRRKQEELQQLEQqr 2580
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK--KKEEAKKKADAAKKKAEEKKKADEAKKK-- 1399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2581 rqqeellAEENQRLREQLQLLEEQHRAA---LAHSEEVTASQVAATKtlpngrdaldgpaaeAEPEHSFDGLRRKVSAQR 2657
Cdd:PTZ00121 1400 -------AEEDKKKADELKKAAAAKKKAdeaKKKAEEKKKADEAKKK---------------AEEAKKADEAKKKAEEAK 1457
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2658 LQEAGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLLLKATNEK 2709
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1367-1591 |
1.65e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1367 AALEKQRQLAEAHAQAKAQAEREAKELQQrmQEEVvrREEAAVDAQQQKRSIQEELQ---QLRQSSEAEIQAKARQAEAA 1443
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEEL--QQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1444 ERsrlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEVELASRVK 1522
Cdd:PRK09510 136 EA--------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1523 AEAEAAREKQRALQAleelrlqAEEAErrlRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1591
Cdd:PRK09510 197 AEAKKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1341-1561 |
1.80e-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: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1341 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQE 1420
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1421 ---ELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1497
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1498 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1561
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1102-1761 |
2.05e-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: 64.43 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1102 EEVLRAHEEQLKE-----AQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVER 1176
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1177 WRERV-------AQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVReQLR 1249
Cdd:pfam01576 417 LQARLseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLR-QLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1250 QEQALLEEieRHGEKVEECQRFAKQyinaIKDYELQLVTYKAQLEPVASPAK-----KPKVQSGSESVIQEY-------- 1316
Cdd:pfam01576 496 DERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaayd 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1317 -----------------VDLRTHYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEAH 1379
Cdd:pfam01576 570 klektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLAR 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1380 A-----QAKAQAEREAKELQQRMQEEVVRR----------EEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR-----Q 1439
Cdd:pfam01576 644 AleealEAKEELERTNKQLRAEMEDLVSSKddvgknvhelERSKRALEQQVEEMKTQLEELEDELQATEDAKLRlevnmQ 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1440 A-------------EAAERSRLRIEEEIRVVRLQLEATERQRGGA-------EGELQALRARAEEAEAQKRQAQEEAERL 1499
Cdd:pfam01576 724 AlkaqferdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKL 803
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1500 RRQVQDesqrkRQAEVELASRVKAEAEA-AREKQRALQALEELRLQAEE----AERRLRQAEVERAR-QVQVALETAQRS 1573
Cdd:pfam01576 804 QAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGASGKS 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1574 AeaeLQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALRLRLQ 1647
Cdd:pfam01576 879 A---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELKAKLQ 955
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1648 AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQA-----VRQRELAEQEL----EKQRQLAEGTAQQRLAAEQELIRL 1718
Cdd:pfam01576 956 EMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQL 1035
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 41322919 1719 RAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1761
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
34-143 |
2.26e-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: 57.90 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 34 QDEQDERdrvqkkTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALD 108
Cdd:cd21299 1 ETSREER------CFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVK 72
|
90 100 110
....*....|....*....|....*....|....*
gi 41322919 109 YLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 143
Cdd:cd21299 73 IGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1492-2027 |
3.10e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1492 AQEEAERLRRQVQDESQRKR---QAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRqAEVERARQVQVALE 1568
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE-KEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1569 TAQRSAEAELQSKRAsFAEKTAQLERSLQEEHVAVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQA 1648
Cdd:PRK03918 242 ELEKELESLEGSKRK-LEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1649 EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLRA 1720
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1721 ETEQGEQQRQLLEEELAR--LQREAAAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR-----------S 1780
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytaelK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1781 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLAEKLAAIGEAT 1846
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1847 RLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SDSELERQKGLVE 1914
Cdd:PRK03918 543 SLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELK 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1915 DTLRQRRQVEEEILALKASFEKAaagKAELElELGRIRSnaEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1994
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590
....*....|....*....|....*....|...
gi 41322919 1995 AAEEEAARQRKAALEEVERLKAKVEEARRLRER 2027
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
159-261 |
3.18e-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: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 159 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 237
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 41322919 238 PEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1434-1655 |
3.25e-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: 62.47 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1434 QAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1513
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1514 EVELASRVKAEAEAAREKQR-ALQALEELRLQAEEAERRLRQAE-VERARQVQVALETAQRSAEAELQSKRASFAEKTAQ 1591
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1592 LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1655
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1689-1920 |
3.40e-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: 62.17 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1689 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1768
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1769 AsKARAEEESRSTSEKSKQRLEAEAGRFRelAEEAARLRAlAEEAKRQRQLAE---EDAARQRAEAER-VLAEKLAAIGE 1844
Cdd:TIGR02794 124 A-KAKQAAEAKAKAEAEAERKAKEEAAKQ--AEEEAKAKA-AAEAKKKAEEAKkkaEAEAKAKAEAEAkAKAEEAKAKAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1845 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1920
Cdd:TIGR02794 200 AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1347-1598 |
3.67e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.04 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1347 EERLAEQQRaEERERLAEVEAALEKQR---QLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQ 1423
Cdd:PRK05035 456 EARQARLER-EKAAREARHKKAAEARAakdKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1424 QLRQSSEAEIQAKARQAEAAERSRLRIEEeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1503
Cdd:PRK05035 535 AEKQAAAAADPKKAAVAAAIARAKAKKAA-------QQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQV 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1504 QDESQRKrqaevelasrVKAEAEAAREKQRALQALEELRLQAEEAERRLR-QAEVERARQVQVALETAQRSAEAELQSKR 1582
Cdd:PRK05035 608 AEVDPKK----------AAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQANAEPEEAEDPKK 677
|
250
....*....|....*.
gi 41322919 1583 ASFAEKTAQLERSLQE 1598
Cdd:PRK05035 678 AAVAAAIARAKAKKAA 693
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1017-1602 |
4.00e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1017 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKLEQVRSlsaiyleklktiSLVI 1095
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLSESVS------------EARE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1096 RGTQgaeevLRAHEEQLK-EAQAVPATLPELEATKASLKKLRAQAEAQQPTFDAL-----------------RDELRGAQ 1157
Cdd:PRK04863 580 RRMA-----LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVteymqqllerereltveRDELAARK 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1158 EV----GERLQQRHGERDveverwrERVAQLLERWQAVLAQTDVRQRELEQLGrqlrYYResadplgAWLQDARrrqeqi 1233
Cdd:PRK04863 655 QAldeeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YFS-------ALYGPAR------ 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1234 QAMPLADSQAVREQLRQEQALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK-- 1304
Cdd:PRK04863 711 HAIVVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKri 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1305 --VQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRM-----EEEERLAEQQRAEERERLAEVEAALEKQRQLAE 1377
Cdd:PRK04863 789 eqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLE 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1378 AHAQAKAQAEREAKE--------LQQRM---QEEVVRREEAAVDAQQQKRSI-------------QEELQQLRQSSEaei 1433
Cdd:PRK04863 869 QAKEGLSALNRLLPRlnlladetLADRVeeiREQLDEAEEAKRFVQQHGNALaqlepivsvlqsdPEQFEQLKQDYQ--- 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1434 QAKARQAEAaeRSRLRIEEEIRVVRLQLEATERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKR 1511
Cdd:PRK04863 946 QAQQTQRDA--KQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYN 1019
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1512 QAEVELASRVKAEAEAAREkqrALQALEELRLQA-EEAERRLR------QAEVERARQVQVALETAQRSAEAELQS--KR 1582
Cdd:PRK04863 1020 QVLASLKSSYDAKRQMLQE---LKQELQDLGVPAdSGAEERARarrdelHARLSANRSRRNQLEKQLTFCEAEMDNltKK 1096
|
650 660
....*....|....*....|
gi 41322919 1583 ASFAEKTAQLERSLQEEHVA 1602
Cdd:PRK04863 1097 LRKLERDYHEMREQVVNAKA 1116
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1412-1956 |
4.44e-09 |
|
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: 62.74 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEeirvVRLQLE--ATERQRGGAEGELQALRARaeeaEAQK 1489
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1490 RQAQEEAERLRRQVQDESQRKRQAEVELASrVKAE--------AEAAREKQRALQALEELRLQAEEAERRLRQAEVERAr 1561
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1562 QVQVALETAQRS-AEAELQSKRASFA--EKTAQLERSLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLKA 1638
Cdd:pfam05701 191 ATKESLESAHAAhLEAEEHRIGAALAreQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 NEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQEL 1715
Cdd:pfam05701 255 ASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1716 IRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeagr 1795
Cdd:pfam05701 319 LRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA---- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1796 frelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAEDE 1873
Cdd:pfam05701 390 ----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1874 AFQR-------------RRLEEQAAQHKADIEERLAQLRKASDSELERQKGLvEDTLRQRRQVEEEILALKASFEKAAAG 1940
Cdd:pfam05701 466 DSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKEG 544
|
570
....*....|....*.
gi 41322919 1941 KAELELELGRIRSNAE 1956
Cdd:pfam05701 545 KLAAEQELRKWRAEHE 560
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4309-4346 |
5.22e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.41 E-value: 5.22e-09
10 20 30
....*....|....*....|....*....|....*...
gi 41322919 4309 QRLLEAQACTGGIIDPSTGERFPVTDAVNKGLVDKIMV 4346
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1335-1583 |
5.62e-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: 61.47 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1335 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQ 1414
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQ-AEWKELEKEEEREEDERILEYLKEKAE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1415 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQ 1493
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAeKKARQRQELQQAREEQIE 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1494 EEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1573
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
250
....*....|
gi 41322919 1574 AEAELQSKRA 1583
Cdd:pfam13868 327 RRERIEEERQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1223-1606 |
6.13e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1223 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK 1302
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1303 PKVQSGSESVIQEYVDLRTHYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AEVEAALEKQRQLAEAHAQ 1381
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1382 AKAQAEREAKELQQRMQEevVRREEAAVDAQQQKRSIQEELQQLRQSSEAE----------------------------- 1432
Cdd:COG4717 207 RLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1433 -------IQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQ 1504
Cdd:COG4717 285 llallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1505 DESQRKRQAEVELASRVKAEaEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1584
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|..
gi 41322919 1585 FAEKTAQLERSLQEEHVAVAQL 1606
Cdd:COG4717 444 LEEELEELREELAELEAELEQL 465
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
154-256 |
6.68e-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: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 154 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 41322919 233 TRLLDPEDVDVPQPDEKSIITYVS 256
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1737-1898 |
6.86e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.81 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1737 ARLQREAAAAtQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRalAEEAKRQ 1816
Cdd:COG2268 206 AEAERETEIA-IAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIA--EANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1817 RQLAEEDAARQR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD 1890
Cdd:COG2268 279 VQRQLEIAEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAI 358
|
....*...
gi 41322919 1891 IEERLAQL 1898
Cdd:COG2268 359 LLMLIEKL 366
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1716-2021 |
7.83e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.89 E-value: 7.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1716 IRLRA-ETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1788
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1789 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1868
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1869 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASdselerQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELEL 1948
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAA------QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1949 grIRSNAEDTLRSKEQAELEAARQRQLAAeeerrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2021
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1161-1468 |
1.02e-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: 61.68 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1161 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdvRQRELEqlgRQLRYYRESAdplgawlQDARRRQEQIQAMPLAD 1240
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1241 SQAVREQLRQEQALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1313
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1314 QEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKEL 1393
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1394 QQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAeAAERSRLRIEEEIRVVRLQLEATERQR 1468
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1422-1975 |
1.20e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 61.80 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1422 LQQLRQSSEAEIQAKARQAEAAERSRlrieeeiRVVRLQLEATER--QRGGAEGELQALRaRAEEAEAQKRQAQEEAERL 1499
Cdd:COG3899 677 EARGPEPLEERLFELAHHLNRAGERD-------RAARLLLRAARRalARGAYAEALRYLE-RALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1500 RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV-QVALETAQRSAEAEL 1578
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFgELALALAERLGDRRL 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1579 QSK-RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1657
Cdd:COG3899 829 EARaLFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1658 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1737
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1738 RLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR 1817
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1818 QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1897
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1898 LRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1975
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLL 1226
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1352-1585 |
1.28e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1352 EQQRAEERERLAEVEAALEKQrqLAEAHAQAkAQAEREAKELQQrmQEEVVRREEAAVDAQQQKRSIQEELQQLrQSSEA 1431
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ--LPELRKEL-EEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA-RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1432 EIQAKARQAEAAERSRLRIEEEIRVVRlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkr 1511
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSP-VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR-- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1512 qaeveLASRVKAEAEAAREKQRALQALEE------LRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASF 1585
Cdd:COG3206 314 -----ILASLEAELEALQAREASLQAQLAqlearlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1653-1848 |
1.29e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1653 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1732
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1733 EEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1812
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 41322919 1813 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1848
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1193-1959 |
1.42e-08 |
|
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: 61.67 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1193 AQTDVRQRE---LEQLGRQLR---YYRESADPLGA-WLQDARRRQEQIQAMPLAdSQAVREQLRQeqALLEEIERHGEKV 1265
Cdd:pfam15921 128 AMADIRRREsqsQEDLRNQLQntvHELEAAKCLKEdMLEDSNTQIEQLRKMMLS-HEGVLQEIRS--ILVDFEEASGKKI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1266 EECQRFAKQYINA--------IKDYELQLVTYKAQLEPVAS--PAKKPKVQSGSESVIQEYVD-----LRTHYSELTTLT 1330
Cdd:pfam15921 205 YEHDSMSTMHFRSlgsaiskiLRELDTEISYLKGRIFPVEDqlEALKSESQNKIELLLQQHQDrieqlISEHEVEITGLT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1331 SQ-------------YIKFISET--------LRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHAQ-AKAQAE 1387
Cdd:pfam15921 285 EKassarsqansiqsQLEIIQEQarnqnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEElEKQLVLANSElTEARTE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1388 REA---------KELQQRMQEEVVRREEAAVDAQQQKR--------SIQ---------------EELQQLRQSSEAEIQA 1435
Cdd:pfam15921 365 RDQfsqesgnldDQLQKLLADLHKREKELSLEKEQNKRlwdrdtgnSITidhlrrelddrnmevQRLEALLKAMKSECQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1436 KARQAEAAERSRLRIEEEIRVVRLQLEATErqrggaegelQALRARAEEAEAqKRQAQEEAERLRRQVQDESQRKRQAeV 1515
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTK----------EMLRKVVEELTA-KKMTLESSERTVSDLTASLQEKERA-I 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1516 ELASrvkaeAEAAREKQRALQALEELR-LQAEEAERRLRQAEVErARQVQVA-----LETAQRSAEAELQ-------SKR 1582
Cdd:pfam15921 513 EATN-----AEITKLRSRVDLKLQELQhLKNEGDHLRNVQTECE-ALKLQMAekdkvIEILRQQIENMTQlvgqhgrTAG 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1583 ASFAEKtAQLERSLQEEHVAVAQLreEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlQAEEVAQQ-------- 1654
Cdd:pfam15921 587 AMQVEK-AQLEKEINDRRLELQEF--KILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR-AVKDIKQErdqllnev 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1655 KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL------AEQELEKQRQL------AEGTAQQ-RLAAEQELIRLRAE 1721
Cdd:pfam15921 663 KTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmqlksAQSELEQTRNTlksmegSDGHAMKvAMGMQKQITAKRGQ 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1722 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVraemevllaskarAEEESRSTSEkskqrLEAEAGRFRELAE 1801
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV-------------ATEKNKMAGE-----LEVLRSQERRLKE 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1802 EAARLRALAEEAkrQRQLAEEDAARQRAEAERVlaeklaaigeatRLKTEAEIALKEKEA----ENERLR-RLAEDEAFQ 1876
Cdd:pfam15921 805 KVANMEVALDKA--SLQFAECQDIIQRQEQESV------------RLKLQHTLDVKELQGpgytSNSSMKpRLLQPASFT 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1877 RRRLEEQAAQHKADIEERLAQlrkasdseleRQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAE---LELELGRIRS 1953
Cdd:pfam15921 871 RTHSNVPSSQSTASFLSHHSR----------KTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEdkgRAPSLGALDD 940
|
....*.
gi 41322919 1954 NAEDTL 1959
Cdd:pfam15921 941 RVRDCI 946
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
154-261 |
1.69e-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: 55.48 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 154 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 41322919 233 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1066-1520 |
1.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1066 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLK-------KLRAQ 1138
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelperleELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1139 AEAQQPTFDALRDELRGAQEVGERLQQrhgERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADP 1218
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEE---LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1219 LGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEecqrfakqyinAIKDYELQLVTYKAQLEPVAS 1298
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL-----------FLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1299 PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEA 1378
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1379 HAQAKAQAEREAKELQQRmQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS-EAEIQAKARQAEAAERSRLRIEEEIRVV 1457
Cdd:COG4717 380 GVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1458 RLQLEATERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAEV-ELASR 1520
Cdd:COG4717 459 EAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVlERASE 523
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1519-2116 |
1.85e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1519 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1599 EHVAVAQLreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgK 1678
Cdd:COG4913 318 LDALREEL---------------------------------DELEAQIRGNGGDRLEQLE-------------------R 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1679 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1758
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1759 KVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGrfrelaEEAARLRALAEEAkrqrQLAEEDAARQRAeAERVL--- 1835
Cdd:COG4913 423 ELEAEIASLERRKSNIPARL----LALRDALAEALG------LDEAELPFVGELI----EVRPEEERWRGA-IERVLggf 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1836 ----------AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED-------------EAFQRRRLEEQAAQHKADIE 1892
Cdd:COG4913 488 altllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfRAWLEAELGRRFDYVCVDSP 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1893 ERLAQLRKA-------SDSELERQKG----------LVEDTLRQRRQVEEEILALKASFEKAAAGKAELelelgrirsna 1955
Cdd:COG4913 568 EELRRHPRAitragqvKGNGTRHEKDdrrrirsryvLGFDNRAKLAALEAELAELEEELAEAEERLEAL----------- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1956 edtlrskeQAELEAARQRQLAAEEERRRREAEERVQkslAAEEEAARQRkaalEEVERLKAKVEEARRLRERAE--QESA 2033
Cdd:COG4913 637 --------EAELDALQERREALQRLAEYSWDEIDVA---SAEREIAELE----AELERLDASSDDLAALEEQLEelEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2034 RQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEE 2113
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERFAAALGDAVERELRENLEERIDALR 779
|
...
gi 41322919 2114 AER 2116
Cdd:COG4913 780 ARL 782
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1690-1877 |
1.96e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1690 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEmevllA 1769
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1770 SKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1849
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180
....*....|....*....|....*...
gi 41322919 1850 TEAEIALKEKEAENERLRRLAEDEAFQR 1877
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1851-2300 |
2.18e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1851 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASDselerqkglVEDTLRQRRQVEEEILAL 1930
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1931 KASFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAARQRQLaaeeerrrrEAEERVQKSLAAEEEAARQRKAALEE 2010
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSL---------ATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2011 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2090
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2091 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2170
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2171 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KNLLDEELQRLKAEATEAARQR-SQVEEELFSVRVQMEELSK 2242
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2243 LKARIEAENRALILRDK-DNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEED 2300
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1342-1603 |
2.56e-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: 59.67 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1342 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaqakAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1421
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLL-------LQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1422 LQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaEGELQALRARAEEAEaQKRQAQEEAERLRR 1501
Cdd:pfam15558 94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAC-HKRQLKEREEQKKV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1502 QVQDESQR-KRQA-EVELASRVKAEAEAARE--KQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1577
Cdd:pfam15558 170 QENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEER 249
|
250 260
....*....|....*....|....*.
gi 41322919 1578 LQSKRASFAEKTAQLERSLQEEHVAV 1603
Cdd:pfam15558 250 QEHKEALAELADRKIQQARQVAHKTV 275
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
163-258 |
2.66e-08 |
|
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: 55.38 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 163 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL-----------------------EN 218
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 219 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 258
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2274-2477 |
2.76e-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: 59.39 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2274 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2349
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2350 KEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2429
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 41322919 2430 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2477
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1359-1828 |
2.76e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.42 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1359 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAqqqkrsiqeelqQLRQSSEAEIQAKAR 1438
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRA------------ALRWALAHGDAELAL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1439 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1518
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1519 SRvkAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1599 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1678
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1679 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1758
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1759 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1828
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1681-2103 |
2.79e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1758
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1759 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1823
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1824 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASD 1903
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1904 SELERQKGLVE-DTLRQRRQVEEEILALKASFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAARQRQLAAEEERR 1982
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1983 RREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQlQLAQEAAQKRLQAEEKAHAFAVQQK 2061
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRELAEEWAALKL 497
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 41322919 2062 EQElqqtlqqeqsVLDQLRGeaeaarraaeeaeearvQAERE 2103
Cdd:COG4717 498 ALE----------LLEEARE-----------------EYREE 512
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
46-140 |
2.81e-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: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 46 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 117
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 41322919 118 VNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1678-1885 |
2.81e-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: 59.39 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAel 1757
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1836
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 41322919 1837 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1885
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1339-1592 |
3.02e-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: 59.16 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1418
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1419 QEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1498
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1499 LRRQVQDESQRKRQAEVELASRVKaEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1578
Cdd:pfam13868 206 LRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR 284
|
250
....*....|....
gi 41322919 1579 QSKRASFAEKTAQL 1592
Cdd:pfam13868 285 RMKRLEHRRELEKQ 298
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1047-1542 |
3.06e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1047 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEaqaVPATLPELE 1126
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1127 ATKASLKKLRAQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLG 1206
Cdd:PRK03918 280 EKVKELKELKEKAEEYI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1207 RQLRYYRE------------------SADPLGAWLQDARRRQEQIQAmPLADSQAVREQLRQEQALL----EEIERHGEK 1264
Cdd:PRK03918 359 ERHELYEEakakkeelerlkkrltglTPEKLEKELEELEKAKEEIEE-EISKITARIGELKKEIKELkkaiEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1265 VEECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTHYSELTTLTSQYIK 1335
Cdd:PRK03918 438 CPVCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1336 FISETLRRMEEE-----ERLA-----------EQQRAEERE-RLAEVEAAL-EKQRQLAEAHAQAKAQAEREAKELQQRM 1397
Cdd:PRK03918 515 YNLEELEKKAEEyeklkEKLIklkgeikslkkELEKLEELKkKLAELEKKLdELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1398 Q--EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEE-EIRVVRLQLEATERQRGGAEGE 1474
Cdd:PRK03918 595 KelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1475 LQALRARAEEAEAQKRQAQEEAERLRRQVqdESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1542
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1412-1593 |
3.46e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRvvrlqleaterqrggaegelqalraraEEAEAQKRQ 1491
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1492 AQEEAER-LRRQVQDESQRKRQAEvelASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER---ARQVQVAL 1567
Cdd:PRK09510 120 AEEAAKQaALKQKQAEEAAAKAAA---AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAA 196
|
170 180
....*....|....*....|....*.
gi 41322919 1568 ETAQRSAEAELQSKRASFAEKTAQLE 1593
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1124-1882 |
3.74e-08 |
|
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: 60.24 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1124 ELEATKASLKKLRAQAEAQQPTFDALRDELRgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELE 1203
Cdd:pfam12128 259 RLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1204 Q-LGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEEcqRFAKQYINAikdy 1282
Cdd:pfam12128 333 AfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKIREAR---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1283 ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYvDLRTHYSELTTLTSQYIkFISETLRRMEEEERLAEQQRAEERERL 1362
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAAN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1363 AEVEAAlekQRQLAEAHAQAKAQAEReakelqqrmqeevVRREEAAVdaQQQKRSIQEELQQLRQSSEAEIQAKARQAEA 1442
Cdd:pfam12128 485 AEVERL---QSELRQARKRRDQASEA-------------LRQASRRL--EERQSALDELELQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1443 AERSRLRIEEEIRVVRLQL--EATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQV-----QDESQRKRQAEV 1515
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLdpEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEEELRERLDKaeealQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1516 ELASRVKAEAEAAREKQRALQALEelrlQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQskraSFAEKTAQLERS 1595
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKK 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1596 LQeehvavaqlreeaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQkslaqaeaekqKEEAEREARR 1675
Cdd:pfam12128 698 HQ-------------------------------AWLEEQKEQKREARTEKQAYWQVVEG-----------ALDAQLALLK 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1676 RGKAEEQAVRQRELAEQELEKQRQLAE-GTAQQRLAA-EQELIRLRAETEQGEQQRQLLeEELARLQREaaAATQKRQEL 1753
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASlGVDPDVIAKlKREIRTLERKIERIAVRRQEV-LRYFDWYQE--TWLQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1754 EAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlaeeakRQRQLAEEDAARQRAEAER 1833
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC------EMSKLATLKEDANSEQAQG 886
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1834 VLAEKLAAiGEATRLKTEAEIALKEKEAEN-----ERLRRLAEDEAFQRRRLEE 1882
Cdd:pfam12128 887 SIGERLAQ-LEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAETWESLREED 939
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1678-1833 |
4.19e-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: 58.70 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1757
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1758 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EAARLRALAEEAKRQRQLAeedAARQRAEAER 1833
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEAAKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1147-1579 |
4.73e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1147 DALRDELRGAQEVGERLQQRHGERDVEVERWRE-----------RVAQLLERWQAV---LAQTDVRQRELEQLGRQLRYY 1212
Cdd:PRK04863 743 DSFDDSVFSVEELEKAVVVKIADRQWRYSRFPEvplfgraarekRIEQLRAEREELaerYATLSFDVQKLQRLHQAFSRF 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1213 RES-------ADPLGAWLQDARRRQEQIQAMPLADSQAVR-----EQLRQEQALLEEI---------ERHGEKVEECQ-- 1269
Cdd:PRK04863 823 IGShlavafeADPEAELRQLNRRRVELERALADHESQEQQqrsqlEQAKEGLSALNRLlprlnlladETLADRVEEIReq 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1270 --------RFAKQYINAIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKF 1336
Cdd:PRK04863 903 ldeaeeakRFVQQHGNAL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHF 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 -ISETLRRMEEEERLAEQQRAeereRLAEVEAALEKQRqlaEAHAQAKAQAeREAKELQQRMQEEVVRreeaavdAQQQK 1415
Cdd:PRK04863 972 sYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERTRAR---EQLRQAQAQL-AQYNQVLASLKSSYDA-------KRQML 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1416 RSIQEELQQL--RQSSEAEIQAKARQAEaaersrlrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQ 1493
Cdd:PRK04863 1037 QELKQELQDLgvPADSGAEERARARRDE--------LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1494 EEAE-------RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKqrALQALeelrlqaeeaerRLRQAEVERARQVQVA 1566
Cdd:PRK04863 1109 EQVVnakagwcAVLRLVKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRL 1174
|
490
....*....|...
gi 41322919 1567 LETAQRsAEAELQ 1579
Cdd:PRK04863 1175 SEDPKR-PERKVQ 1186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1497-1973 |
6.81e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1497 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERArqvqvalETAQRSAEA 1576
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-------ELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1577 ELQSKRASFAEKTAQLERSLQEEHVAVAQLreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1656
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEEL--------------EERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1657 LAQAeaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEEL 1736
Cdd:COG4717 188 LATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1737 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ 1816
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1817 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEER 1894
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1895 LAQLRKASDSELERQKGLVEDTLRQR-RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR 1973
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1344-1597 |
7.33e-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: 58.01 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1344 MEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE-AKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1422
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVR-----------LQLEATERQRGGAEGELQALRARAEEAEAQKRQ 1491
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekeeereedERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1492 ---AQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALE 1568
Cdd:pfam13868 188 rlrAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
|
250 260
....*....|....*....|....*....
gi 41322919 1569 TAQRSAEAELQSKRASFAEKTAQLERSLQ 1597
Cdd:pfam13868 268 RKQAEDEEIEQEEAEKRRMKRLEHRRELE 296
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1678-2051 |
7.86e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1757
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1835
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1836 AEKLAAIGEatrlKTEAEIALKEKEAENERLRRLaedeafqrrrleeqaaQHKADIEERLAQLRKASDSELERQKGLVED 1915
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFL----------------DQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1916 TLRQRRQVEEEilalkasfekaAAGKAELELELGRIR-SNAEdtlrsKEQAELEAARQRQLAAEEERRRREAEERVQKSL 1994
Cdd:pfam02029 229 GLSQSQEREEE-----------AEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1995 AAEEEaaRQRKAalEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2051
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1423-1590 |
8.15e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSsEAEIQAKARQAEAAERSRLRIEEeiRVVRLQLEATERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1497
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1498 RLR-RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEA 1576
Cdd:PRK05035 494 RVKaKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170
....*....|....
gi 41322919 1577 ELQSKRASFAEKTA 1590
Cdd:PRK05035 574 EVDPKKAAVAAAIA 587
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4040-4076 |
9.10e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 9.10e-08
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 4040 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4076
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1352-2031 |
1.06e-07 |
|
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: 58.52 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1352 EQQRAEERERLAEVEAALEKQRQLAE---AHAQAKAQAEREAKELQQRMQE------------------EVVRREEAAVD 1410
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNeikALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyhnhqrTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1411 AQQQKRSIQEELQQLRQSS---EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRG----------------GA 1471
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpfserqiknfhtlvieRQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1472 EGELQALRARAEEAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRlq 1544
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRdekkglgRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR-- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1545 aeEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLER---------SLQEEHVAVAQLREEAERRAQ 1615
Cdd:TIGR00606 482 --KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttrtqmeMLTKDKMDKDEQIRKIKSRHS 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1616 QQAEAERAREEAERELERW-QLKANEALRLRLQAEEVaqQKSLAQAEAEKQKEEAerearrrgkaeeqavRQRELAEQEL 1694
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWlHSKSKEINQTRDRLAKL--NKELASLEQNKNHINN---------------ELESKEEQLS 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1695 EKQRQLAEGTAQQrlAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1764
Cdd:TIGR00606 623 SYEDKLFDVCGSQ--DEESDLERLKEEIEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1765 EVLLASKARAEEESRSTSEKSKQRLEAEAGRF-----------RELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAE 1832
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqsiidlkeKEIPELRNKLQKVNRDIQRLKNdIEEQETLLGTIMPE 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1833 RVLAEKLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR 1899
Cdd:TIGR00606 781 EESAKVCLTdVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQ 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1900 --KASDSELERQKGLVEDTLRQRRQVEE-------EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1970
Cdd:TIGR00606 861 hlKSKTNELKSEKLQIGTNLQRRQQFEEqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1971 RQRQLAAEEERRRREAEERVQKSLaaEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2031
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
32-146 |
1.44e-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: 53.47 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 32 WAQDEQDERdrvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQ 104
Cdd:cd21331 14 WTLLEGETR---EERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCN 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 41322919 105 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 146
Cdd:cd21331 89 YAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1776-2061 |
1.50e-07 |
|
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: 57.83 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1776 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlaeKLAAIGEATRLKTE 1851
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1852 AE-----IALKEKEAENERLRR--LAEDEAFQRR--RLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTL----- 1917
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQeeIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVemeqi 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1918 ---------RQRRQVEEEilaLKASFEKAAAGKAELELELGRIRSNAEDtlRSKEQAELEAARQRQLAAEEERRRREAEE 1988
Cdd:pfam17380 426 raeqeearqREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEE--RKRKKLELEKEKRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1989 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARrlRERAEQESARQLQLAQE---AAQKRLQAEEKAHAFAVQQK 2061
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERrriQEQMRKATEERSRLEAMERE 574
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1362-1774 |
1.57e-07 |
|
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: 58.33 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1362 LAEVEAALEKQRQLAEAHAQAkaqaeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE----------- 1430
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVA-----REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 --------AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1502
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1503 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1582
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1583 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1662
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1663 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQRE 1742
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 41322919 1743 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1774
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2248-2475 |
1.92e-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: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2248 EAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLS-----VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA 2322
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2323 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2401
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2402 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE-LEREKEKLQQEAKLLQLKSEE 2475
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1479-1599 |
1.94e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.19 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1479 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaevELASRVKAEAEAAREKQRAlqaleELRLQAE----EAERRLRQ 1554
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 41322919 1555 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEE 1599
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAE 315
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1339-1561 |
2.21e-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: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQkr 1416
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1417 siqeelqqlrqsseaeiQAKARQAEAAersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEE- 1495
Cdd:TIGR02794 146 -----------------EEAAKQAEEE--------------AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1496 ---AERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERAR 1561
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1431-1563 |
2.25e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 56.21 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 AEIQAKARQAEAAersrlrieeeIRVVRLQLEATERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLR---------R 1501
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQalykkgavsQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1502 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1563
Cdd:COG1566 148 QELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2167-2470 |
2.34e-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: 57.34 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2167 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKAR 2246
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2247 IEAENRAL------ILRDKDNTQRFLQEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2318
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2319 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLeaerqrqlemsaeaERLKLRVAEMSRAQAR 2398
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI--------------EELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2399 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2470
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1537-1975 |
2.34e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 57.33 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1537 ALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ---------LR 1607
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALrlaaalapfWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1608 EEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1687
Cdd:COG3903 557 LRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAA 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1688 ELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVL 1767
Cdd:COG3903 637 AAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAA 716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1768 LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATR 1847
Cdd:COG3903 717 AAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1848 LKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEI 1927
Cdd:COG3903 797 AAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAA 876
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 41322919 1928 LALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQL 1975
Cdd:COG3903 877 AAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1690-1905 |
2.45e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1690 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLA 1769
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1770 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1838
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1839 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSE 1905
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1365-1584 |
2.55e-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: 56.01 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1365 VEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAE 1444
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKL----EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1445 RSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAE 1524
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKA-KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1525 AEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRAS 1584
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1827-2217 |
2.78e-07 |
|
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: 57.06 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1827 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasDSEL 1906
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1907 ERQKglVEDTLRQRRQVEEEILALKASFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAARQRQLAaeeerrrre 1985
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1986 aeervqkslaaEEEAARQRKAALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHafavQQKEQE 2064
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLR----QQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2065 LQQTLQQEQSVLDQLRGEAEAARRAaeeaeearvqaEREAAQSRRQVEEAERlKQSAEEQAQARAQAQAAAEKLRKEAEQ 2144
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKIL-----------EKELEERKQAMIEEER-KRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2145 EaarraqaeqaalRQKQaadAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKNLLDEELQRLKAEAT 2217
Cdd:pfam17380 541 E------------RRKQ---QEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1346-1530 |
2.97e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1346 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAEREAKELQQRMqeevvrrEEAAVDAQQQKRSIQEELQQL 1425
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRA-------AAAAKKAAAEAKKKAEAEAAK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1426 RQSSEAEIQAKARQAEAAersrlrieeeirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqvqd 1505
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKA------------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA--------- 230
|
170 180
....*....|....*....|....*
gi 41322919 1506 ESQRKRQAEVELASRVKAEAEAARE 1530
Cdd:PRK09510 231 AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1788-1974 |
3.24e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1788 RLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1863
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1864 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAS 1933
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322919 1934 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1974
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1345-1510 |
3.50e-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: 55.62 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1345 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQ 1424
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1425 LRQSSEAEIQAKARQAEA-AERSRLRIEEEI----RVVRLQLEATERQRGGAEGELQALRARAEEAEAQK------RQAQ 1493
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 41322919 1494 EEAERLRRQVQDESQRK 1510
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2258-2607 |
3.55e-07 |
|
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: 56.67 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2258 DKDNTQRFLQEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEKmlkEKMQAVQEATRLKAEAELLQQQKE 2337
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDRQ---AAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2338 LAQEQARRLQEDKEQMAQQLAEETQGFQ--RTLEAERQRQlEMSAeAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2415
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQmeRQQKNERVRQ-ELEA-ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2416 -KLHRTELATQEKVTLVQTLEIQRQqsdHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqllqetqaLQQS 2494
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQ---QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI-----------LEKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2495 FLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAQQLREEQQRQqqqmeqerqrlvasmEEARRRQHEAEEGvRRKQEELQ 2574
Cdd:pfam17380 501 LEERKQAMIEEER-----KRKLLEKEMEERQKAIYEEERRREA---------------EEERRKQQEMEER-RRIQEQMR 559
|
330 340 350
....*....|....*....|....*....|...
gi 41322919 2575 QLEQQRRQQeellaEENQRLREQLQLLEEQHRA 2607
Cdd:pfam17380 560 KATEERSRL-----EAMEREREMMRQIVESEKA 587
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1677-1919 |
3.79e-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: 56.50 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqreaaaATQKRQEL 1753
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1754 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeagrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1833
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1834 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGL 1912
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 41322919 1913 VEDTLRQ 1919
Cdd:pfam15709 516 AQEQARQ 522
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1726-1901 |
4.36e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1726 EQQRQLLEEELAR-LQREAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGrfrelAEEAA 1804
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAK-----AAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1805 RLRALAEeakrqrQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1884
Cdd:PRK09510 146 KAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 41322919 1885 AQHKADIEERLAQLRKA 1901
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2303-2604 |
5.11e-07 |
|
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: 56.29 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2303 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQR-QLEMSA 2380
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2381 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLREaIAELEREK 2459
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2460 EKL---QQEAKLLQLK--SEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQ 2534
Cdd:pfam17380 423 EQIraeQEEARQREVRrlEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2535 QRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRrqqeellaEENQRLREQLQLLEEQ 2604
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2179-2475 |
5.46e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2179 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILR- 2257
Cdd:PRK02224 321 DRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERf 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2258 -----DKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAE-------------------------------EDL 2301
Cdd:PRK02224 401 gdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpvegsphvetieedrervEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2302 AQQRALAE---KMLKEKMQAVQEATRLKAEAELLQQQKELAQE---QARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2375
Cdd:PRK02224 481 EAELEDLEeevEEVEERLERAEDLVEAEDRIERLEERREDLEEliaERRETIEEKRERAEELRERAAELEAEAEEKREAA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2376 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK-------------QAEEIGEKL-HRTELATQEKVTLVQTLEIQRQ-Q 2440
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaaiadaedEIERLREKReALAELNDERRERLAEKRERKRElE 640
|
330 340 350
....*....|....*....|....*....|....*
gi 41322919 2441 SDHDAERLREAIAELEREKEKLQQEAKLLQLKSEE 2475
Cdd:PRK02224 641 AEFDEARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1920-2475 |
5.95e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1920 RRQVEEEILALKaSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEE 1999
Cdd:PRK03918 147 REKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2000 AARQRKaalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL 2079
Cdd:PRK03918 225 KLEKEV---KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2080 RGEAEAARRAAEEAEEARvqaEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQ 2159
Cdd:PRK03918 302 YEEYLDELREIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2160 KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE-----LFSVR 2234
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2235 VQMEELSKLKARIEAENRALiLRDKDNTQRFLQEEAE--KMKQVAEEAARLSvaaqeaARLRQLAEEDLAQQRALAEKML 2312
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKL-RKELRELEKVLKKESEliKLKELAEQLKELE------EKLKKYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2313 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2391
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKElEELGFESVEELEERLKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2392 msRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2471
Cdd:PRK03918 612 --KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEK 687
|
....
gi 41322919 2472 KSEE 2475
Cdd:PRK03918 688 RREE 691
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2163-2363 |
6.25e-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: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2163 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEE--- 2239
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2240 --------LSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM 2311
Cdd:COG3883 94 alyrsggsVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2312 LKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQG 2363
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1397-1565 |
6.31e-07 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 55.92 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1397 MQEEVVRREEAAVDAQQQkrsiqeELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQ 1476
Cdd:COG1193 497 LPEEIIERARELLGEESI------DVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK-------E 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1477 ALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaevelasrvKAEAEAAREKQRALQALEElRLQAEEAERRLRQA 1555
Cdd:COG1193 564 EILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKAK 627
|
170
....*....|
gi 41322919 1556 EVERARQVQV 1565
Cdd:COG1193 628 PAKPPEELKV 637
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1320-1453 |
6.33e-07 |
|
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: 54.22 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1320 RTHYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreakelQQ 1395
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE------LL 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1396 RMQEEVVRREEAAVDAQQQKRSIQEEL----QQLRQSSEAEIQAKARQAEAA-----ERSRLRIEEE 1453
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3721-3756 |
6.78e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 6.78e-07
10 20 30
....*....|....*....|....*....|....*.
gi 41322919 3721 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3756
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2316-2461 |
9.58e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.41 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2316 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLAEEtQGFQRTLEAERQRQLEMSAEAERLKL 2387
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2388 RVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2461
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4143-4171 |
1.02e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.71 E-value: 1.02e-06
10 20
....*....|....*....|....*....
gi 41322919 4143 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4171
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2274-2478 |
1.05e-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: 54.08 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2274 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2353
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2354 AQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2433
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41322919 2434 LEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQT 2478
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1334-1577 |
1.05e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1334 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQ 1413
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1414 QKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAE----EAEAQK 1489
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1490 RQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALET 1569
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*...
gi 41322919 1570 AQRSAEAE 1577
Cdd:COG3883 258 AAGSAGAA 265
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1737-2467 |
1.16e-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: 55.11 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1737 ARLQREAAAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1813
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1814 KRQRQLAEEDAAR---QRAEAERVLAEKLAAIGEATRLKTEAEIalkekEAENERLR---RLAEDEAfQRRRLEEQAAQH 1887
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRV-----QAENARLEmhfKLKEDHE-KIQHLEEEYKKE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1888 KADIEERLAQLRKASDSELERQKGL---VEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSkeq 1964
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST--- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1965 aeleaarQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKV---EEARRLRERAEQESARQLQLAQE 2041
Cdd:pfam05483 312 -------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2042 AAQKRLQAEEKAHAFAVQQKEQelqqtlqqeqsvLDQLRgeaeaarraaeeaeeaRVQAEREAA-QSRRQVEE-AERLKQ 2119
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVE------------LEELK----------------KILAEDEKLlDEKKQFEKiAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2120 SAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEE 2197
Cdd:pfam05483 437 KEQELIFLLQA---------------------------REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2198 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELskLKARIEAENRALILRDKDNTQR--FLQEEAE---K 2272
Cdd:pfam05483 490 LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2273 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQ 2352
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2353 MAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQ---------------ARAEEDAQRFRKQAEEIGEKL 2417
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSEL 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 41322919 2418 HRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAK 2467
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1347-1974 |
1.21e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1347 EERLAEQQRAeeRERLAEVEAALEK-QRQLA------------------EAHAQAKAQAEREAKELQQRMQEEVVRREEA 1407
Cdd:PRK10246 253 DELQQEASRR--QQALQQALAAEEKaQPQLAalslaqparqlrphweriQEQSAALAHTRQQIEEVNTRLQSTMALRARI 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1408 AVDAQQQKRSIQEELQQLRQ-SSEAEIQAKARQAEAAERSRL----RIEEEIRVVRLQLEATERQRGGAEGELQALRARa 1482
Cdd:PRK10246 331 RHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGWRAQFsqqtSDREQLRQWQQQLTHAEQKLNALPAITLTLTAD- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLR---RQVQDESQRKRQAEVElasrvKAEAEAAREKQRALQALEELRLQAEEaerrlRQAEVER 1559
Cdd:PRK10246 410 EVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQ-----VAIQNVTQEQTQRNAALNEMRQRYKE-----KTQQLAD 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1560 ARQVqvaleTAQRSAEAELQSKRASF-AEKTAQLERSlqEEHVAVAQLREEAERRAQQQAEAERAreeaerelERWQLKa 1638
Cdd:PRK10246 480 VKTI-----CEQEARIKDLEAQRAQLqAGQPCPLCGS--TSHPAVEAYQALEPGVNQSRLDALEK--------EVKKLG- 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1639 NEALRLRLQAEEVAQQKSlaqaeaekqkeeaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRL 1718
Cdd:PRK10246 544 EEGAALRGQLDALTKQLQ---------------------RDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPW 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1719 RAETEQGEQQRQLLEEELArLQREAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAE 1792
Cdd:PRK10246 602 LDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1793 AGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE- 1871
Cdd:PRK10246 681 QNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKa 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1872 ----DEAFQRRRLEEQAAQHKADIEE----RLAQLRKASDSELERQKGLVEdtlrQRRQVEEEILALKASFEKAAAGKAE 1943
Cdd:PRK10246 751 qaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQ 826
|
650 660 670
....*....|....*....|....*....|....*.
gi 41322919 1944 LELEL----GRIRSNAEDTLRSKEQAELEA-ARQRQ 1974
Cdd:PRK10246 827 IQQELaqlaQQLRENTTRQGEIRQQLKQDAdNRQQQ 862
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1590 |
1.30e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1376 AEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEI- 1454
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEAEIEERREELg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1455 -RVVRLQ------------------------LEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1509
Cdd:COG3883 90 eRARALYrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1510 KRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKT 1589
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
.
gi 41322919 1590 A 1590
Cdd:COG3883 250 G 250
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1034-1601 |
1.46e-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: 55.05 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1034 EGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLK 1113
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQE--QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1114 EAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERlqQRHGERDVEVERWRERVAQLLERWQavla 1193
Cdd:TIGR00606 482 KAER---ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQL--NHHTTTRTQMEMLTKDKMDKDEQIR---- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1194 qtDVRQRELEQLGRQLRYYRESADpLGAWLQDARRRQEQIQ------AMPLADSQAVREQLR-QEQALLEEIERHGEKVE 1266
Cdd:TIGR00606 553 --KIKSRHSDELTSLLGYFPNKKQ-LEDWLHSKSKEINQTRdrlaklNKELASLEQNKNHINnELESKEEQLSSYEDKLF 629
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1267 EcqrfakqyINAIKDYELQLVTYKAQLEpvaSPAKKPKVQSGSESVIQEYVDLRTHYSE----LTTLTSQYIKFISETLR 1342
Cdd:TIGR00606 630 D--------VCGSQDEESDLERLKEEIE---KSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1343 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEevvrreeAAVDAQQQKRSIQEEL 1422
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK-------VNRDIQRLKNDIEEQE 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1502
Cdd:TIGR00606 772 TLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1503 VQDESQRKRQAEV---ELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEvERARQVQVALETAQRSAEAELQ 1579
Cdd:TIGR00606 852 IQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAK-EQDSPLETFLEKDQQEKEELIS 930
|
570 580
....*....|....*....|..
gi 41322919 1580 SKRASfaEKTAQLERSLQEEHV 1601
Cdd:TIGR00606 931 SKETS--NKKAQDKVNDIKEKV 950
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2158-2614 |
1.48e-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: 54.97 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2158 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQ--LEETDHQKnllDEELQRLKAEATEAARQRSQVEEELFSVRV 2235
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQ---EIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2236 QMEELSKLKARIEAENRAL-ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2314
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELdILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2315 KMQAVQEATRLKAEAE-LLQQQKELAQEQARRLQEDKEQ------------MAQQLAEETQGFQRTLEAERQRQLEMSAE 2381
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEqIHLQETRKKAVVLARLLELQEEpcplcgscihpnPARQDIDNPGPLTRRMQRGEQTYAQLETS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2382 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelaTQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2461
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS---KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2462 LQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDsllqrerfiEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQM 2541
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER---------VREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2542 EQERQRLVASMEEARRRQHEAEEGVRRkqeELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE 2614
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDR---EFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2179-2464 |
1.61e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2179 RQKAQVEQELTTLRLQLeeTDHQknlldeelQRLKAEATEAArQRSQVEEELFSVRVQME----ELSKLKARIEAenraL 2254
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQ--------QALDVQQTRAI-QYQQAVQALERAKQLCGlpdlTADNAEDWLEE----F 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2255 ILRDKDNTQRFLQEE-----AEKMKQVAEEAARL------SVAAQEAARLRQLAEEDLAQQRALAEKM---------LKE 2314
Cdd:PRK04863 448 QAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQ 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2315 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MS 2393
Cdd:PRK04863 528 RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAA 600
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2394 RAQA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLQQ 2464
Cdd:PRK04863 601 RAPAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1310-1546 |
1.72e-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: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1310 ESVIQEYVDLRThySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ---RQLAEAHAQ-AKAQ 1385
Cdd:COG3206 155 NALAEAYLEQNL--ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQlAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1386 AEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEAtE 1465
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAEL-EAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-E 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1466 RQRGGAEGELQALRARAEEAEAQKRQAQeeaerLRRQVQDESQRkrqaEVELAsRVKAEAEAAREK-QRALQALEELRLQ 1544
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQ-----LEARLAELPEL----EAELR-RLEREVEVARELyESLLQRLEEARLA 380
|
..
gi 41322919 1545 AE 1546
Cdd:COG3206 381 EA 382
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1337-2244 |
1.88e-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: 54.67 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 ISETLRRMEEEERLaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEreAKELQQRMQEEVVRREEAAVDaqqqkr 1416
Cdd:TIGR00606 178 IFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESSREIVKSYENELD------ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1417 siqeelqqlrqsseaEIQAKARQAEAAERSRLRIEEEIRvvrlQLEATERQRGGAEGELQALraRAEEAEAQKRQAQEEA 1496
Cdd:TIGR00606 249 ---------------PLKNRLKEIEHNLSKIMKLDNEIK----ALKSRKKQMEKDNSELELK--MEKVFQGTDEQLNDLY 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1497 ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVER-ARQVQVALETAQRSAE 1575
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIqSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1576 AELQSKRASFAEKtaqleRSLQEEHVAVAQLREeaerraqqqaeaerareeaerelerwQLKANEALRLRlQAEEVAQQK 1655
Cdd:TIGR00606 388 SERQIKNFHTLVI-----ERQEDEAKTAAQLCA--------------------------DLQSKERLKQE-QADEIRDEK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1656 SLAQAEAEKqkeeaerearrrgKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAE---------TEQGE 1726
Cdd:TIGR00606 436 KGLGRTIEL-------------KKEILEKKQEEL--KFVIKELQQLEGSSDRILELDQELRKAERElskaeknslTETLK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1727 QQRQLLEEELARLQREAAAATQKRQELEAElAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL 1806
Cdd:TIGR00606 501 KEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1807 RALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEI----ALKEKEAENERLRRLAEDEAFQRRRLE 1881
Cdd:TIGR00606 580 HSKSKEINQTRDrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1882 EQAAQHKADIEER---------LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKaaagKAELELELGRIR 1952
Cdd:TIGR00606 660 GATAVYSQFITQLtdenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK----RRDEMLGLAPGR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1953 SNAEDtLRSKEQAELEAARQRQLAAEEERRRREAEERVQ-KSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE 2031
Cdd:TIGR00606 736 QSIID-LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2032 SaRQLQLAQEAAQKRLQAEEKAHAF-AVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2110
Cdd:TIGR00606 815 L-QGSDLDRTVQQVNQEKQEKQHELdTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2111 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEK--------HKKFAEQTLRQKA 2182
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLK 973
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2183 QVEQELTTLRLQLEETDHQKNLLDEELqRLKAEATEAARQRSQVEEELFSVRVQMEELSKLK 2244
Cdd:TIGR00606 974 QKETELNTVNAQLEECEKHQEKINEDM-RLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1692-1849 |
1.88e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.25 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1692 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqrEAAAATQKRQELEAELAKVRAemevllAS 1770
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1771 KARAEEESRSTSEKSKQRLEAEAGRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1849
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
33-152 |
2.25e-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: 50.44 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 33 AQDEQDERDRVQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHK 99
Cdd:cd21325 14 SEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFII 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 100 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 152
Cdd:cd21325 94 QENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1347-1594 |
2.26e-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: 53.88 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1347 EERLAEQQRAEERERLAEVEAAlekQRQLAEAHAQAKAQaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR 1426
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSQGL---ASRLTPEEYRKRKR-TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1427 QSSEAEIQAK-------------ARQAEAAERS-----------RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1482
Cdd:pfam05667 286 GSSTTDTGLTkgsrfthteklqfTNEAPAATSSpptkveteeelQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLRRQVQ------------DESQRKRQAEVELASRVKAEAEAAREKQRA--LQALEELRL----Q 1544
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQYKvkkktldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEaksnK 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1545 AEEAERRLRQAEVERARQVQVAletaqrsaeAELQSKRASFAEKTAQLER 1594
Cdd:pfam05667 446 EDESQRKLEEIKELREKIKEVA---------EEAKQKEELYKQLVAEYER 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3926-3963 |
2.28e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.28e-06
10 20 30
....*....|....*....|....*....|....*...
gi 41322919 3926 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3963
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1752-2409 |
2.29e-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: 54.35 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1752 ELEAELAKVRAEMEVLLAskaraEEESRSTSEKSKQRLEAEAgrfreLAEEAARLRALAEEAKRQRQLAEEDAARQRAEA 1831
Cdd:pfam15921 246 QLEALKSESQNKIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1832 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASDSELERQKG 1911
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1912 LVEDTLRQRRQVEEEIlalkasfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAARQrqlaaeeerrrrEAEERVQ 1991
Cdd:pfam15921 393 LSLEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQ 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1992 KSLAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQL-AQEAAQKRLQAEEKAHAFAVQQKEQELQQTL 2069
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLeSSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2070 QQEQSVLDQLRgeaeaaRRAAEEAEEARVQAEREAAqsRRQVEEAERLKQsaeeqaqaraqaqaaaeklrkeaeqeaarr 2149
Cdd:pfam15921 524 SRVDLKLQELQ------HLKNEGDHLRNVQTECEAL--KLQMAEKDKVIE------------------------------ 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2150 aqaeqaALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV-- 2226
Cdd:pfam15921 566 ------ILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvn 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2227 --EEELFSVRVQMEELSKLKARIEAENRAL--ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQ---EAAR--LRQLA 2297
Cdd:pfam15921 640 agSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQselEQTRntLKSME 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2298 EED-------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaEETQGF 2364
Cdd:pfam15921 720 GSDghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQ 798
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 41322919 2365 QRTLeaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2409
Cdd:pfam15921 799 ERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1326-1563 |
2.37e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1326 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREAKELQQrMQEEVVR 1403
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1404 REEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggAEGELQALRAR-A 1482
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEaAREKQRALQALEELrlqAEEAERRLRQAEVERARQ 1562
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVAREL---YESLLQRLEEARLAEALT 384
|
.
gi 41322919 1563 V 1563
Cdd:COG3206 385 V 385
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2159-2344 |
2.77e-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: 53.49 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2159 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKNLLDEELQRLKAEAteaarqrSQVEEELFSVRVQME 2238
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2239 ELSKLKARIEaenRAL-ILRDKDNT----QRFLQEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2310
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 41322919 2311 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2344
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1716-2603 |
3.48e-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: 53.82 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1716 IRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1793
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1794 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1873
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1874 AFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQkglvedtlrQRRQVEEeilalkasfeKAAAGKAELELELGRIRS 1953
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1954 NAEdtLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2033
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2034 rQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQL-RGEAEAARRAAEEAEEARVQAEREAAQSRRQVE 2112
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2113 EAERLKQSAEEQAQARAQAQAAAEKlRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR 2192
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLA-RLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVY 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2193 LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELsklkarieaenralilrdkdntQRFLQEEAEK 2272
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL----------------------QDLTEKLSEA 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2273 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAekmlkekmqavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQ 2352
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA-----------LKLTALHALQLTLTQERV--REHALSIRVLPKE 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2353 MAQQlaeetqgfqrtleaerqrqlemsaeaerlklrvaemsraQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2432
Cdd:TIGR00618 674 LLAS---------------------------------------RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2433 TLEIQRQQSdhdAERLREAIAELEREKEKLQQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLsekdsLLQRERFIEQE 2512
Cdd:TIGR00618 715 EYDREFNEI---ENASSSLGSDLAAREDALNQSLKELM---HQARTVLKARTEAHFNNNEEVTA-----ALQTGAELSHL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2513 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQ 2592
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQ 863
|
890
....*....|.
gi 41322919 2593 RLREQLQLLEE 2603
Cdd:TIGR00618 864 LTQEQAKIIQL 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1149-1580 |
3.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1149 LRDELRGAQEVGERLQQRHGERDV-EVERWRERVAQLLERwQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDAR 1227
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1228 RRQEQIQAMpladsQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLepvaSPAKKPKVQS 1307
Cdd:COG4717 126 QLLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----SLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1308 GSESVIQEYVDLRTHYSELTTLTSQyIKFISETLRRMEEE-ERLAEQQRAEERERLAEVEAAL----------------- 1369
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEE-LEELEEELEQLENElEAAALEERLKEARLLLLIAAALlallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1370 -EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRsIQEELQQLRQSSEAEIQAKARQAEAAERSRL 1448
Cdd:COG4717 276 aGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE-LLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1449 RIEEEIRVVRLQLEATERQ----RGGAEGElQALRARAEEAEaQKRQAQEEAERLRRQVQDE-SQRKRQAEVELASRVKA 1523
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallaEAGVEDE-EELRAALEQAE-EYQELKEELEELEEQLEELlGELEELLEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1524 EAEAAREKQRALQAlEELRLQAEEAERRLRQAEVERARQVQvALETAQRSAEAELQS 1580
Cdd:COG4717 433 ELEELEEELEELEE-ELEELREELAELEAELEQLEEDGELA-ELLQELEELKAELRE 487
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
44-151 |
3.83e-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: 49.66 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 44 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 110
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 41322919 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 151
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
966-1505 |
3.91e-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: 53.43 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 966 QQLLQSLEQGAQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIA-EQQKAQAEVEGLGKGVARLS 1044
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1045 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRGTQGAEEVLRAHEEQLKEAQAVpaTLPE 1124
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1125 LEATKASLKKLRAQAEAQQPTFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1195
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1196 DVRQRELEQLGRQLRYYRESADPLGAWLQDARR---RQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfa 1272
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1273 kQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAE 1352
Cdd:TIGR00618 643 -LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN 721
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1353 QQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAEREAKELQQRMQEEVV------RREEAAVDAQQQKRSIQEELQQL 1425
Cdd:TIGR00618 722 EIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAalqtgaELSHLAAEIQFFNRLREEDTHLL 801
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1426 RQsSEAEIQAKARQAEAAersRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1505
Cdd:TIGR00618 802 KT-LEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2803-2839 |
4.07e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 4.07e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 2803 IRLLEAQIATGGVIDPVHSHRVPVDVAYRRGYFDEEM 2839
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1743-1974 |
4.49e-06 |
|
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: 52.46 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1743 AAAATQKRQELEAELAKVRAEMEVL---LASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQL 1819
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELekeLAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1820 AEEDAARQRAEAERVLAeKLAAIGEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRlEEQAAQHKADIEErLAQLR 1899
Cdd:COG4942 95 LRAELEAQKEELAELLR-ALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPAR-REQAEELRADLAE-LAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1900 KASDSELERQKglvedtlRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQ 1974
Cdd:COG4942 167 AELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1352-1534 |
4.57e-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: 51.08 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1352 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAavdaqqqkrsiqeELQQLRQSSEA 1431
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-------------EEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1432 EIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkr 1511
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE--- 166
|
170 180
....*....|....*....|...
gi 41322919 1512 qaevELASRVKAEAEAAREKQRA 1534
Cdd:COG1579 167 ----ELAAKIPPELLALYERIRK 185
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2257-2412 |
4.77e-06 |
|
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: 52.65 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2257 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2333
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2334 QQKELAQEQARRLQEDKE---QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRaqaRAEEDAQRF---- 2406
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 41322919 2407 -RKQAEE 2412
Cdd:pfam15709 512 aMKQAQE 518
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1406-1605 |
4.94e-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: 52.16 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1406 EAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvRLQLEATERQrggaeGELQALRARAEEA 1485
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ----RAAAEKAAKQ-----AEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1486 EAQKRQAQEEAErlrrqvqdesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL---RQAEVERARQ 1562
Cdd:TIGR02794 120 QAEEAKAKQAAE-----------AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAK 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322919 1563 VQValETAQRSAEAElQSKRASFAEKTAQLERSLQEEHVAVAQ 1605
Cdd:TIGR02794 189 AKA--EEAKAKAEAA-KAKAAAEAAAKAEAEAAAAAAAEAERK 228
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1331-2058 |
5.38e-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: 52.83 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1331 SQYIKFIS---ETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQAEREA---KELQQRMQEEVVRR 1404
Cdd:pfam07111 62 SQQAELISrqlQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEGLRAAlagAEMVRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1405 EeaavdAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSrlrieeeirvvrlqLEATERQRGGAEGELQalraraee 1484
Cdd:pfam07111 141 E-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLA-------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1485 aeaqkrQAQEEAERLRRQVQdESQRKRQAEVELASRVKaeaeaareKQRALQALEELRLQAEEAERRLRQAEVERARQVQ 1564
Cdd:pfam07111 194 ------EAQKEAELLRKQLS-KTQEELEAQVTLVESLR--------KYVGEQVPPEVHSQTWELERQELLDTMQHLQEDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1565 VALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRaqqqaeaerareeaereLERWQLKANeALRL 1644
Cdd:pfam07111 259 ADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL-----------------LNRWREKVF-ALMV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1645 RLQAEEVAQQKSLAQAEAEKQKEEAEREarrrGKAEEQAVRQRELaeqelekqrqlaegtaqQRLAAEQELIRLRAETEQ 1724
Cdd:pfam07111 321 QLKAQDLEHRDSVKQLRGQVAELQEQVT----SQSQEQAILQRAL-----------------QDKAAEVEVERMSAKGLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1725 GEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSekskQRLEAEAGRFRELAEEAA 1804
Cdd:pfam07111 380 MELSRA--QEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLS----NRLSYAVRKVHTIKGLMA 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1805 RLRALAEeaKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1884
Cdd:pfam07111 454 RKVALAQ--LRQESCPPPPPAPPVDADLSLELEQLRE--ERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1885 AQHKADIEERLAQLRKASDSELERQKGLVED--TLRQRRQVEEEILAlKASFEKAAagkaelELELgRIRSNAEDTLRsk 1962
Cdd:pfam07111 530 EQELQRAQESLASVGQQLEVARQGQQESTEEaaSLRQELTQQQEIYG-QALQEKVA------EVET-RLREQLSDTKR-- 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1963 eqaeleaarqrqlaaeeerRRREAEERVQK---SLAAEEEAARQRKAALEEVERLK--AKVEEARRLRERAEQ-ESARQL 2036
Cdd:pfam07111 600 -------------------RLNEARREQAKavvSLRQIQHRATQEKERNQELRRLQdeARKEEGQRLARRVQElERDKNL 660
|
730 740
....*....|....*....|..
gi 41322919 2037 QLAQEAAQKRLQAEEKAHAFAV 2058
Cdd:pfam07111 661 MLATLQQEGLLSRYKQQRLLAV 682
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1678-1972 |
5.43e-06 |
|
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: 53.30 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEElarlqreaaaatqkRQE 1752
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEE--------------SRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1753 LEAELAKVRAEMEVLLAS-------------------KARAEEESRSTSEKSKQRLEAEAGRF----RELAEEAARLRAL 1809
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAG 1697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1810 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1889
Cdd:NF012221 1698 VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDES 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1890 DIEERlaqlRKASDSELERQKGLVEDtlrqrrqVEEEILALKASFEKAAAGKaelelelgrirsNAEDtLRSKEQAELEA 1969
Cdd:NF012221 1778 DKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG-LTEQEQEALEG 1833
|
...
gi 41322919 1970 ARQ 1972
Cdd:NF012221 1834 ATN 1836
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3394-3426 |
5.59e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.78 E-value: 5.59e-06
10 20 30
....*....|....*....|....*....|...
gi 41322919 3394 ATGFLVDPVRNQRLYVHEAVKAGVVGPELHEQL 3426
Cdd:pfam00681 7 ATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1517-1765 |
5.93e-06 |
|
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: 52.07 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1517 LASRVKAEAEAAREKQRALQALEElRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1596
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1597 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1676
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1756
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 41322919 1757 LAKVRAEME 1765
Cdd:COG4942 229 IARLEAEAA 237
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1710-1805 |
6.08e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1710 AAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1789
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 41322919 1790 EAEAGRFrELAEEAAR 1805
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1372-1500 |
6.14e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.59 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1372 QRQLAEAHAQ-AKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKArQAEAAERSRLRI 1450
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1451 EEEIRVVRLQLEATERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1500
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2166-2603 |
7.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2166 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA------EATEAARQRSQVEEELFSVRVQMEE 2239
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2240 LSKLKARIEAENRALI--LRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2317
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2318 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2392
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2393 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-EAKL 2468
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2469 LQLKSEEMQtvqqeqllqetqalQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQqrqqqqmeqerqrl 2548
Cdd:PRK03918 542 KSLKKELEK--------------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER-------------- 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2549 VASMEEARRRQHE---AEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE 2603
Cdd:PRK03918 594 LKELEPFYNEYLElkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
154-261 |
7.12e-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: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 154 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFSVAERDLGV 232
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 41322919 233 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 261
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1378-1866 |
7.21e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.75 E-value: 7.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1378 AHAQAKAQAEREAKELQQR------MQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE--AEIQAKARQAEAAERsrlr 1449
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAkaaktpAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDnfPKLSAELRQQLNNER---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1450 ieEEIRVVRLQLEAterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDESQRKRQAEVElASRVKAEAEaar 1529
Cdd:PRK10929 93 --DEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQLNEIE--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1530 ekqRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSA--EAELQSKRASFAEK-TAQLERSLQeehvavaql 1606
Cdd:PRK10929 158 ---RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1607 reeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgkaeeqavRQ 1686
Cdd:PRK10929 226 ----------------------------------ALRNQLNSQ-----------------------------------RQ 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1687 RElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQREAAAATQK-RQELEA------ELAK 1759
Cdd:PRK10929 237 RE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlreqsqWLGV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1760 VRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAE 1837
Cdd:PRK10929 315 SNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAEQNRILDA 383
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 41322919 1838 KLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1866
Cdd:PRK10929 384 QLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1681-1972 |
7.81e-06 |
|
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: 51.61 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQR-------EAAAATQKRQEL 1753
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1754 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1832
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1833 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SDSELERQ 1909
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1910 KGLVEDTLRQRRQVEEEILALKASFEKAAagkAELELELGRIRSNaedtlRSKEQAELEAARQ 1972
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQAN---RRLKEELQRERAE-----RALAQGALEIARE 399
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2157-2359 |
8.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2157 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQknLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2236
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2237 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAArlrqlaeEDLAQQRAlaekmlkekm 2316
Cdd:COG4913 325 LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA-------EEFAALRA---------- 387
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322919 2317 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAE 2359
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
619-711 |
8.30e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.32 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 619 HSFVAAATKELMWLNEKEEEEVGFDWSDRNTNMTAKKESYSALMRELELKEKKIKELQNAGDRLLREDHPARPTVESFQA 698
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 41322919 699 ALQTQWSWMLQLC 711
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3094-3130 |
8.42e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 8.42e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 3094 KLLSAEKAVTGYRDPYTGQSVSLFQALKKGLIPREQG 3130
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1895-2417 |
8.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1895 LAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELelgrirsnaedtlRSKEQAELEAARQRq 1974
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-------------LEEELEELEAELEE- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1975 laAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2054
Cdd:COG4717 114 --LREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2055 AfAVQQKEQELQQTLQQEQSVLDQLRgeAEAARRAAEEAEEARVQAEREAAQSRRQVEEAERLKQSA---EEQAQARAQA 2131
Cdd:COG4717 192 E-ELQDLAEELEELQQRLAELEEELE--EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAaalLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2132 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQR 2211
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2212 LKAEATEAARQRSQVEEElfsvrVQMEELSKLKARIEAENRALIlrdkdntqRFLQEEAEKMKQVAEEAARLSvaaqeaA 2291
Cdd:COG4717 349 LQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEEL--------RAALEQAEEYQELKEELEELE------E 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2292 RLRQLAEEDLAQQRALAEKMLKEKMQAVQEatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2371
Cdd:COG4717 410 QLEELLGELEELLEALDEEELEEELEELEE-----ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 41322919 2372 RQRQLEmsaEAERLKLRVAEMSRAQARAEEDAQ-RFRKQAEEIGEKL 2417
Cdd:COG4717 485 LRELAE---EWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1227-1559 |
9.06e-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: 51.82 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1227 RRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGE---KVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKP 1303
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1304 KVQSG-SESVIQEYVDlrthysELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERER---LAEVEAALEKQRQLAEAH 1379
Cdd:pfam07888 121 LAQRAaHEARIRELEE------DIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1380 AQAK-AQAEREAKELQqrMQEEVVRREEAAVDAQQQKRSIQEELQQLR------QSSEAEIQAKARQAEAAERSRLRIEE 1452
Cdd:pfam07888 195 QELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLEELRslqerlNASERKVEGLGEELSSMAAQRDRTQA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1453 EIRVVRLQLEATERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREK 1531
Cdd:pfam07888 273 ELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK 352
|
330 340
....*....|....*....|....*...
gi 41322919 1532 QRALQALEELRLQAEEAERRLRQAEVER 1559
Cdd:pfam07888 353 DCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3462-3498 |
9.47e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.47e-06
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 3462 IRLLEAQIATGGIIDPVHSHRVPVDVAYQRGYFSEEM 3498
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1553 |
9.98e-06 |
|
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: 52.05 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1024 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRGTQGAEE 1103
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1104 VLRAHEEQLKEAQAVPATLPELEATKASLkklraQAEAQQpTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1183
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1184 LLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLGAWLQDARRRQEQIqamplADSQAVREQLRQEQALLEE 1257
Cdd:pfam05557 144 LKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELARI-----PELEKELERLREHNKHLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1258 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKK------------PKVQSGSESVIQEYVDLRTHYSE 1325
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaqdtglnlRSPEDLSRRIEQLQQREIVLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1326 LTTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAHAQA 1382
Cdd:pfam05557 299 NSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNYSPQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1383 KAQAEREAKELQQRMQeevVRREEAAVDAQQQKRSIQEELQQLrQSSEAEIQAKARQAEAAERSRLRIE-----EEIRVV 1457
Cdd:pfam05557 378 LLERIEEAEDMTQKMQ---AHNEEMEAQLSVAEEELGGYKQQA-QTLERELQALRQQESLADPSYSKEEvdslrRKLETL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1458 RLQLEATERQRGGAEGEL--QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRAL 1535
Cdd:pfam05557 454 ELERQRLREQKNELEMELerRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570 580
....*....|....*....|....*..
gi 41322919 1536 ---------QALEELRLQAEEAERRLR 1553
Cdd:pfam05557 534 pettstmnfKEVLDLRKELESAELKNQ 560
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1337-1542 |
1.09e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQK 1415
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1416 RSIQEELQQLRQsseaeiqakarQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKR----- 1490
Cdd:COG1842 94 AELEAQAEALEA-----------QLAQLEEQVEKLKEALRQLESKLEELKAKK-------DTLKARAKAAKAQEKvneal 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1491 ------QAQEEAERLRRQV-QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELR 1542
Cdd:COG1842 156 sgidsdDATSALERMEEKIeEMEARAEAAAELAAGDSLDDELAELEADSEVEDELAALK 214
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1338-1588 |
1.13e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.41 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1338 SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvrREEAAVDAQQQKRS 1417
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSW--EKEEKRDSRLGRYK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1418 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQ---------------------------RGG 1470
Cdd:pfam02029 130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVkdekikkekkvkyeskvfldqkrghpeVKS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1471 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK----RQAEVELASRvkaEAEAAREKQR-ALQALEEL---- 1541
Cdd:pfam02029 210 QNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKleelRRRRQEKESE---EFEKLRQKQQeAELELEELkkkr 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1542 ---RLQAEEAERRLRQAEVERarqvQVALETAQRSAEAELQSKRASFAEK 1588
Cdd:pfam02029 287 eerRKLLEEEEQRRKQEEAER----KLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1769-1968 |
1.14e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1769 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1848
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1849 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEIL 1928
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41322919 1929 ALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1968
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1014-1606 |
1.14e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1014 EPARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISL 1093
Cdd:PRK10246 254 ELQQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1094 VIRGTQGAEEVLRAHEEQLKEAQAVPATLPELeatkaslkklrAQAEAQQPTFDALRDELRG-----AQEVGERLQQRhg 1168
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR-- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1169 erdveveRWRERVAQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLGAWLQDARRRQEQIQAmplADSQA 1243
Cdd:PRK10246 384 -------QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNV 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1244 VREQLRQEQALLEEIERHGEKVEE-------CQRFAKqyinaIKDYELQ--------------------LVTYKAqLEPV 1296
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLEAQraqlqagqpcplcgstshpaVEAYQA-LEPG 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1297 ASPAKKPKVQSGSESVIQEYVDLRthySELTTLTSQYIKFISETLRRMEEEERLAEQQRaeererlaEVEAALEKQRQLA 1376
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALR---GQLDALTKQLQRDESEAQSLRQEEQALTQQWQ--------AVCASLNITLQPQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1377 EAHAQAKAQAEREAKELQQRMQEEVVRREEAAvdAQQQKRSIQEELQQLRQSSEAEIQAKARQ--AEAAERSRL--RIEE 1452
Cdd:PRK10246 596 DDIQPWLDAQEEHERQLRLLSQRHELQGQIAA--HNQQIIQYQQQIEQRQQQLLTALAGYALTlpQEDEEASWLatRQQE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1453 EIRVVRLQLEATERQRGGAE--------GELQALRARAEEAEAQK-RQAQEEAERLRRQVQ-------DESQRKRQAEVE 1516
Cdd:PRK10246 674 AQSWQQRQNELTALQNRIQQltplletlPQSDDLPHSEETVALDNwRQVHEQCLSLHSQLQtlqqqdvLEAQRLQKAQAQ 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1517 LASRVKAEAEAAREKQRALQALEELRLQAEEAERRLrqaevERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSL 1596
Cdd:PRK10246 754 FDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNL-----ENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
650
....*....|
gi 41322919 1597 QEEHVAVAQL 1606
Cdd:PRK10246 829 QELAQLAQQL 838
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1304-1519 |
1.20e-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: 50.92 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1304 KVQSGSESVIQEYVDLRTHYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA-- 1378
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLal 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1379 --HAQAKAQAEREAKELQQRMQEevvRREEAavdaqQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIrv 1456
Cdd:COG4942 125 llSPEDFLDAVRRLQYLKYLAPA---RREQA-----EELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1457 vrlqleaTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1519
Cdd:COG4942 195 -------AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3928-3966 |
1.20e-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: 1.20e-05
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3928 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3966
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1692-2080 |
1.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1692 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQR--EAAAATQKRQELEAELAKVRAEMEvlla 1769
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1770 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEaervlaeklaaigEATRLK 1849
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-------------ELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1850 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrQVEEEILA 1929
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1930 LKASF---EKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2006
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2007 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEK-AHAFAVQQKEQELQQTLQQEQSVLDQLR 2080
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEEELEELEEELEELE 445
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
41-140 |
1.36e-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: 47.27 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 41 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 116
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 41322919 117 LVNIRNDDIADGNPKLTLGLIWTI 140
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1677-2060 |
1.37e-05 |
|
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: 51.55 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQREAAAATQK 1749
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1750 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1824
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1825 ARQRAEAERvlaeklaaiGEATRL---KTEAEIA---------LKEKEAENERLRRLAEDEAFQRRR---LEEQAAQHKA 1889
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAeeeakrradAKLKEAVEKNVATSEQDKPKRRAKrgvLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1890 DIEErlaqlrKASDSELERQKgLVEDTLRQRRQVEEEILALKASFEKAAAGKAE------------LELELgrirsnAED 1957
Cdd:NF033838 280 ENDA------KSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AES 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1958 TLRSKEqAELEAARQRQLAAEEERRRREAEERVQKSLAAE---EEAARQRKAALEEVERlkaKVEEARRLRER-AEQ-ES 2032
Cdd:NF033838 347 DVKVKE-AELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEEAKR---KAAEEDKVKEKpAEQpQP 422
|
410 420
....*....|....*....|....*....
gi 41322919 2033 ARQLQLAQEAAQKRLQAEE-KAHAFAVQQ 2060
Cdd:NF033838 423 APAPQPEKPAPKPEKPAEQpKAEKPADQQ 451
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1781-2052 |
1.43e-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: 50.69 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1781 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA-EIALKEK 1859
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1860 EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKAsfeKAAA 1939
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1940 GKAELELELGRIRSNAEDTLRSKEQAElEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAK-V 2018
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270
....*....|....*....|....*....|....
gi 41322919 2019 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2052
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE 290
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1351-1779 |
1.52e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.06 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1430
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1510
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1511 RQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTA 1590
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1591 QLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1670
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1671 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKR 1750
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 41322919 1751 QELEAELAKVRAEMEVLLASKARAEEESR 1779
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2269-2428 |
1.54e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2269 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2348
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2349 DKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2428
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1678-1893 |
1.60e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.10 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ-------------LLEEEL 1736
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVikagarpdnsaviAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1737 ARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfrelaeeAARLRALAeeAKRQ 1816
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVA---------AAIARAKA--KKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1817 RQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1893
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2174-2608 |
1.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2174 AEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRA 2253
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2254 LI-LRDKDNTQRFLQEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2332
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2333 QQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRFRKQAE 2411
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2412 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllqETQAL 2491
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2492 QQSFLSEKDSLLQRERFIEQEKAKLEQLfqdEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVrrkqe 2571
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----- 448
|
410 420 430
....*....|....*....|....*....|....*..
gi 41322919 2572 elqqleqqrrqqeellaeenQRLREQLQLLEEQHRAA 2608
Cdd:COG4717 449 --------------------EELREELAELEAELEQL 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2099-2471 |
1.92e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2099 QAEREAAQSRRQVEEAE-RLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQT 2177
Cdd:COG4717 92 ELQEELEELEEELEELEaELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2178 LRQKAQ------------VEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQmEELSKLKA 2245
Cdd:COG4717 172 LAELQEeleelleqlslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2246 RIEAENRALILRDKDNTQRFLQEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLaqQRALAEK 2310
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL--EELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2311 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfqrTLEAERQRQLEMSAEAERLKLRVA 2390
Cdd:COG4717 329 GLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2391 EMSR--AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREAIAELEREK 2459
Cdd:COG4717 406 ELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQELEELKAEL 485
|
410
....*....|..
gi 41322919 2460 EKLQQEAKLLQL 2471
Cdd:COG4717 486 RELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1428-1641 |
1.96e-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: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1428 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1505
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1506 ESQRKRQAEV-------------ELASRVKAEAEAAREKQRALQALEELRLQAEEAerrlrQAEVERARQVQVALETAQR 1572
Cdd:COG3883 93 RALYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAK-----KAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1573 SAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1641
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
32-151 |
2.02e-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: 47.70 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 32 WAQDEQDERdrvQKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFH 98
Cdd:cd21324 16 GTQHSYSEE---EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 99 KLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 151
Cdd:cd21324 93 IQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1999-2343 |
2.16e-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: 50.89 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1999 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQEAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2070
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2071 qeqsvLDQLRgEAEAARRAAEEAEEARVQAEREAAQSR--RQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQeaAr 2148
Cdd:pfam17380 362 -----LERIR-QEEIAMEISRMRELERLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE--A- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2149 raqaeqaalRQKQAADAEMEKhkkfaeqtlrqkaqvEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEE 2228
Cdd:pfam17380 433 ---------RQREVRRLEEER---------------AREMERVRLEEQERQQQ-------VERLRQQEEERKRKKLELEK 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2229 ElfsvrvqmeelSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALA 2308
Cdd:pfam17380 482 E-----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE 550
|
330 340 350
....*....|....*....|....*....|....*....
gi 41322919 2309 EKMLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2343
Cdd:pfam17380 551 RRRIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1362-1456 |
2.22e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1362 LAEVEAALEKQRQLAEAHAQAKAQAEREAkelqQRMQEEVVRREEAAVDAQQQKRSIQEELQQLR-QSSEAEIQAKARQA 1440
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 41322919 1441 EAAERSRLRI---EEEIRV 1456
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2166-2606 |
2.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2166 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEelfsVRVQMEELSKLKA 2245
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2246 RIEAENRALILRDKdNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEedlaqqraLAEKMLKEKMQAVQEATRL 2325
Cdd:PRK03918 249 SLEGSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2326 KAEAELLQQQKELAQEQARRLQEDKEQMA--QQLAEETQGFQRTLEAERQRQLEMSAEAERLK-LRVAEMSRAQARAEED 2402
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKelEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2403 AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---------SDHDAERLREAIAELER-EKEKLQQEAKLLQLK 2472
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEYTAELKRiEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2473 SEEMQTvqqeqllqetqalqQSFLSEKDSLLQRERFIEQEKA---KLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLV 2549
Cdd:PRK03918 480 KELREL--------------EKVLKKESELIKLKELAEQLKEleeKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 2550 ASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHR 2606
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYN 602
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1339-1576 |
2.46e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAEREAKelqqrmqeevvrreeAAVDAQQ 1413
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAK---------------AAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1414 QKRSIQEELQQLRQSSEAEIQAKARqAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqalRARAEEAEAQKRQAQ 1493
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAK-AKAAALAKQKREGTEEVTEEEKAAAKAKAAAAA------KAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1494 EEAERlrrqvQDESQRKRQAEVELASRVKAEAeAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRS 1573
Cdd:PRK07735 151 EEVTE-----EEEETDKEKAKAKAAAAAKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
...
gi 41322919 1574 AEA 1576
Cdd:PRK07735 225 QGN 227
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
39-147 |
2.47e-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: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 39 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 109
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322919 110 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1352-1479 |
2.49e-05 |
|
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: 49.50 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1352 EQQRAEERERLAEVEAALEKQRQLAEAHAQAK-AQAEREAKELQQRMQEEVVrreeaavdaQQQKRSIQEELQQLRQSSE 1430
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKAEaAEQERKLLEEQQRELEQKL---------EDQERSYEEHLRQLKEKME 247
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 41322919 1431 AEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALR 1479
Cdd:cd16269 248 EERENLLKEQERALESKLKEQEALLEEGFKEQAELLQE-----EIRSLK 291
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1635-2053 |
2.51e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1635 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1714
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1715 LIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1794
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1795 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 1874
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1875 FQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSN 1954
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1955 AEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2034
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 41322919 2035 QLQLAQEAAQKRLQAEEKA 2053
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1351-1512 |
2.65e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 50.67 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSE 1430
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 AEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDESQRK 1510
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 41322919 1511 RQ 1512
Cdd:PRK12678 216 EE 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1342-1457 |
2.70e-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: 50.34 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1342 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-EREAKELQQRMQEEVVRREEAAVD---------A 1411
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKR----SIQEELQQLRQSSEAEiqaKARQAEAAERsRLRIEEEIRVV 1457
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAE---EKARLEAEER-RQKEEEAARLA 508
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2160-2362 |
2.72e-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: 50.99 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2160 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDHQknlldeelqrlkAEATEAARQRSQVEEELF 2231
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2232 SVRVqmeELSKLKARIEA----------------ENRALILRDK-----DNTQRFLQEEAEKMKQ--------VAEEAAR 2282
Cdd:NF012221 1617 AVTK---ELTTLAQGLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAK 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2283 LSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQ 2362
Cdd:NF012221 1694 SEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAK 1773
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2282-2448 |
2.75e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2282 RLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELaQEQARRLQEDKEQMAQQLA 2358
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2359 ------EETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGE 2415
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK 183
|
170 180 190
....*....|....*....|....*....|....
gi 41322919 2416 klhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2448
Cdd:PRK12704 184 -----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1062-1502 |
2.95e-05 |
|
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: 50.50 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1062 TLRSELEltlGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQL-----------KEAQAVPATLPE----LE 1126
Cdd:pfam15921 437 AMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlesseRTVSDLTASLQEkeraIE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1127 ATKASLKKLRAQAEAQQPTFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVAQLLE-------RWQAVLAQTD 1196
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrTAGAMQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1197 VRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQrfaKQYI 1276
Cdd:pfam15921 594 QLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELN 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1277 NAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTHYSELTTLTSqyikfiseTLRRMEEEERLAeqqra 1356
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA----- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1357 eererlaeVEAALEKQRQLAEAHAQAKAqaereakelqqrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQssEAEIQAK 1436
Cdd:pfam15921 726 --------MKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ--ELSTVAT 783
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1437 ARQAEAAERSRLRIEEEirvvRLQLEATERQRGGAEGELQAlrarAEEAEAQKRQAQEEAeRLRRQ 1502
Cdd:pfam15921 784 EKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQESV-RLKLQ 840
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1223-1447 |
2.99e-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: 49.76 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1223 LQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakk 1302
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1303 pKVQSGSESVIQEYVD-LRTHY-----SELTTLTSQyiKFISETLRRMEEEERLAEQQRA------EERERLAEVEAALE 1370
Cdd:COG4942 94 -ELRAELEAQKEELAElLRALYrlgrqPPLALLLSP--EDFLDAVRRLQYLKYLAPARREqaeelrADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1371 KQRqlaeahaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQsSEAEIQAKARQAEAAERSR 1447
Cdd:COG4942 171 AER-------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAA 239
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1343-1561 |
3.18e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1343 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1422
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEAEIQAKARQAeaaersrlrieeeirvvrlqLEATERQRGGAEGElqalrARAEEAEAQKRqaQEEAERLRRQ 1502
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEA--------------------LKAKDHKAFDLKQE-----SKASEKEAEDK--ELEAQKKREP 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1503 VQDESQRKRQaevELASRVKAEAEAAREKQR---------ALQALEELRLQAEEAERRLRQAEVERAR 1561
Cdd:pfam05262 333 VAEDLQKTKP---QVEAQPTSLNEDAIDSSNpvyglkvvdPITNLSELVLIDLKTEVRLRESAQQTIR 397
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1647-1823 |
3.40e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1647 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1722
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1723 EQGEQQRQLLEEELArlQREAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAgrfr 1797
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA---- 234
|
170 180
....*....|....*....|....*.
gi 41322919 1798 ELAEEAARLRALAEEAKRQRQLAEED 1823
Cdd:PRK09510 235 KAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2206-2412 |
3.45e-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: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2206 DEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIlRDKDNTQRFLQEEAEKMKQVAEEAARLSV 2285
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2286 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2357
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2358 AEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2412
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1683-2051 |
3.50e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1683 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--REAAAATQKRQELEA 1755
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1756 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1835
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1836 aEKLAAIGEATRLKTEAEIALKEKEAenerlrrlaedeafqrrRLEEQAAQHKADIEERLaqlrkasdsELERQKGLVED 1915
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAED-----------------WLEEFQAKEQEATEELL---------SLEQKLSVAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1916 TLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQR-QLAAEEERRRREAEERVQKSL 1994
Cdd:PRK04863 471 AHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRlRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1995 AAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQAEE 2051
Cdd:PRK04863 551 DDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1231-1546 |
3.51e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1231 EQIQAMPLADSQAVREQLRQEQALLEEIERHGEKveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSE 1310
Cdd:PRK10929 33 EQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1311 SVIQEYVDLRTHYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAer 1388
Cdd:PRK10929 106 ALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 eakelqqrMQEEVVRReEAAVDaqqqkrsiQEELQQLRQSSEAEIqakAR-QAEAAERSRLRIEEEIRVVRLQLEaTERQ 1467
Cdd:PRK10929 178 --------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQALRNQLN-SQRQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1468 RggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEA----EAAREKQRALQALEE 1540
Cdd:PRK10929 237 R------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNT 304
|
....*.
gi 41322919 1541 LRLQAE 1546
Cdd:PRK10929 305 LREQSQ 310
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2181-2733 |
3.60e-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: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2181 KAQVEQELTTLRLQLEETDHQKNLLDEELQRlkaEATEAARQRSQVEEELFSVRVQMEELSKLKAriEAENRALILRDKD 2260
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2261 NTQ-RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2335
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2336 ----KELAQEQARRLQEDKEQMaQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2411
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2412 EIGEKLHRTElatQEKVTLVQT-------LEIQ----RQQSDHDAERLREAIAELEREKEK---LQQEAKLLQLKSEEMq 2477
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQArekeihdLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKEL- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2478 TVQQEQLLQETQALQQSFLSEKDsllQRERFIEQekakLEQLFQDEVakaqqlreeqqRQQQQMEQERQRLVASMEEARR 2557
Cdd:pfam05483 505 TQEASDMTLELKKHQEDIINCKK---QEERMLKQ----IENLEEKEM-----------NLRDELESVREEFIQKGDEVKC 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2558 RQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEE--QHRAALAHSEEVTASQVAATKTLPNGRDaLDG 2635
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhQENKALKKKGSAENKQLNAYEIKVNKLE-LEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2636 PAAEAEPEHSFDGLRRKVSAQRLQEAGIL--------SAEELQRLAQ------GHTTVDELARREDVRH----YLQGRSS 2697
Cdd:pfam05483 646 ASAKQKFEEIIDNYQKEIEDKKISEEKLLeevekakaIADEAVKLQKeidkrcQHKIAEMVALMEKHKHqydkIIEERDS 725
|
570 580 590
....*....|....*....|....*....|....*.
gi 41322919 2698 IAGLLLKATNEKLSVYAALQRQLLSPGTALILLEAQ 2733
Cdd:pfam05483 726 ELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQ 761
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2185-2414 |
4.08e-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: 50.34 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2185 EQELTTLRLQLEE----TDHQKNLLDEELQRLKAEATEAARQRS-----QVEEELFSVRVQMEELSKLKARI-EAENRal 2254
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2255 iLRDKDNTQRFLQEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2334
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2335 Q-KEL---------AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQ 2404
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 41322919 2405 RFRKQAEEIG 2414
Cdd:COG3096 673 RLLALAERLG 682
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1712-1861 |
4.08e-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: 48.38 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1712 EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS-TSEKSKQRLE 1790
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1791 AE----AGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEatrLKTEAEIALKEKEA 1861
Cdd:COG1579 96 KEieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2271-2632 |
4.30e-05 |
|
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: 50.07 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2271 EKMKQVAEEaarLSVAAQEAARLRQLAEEDLAQQRALA-EKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQARRLQED 2349
Cdd:TIGR02169 170 RKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKR-EYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2350 keqmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSraqaraEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2429
Cdd:TIGR02169 246 ----LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2430 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqQEQLLQETQALQQSFLSEKDSLLQRERFI 2509
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE-LEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2510 EQEKAKLEQL------FQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqqRRQQ 2583
Cdd:TIGR02169 395 EKLKREINELkreldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-----------LAAD 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 41322919 2584 EELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDA 2632
Cdd:TIGR02169 464 LSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1342-1550 |
4.32e-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: 49.56 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1342 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEREakelQQRMQEEVVRREEAAVDAQQQKRSIQEE 1421
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRR-FEEIRLRKQRLEEE----RQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1422 LQQLRQsseaEIQAKaRQAEAAERSrlrieeeirvvrlqlEATERQRGGAEGELqalraraeeAEAQKRQAQ-EEAERLr 1500
Cdd:pfam15709 428 FRRKLQ----ELQRK-KQQEEAERA---------------EAEKQRQKELEMQL---------AEEQKRLMEmAEEERL- 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 41322919 1501 rqvqdESQRKRQaEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER 1550
Cdd:pfam15709 478 -----EYQRQKQ-EAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2766-2802 |
4.33e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.33e-05
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 2766 KLLSAERAVTGYKDPYTGQQISLFQAMQKGLIVREHG 2802
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4136-4164 |
4.33e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.33e-05
10 20
....*....|....*....|....*....
gi 41322919 4136 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4164
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2278-2619 |
4.38e-05 |
|
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: 49.97 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2278 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2357
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2358 AEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2432
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2433 TLEIQRQQSDHDAERLREAIAELEREKeKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQE 2512
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2513 KAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLvasmEEARRRQHEAEEGVR-RKQEELQQLEQQRRQQEELLAEEN 2591
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL----EEEEESIELKQGKLTeEKEELEKQELKLLKDELELKKSED 472
|
330 340
....*....|....*....|....*...
gi 41322919 2592 QRLREQLQLLEEQHRAALAHSEEVTASQ 2619
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQ 500
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1403-1756 |
4.57e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1403 RREEAAVDAQQQKRSIQEELQQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1482
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1562
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1563 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1642
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1643 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1722
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 41322919 1723 EQGEQQRQLLEEELARLQREAAAATQKRQELEAE 1756
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1779-1945 |
4.96e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1779 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1857
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1858 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQR--RQVEEEILALKASFE 1935
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEARHEAAVLI 175
|
170
....*....|
gi 41322919 1936 KAAAGKAELE 1945
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1318-1597 |
5.05e-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: 49.45 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1318 DLRTHYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAERE-A 1390
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1391 KELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAE------AAERSRLRIEEEirVVRLQLEAT 1464
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1465 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAarekqralqaleelrl 1543
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA---------------- 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1544 qaeeaerrlRQAEVERARQ--------VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQ 1597
Cdd:pfam15450 446 ---------REFEVEAMRQelaallssVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1479-1654 |
5.68e-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: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1479 RARAEEAEAQ------KRQAQEEAERLRrQVQDESQRKRQAEVELASRVKAEAEAAReKQRalqaLEELRLQAEEAER-- 1550
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQRRLQ-QEQLERAEKMREELELEQQRRFEEIRLR-KQR----LEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1551 -RLRQAEVERARQVQVA----LETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERARE 1625
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKA 490
|
170 180 190
....*....|....*....|....*....|....
gi 41322919 1626 EAERelERWQLKANEALRLRL-----QAEEVAQQ 1654
Cdd:pfam15709 491 RLEA--EERRQKEEEAARLALeeamkQAQEQARQ 522
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
43-144 |
5.71e-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: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 43 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHRQVKLV 118
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 41322919 119 NIRNDDIADGNPKLTLGLIWTIILHF 144
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1330-1496 |
5.90e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1330 TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQ--AKAQAEREAKELQQRMQEEVVRREE- 1406
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPn 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1407 --AAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIR-------VVRLQLEATERQRGGAEGELQA 1477
Cdd:COG3206 290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpELEAELRRLEREVEVARELYES 369
|
170
....*....|....*....
gi 41322919 1478 LRARAEEAEAQKRQAQEEA 1496
Cdd:COG3206 370 LLQRLEEARLAEALTVGNV 388
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2238-2365 |
6.28e-05 |
|
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: 48.34 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2238 EELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEK 2315
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEK 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41322919 2316 MQavQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQ 2365
Cdd:cd16269 246 ME--EERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2263-2472 |
6.35e-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: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2263 QRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2342
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2343 ARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2422
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDE---RILEYLKEKAEREEEREAEREEIEEEKEREIARLR 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 41322919 2423 ATQEKvtlvqTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2472
Cdd:pfam13868 191 AQQEK-----AQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQ 235
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2251-2617 |
6.36e-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: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2251 NRALILRDKDNTQRflQEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2325
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2326 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2391
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2392 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQL 2471
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2472 KSEEMQtvqqeqllqetqalqqsflsekdslLQRERFIEQEKAKLEQLFQdEVAKAQQLREEQQRQQQQMEQERQRLVAS 2551
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2552 MEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQR------LREQLQLLEEQHRAALAHSEEVTA 2617
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTA 630
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2691-2729 |
6.43e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.70 E-value: 6.43e-05
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 2691 YLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTALIL 2729
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1412-1547 |
6.44e-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: 47.61 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQ---SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGA---------EGELQALR 1479
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1480 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEE 1547
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1483-1562 |
6.82e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL----ASRVKAE--AEAAREKQRALQA-LEELRLQAEEAERRLRQA 1555
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqQELVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 41322919 1556 EVERARQ 1562
Cdd:PRK11448 218 RKEITDQ 224
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2261-2728 |
6.88e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.20 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2261 NTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2340
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2341 EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2420
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2421 ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLkseemqtvqqeqLLQETQALQQSFLSEKD 2500
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAA------------LAALLLALLALAAALLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2501 SLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQR 2580
Cdd:COG4995 235 LLLLALLALAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2581 RQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQE 2660
Cdd:COG4995 315 LALLLLAALLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2661 AGILSAEELQRLAQGHTTVDELARREDVRHYLQGRSSIAGLL-LKATNEKLSVYAALQRQLLSPGTALI 2728
Cdd:COG4995 395 LLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIeYIILPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1346-2054 |
7.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1346 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEE 1421
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1422 LQQLR-QSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQ-----LEATERQRGGAEGELQALRARAEEAEAQKRQAQEE 1495
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1496 AERLRRQVQDESQRKRQAEV--ELASRVKAEAEAAREKQRALQALEELRLQAEEAER----RLRQAEVERARQVQVALET 1569
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1570 AQRSAEaelqsKRASFAEKTAQLERSLQEEHVAvaqlreeaerrAQQQAEAERAREEAERELERWQLKANEALRLRLQAE 1649
Cdd:PRK04863 538 LLAEFC-----KRLGKNLDDEDELEQLQEELEA-----------RLESLSESVSEARERRMALRQQLEQLQARIQRLAAR 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1650 EVAQQKslaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLaEGTAQQRLAAEQELIRLRAETEqgEQQR 1729
Cdd:PRK04863 602 APAWLA-----------------------AQDALARLREQSGEEFEDSQDV-TEYMQQLLERERELTVERDELA--ARKQ 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1730 QLLEE----------ELARLQR------------------------------------------EAAAATQKRQELEAEL 1757
Cdd:PRK04863 656 ALDEEierlsqpggsEDPRLNAlaerfggvllseiyddvsledapyfsalygparhaivvpdlsDAAEQLAGLEDCPEDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 AKVRAEMEVLLASKARAEEESRSTSEKSKQRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAE----- 1830
Cdd:PRK04863 736 YLIEGDPDSFDDSVFSVEELEKAVVVKIADR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDvqklq 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1831 -----AERVLAEKLA---------AIGEATRLKTEAEIALKEKEAENERLR--------------------RLAEDEAFQ 1876
Cdd:PRK04863 814 rlhqaFSRFIGSHLAvafeadpeaELRQLNRRRVELERALADHESQEQQQRsqleqakeglsalnrllprlNLLADETLA 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1877 RRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELElELGRIR---- 1952
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALT-EVVQRRahfs 972
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1953 -SNAEDTLrSKEQAELEAARQRQLAAEEERRRREAE-----------ERVQKSLAAEEEAARQ-RKAALEEVE----RLK 2015
Cdd:PRK04863 973 yEDAAEML-AKNSDLNEKLRQRLEQAEQERTRAREQlrqaqaqlaqyNQVLASLKSSYDAKRQmLQELKQELQdlgvPAD 1051
|
810 820 830
....*....|....*....|....*....|....*....
gi 41322919 2016 AKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAH 2054
Cdd:PRK04863 1052 SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1269-1600 |
7.56e-05 |
|
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: 49.24 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1269 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTHY-SELTTLTSQyikfiSETLRRMEEE 1347
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1348 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREA--------KELQQRMQEEVVRREEAAVDAQQQKRSIQ 1419
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1420 EELQQLRQsSEAEIQAKarQAEAaerSRLrieEEIRVVRLQLEATERQRGGAE-GELQALRARAEEAEAQKRQA------ 1492
Cdd:NF033838 201 RDEEKIKQ-AKAKVESK--KAEA---TRL---EKIKTDREKAEEEAKRRADAKlKEAVEKNVATSEQDKPKRRAkrgvlg 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1493 --------QEEAERLRRQVQDES----QRKRQAEVELASRVKAEAEAAREKQR-------ALQALEELRLQAEEAERRLR 1553
Cdd:NF033838 272 epatpdkkENDAKSSDSSVGEETlpspSLKPEKKVAEAEKKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKVK 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1554 QAEVERARQV--QVALETAQRSAEAELQSKRA--SFAEKTAQLERSLQEEH 1600
Cdd:NF033838 352 EAELELVKEEakEPRNEEKIKQAKAKVESKKAeaTRLEKIKTDRKKAEEEA 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2175-2478 |
7.63e-05 |
|
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: 49.35 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2175 EQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE--------------LFSVRVQMEEL 2240
Cdd:pfam15921 345 EELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDR 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2241 SKLKARIEAENRALILRDKDNTQR---FLQEEAEKMKQVAEEAARLSVAAQeaaRLRQLAEEDLAQQRALAEK------- 2310
Cdd:pfam15921 425 NMEVQRLEALLKAMKSECQGQMERqmaAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTAKKMTLESSertvsdl 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2311 --MLKEKMQAVQ----EATRLKAEAEL-LQQQKELAQE--QARRLQEDKEQMAQQLAEEtqgfQRTLEAERQRQLEMSAE 2381
Cdd:pfam15921 502 taSLQEKERAIEatnaEITKLRSRVDLkLQELQHLKNEgdHLRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2382 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR-QQSDHDAERLReAIAELEREKE 2460
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvKLVNAGSERLR-AVKDIKQERD 656
|
330 340 350
....*....|....*....|....*....|....*.
gi 41322919 2461 KLQQEAKL------------------LQLKSEEMQT 2478
Cdd:pfam15921 657 QLLNEVKTsrnelnslsedyevlkrnFRNKSEEMET 692
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1701-2197 |
7.71e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 49.09 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1701 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV----------RAEMEVLLAS 1770
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1771 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1850
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1851 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1930
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1931 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2010
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2011 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAA 2090
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2091 EEAEEARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2170
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 41322919 2171 KKFAEQTLRQKAQVEQELTTLRLQLEE 2197
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1359-1769 |
7.80e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1359 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVvRREEAAVDAQQQKRSIQEELQQLRQSSEAEiqaKAR 1438
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERL-AELEAKRQAEEEAREAKAEAEQRAAELAAE---AAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1439 QAEAAERSRLRIEEEIRvvrlqlEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELA 1518
Cdd:COG3064 78 KLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1519 SRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:COG3064 152 AEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASRE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1599 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1678
Cdd:COG3064 232 AALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1679 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1758
Cdd:COG3064 312 AAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGI 391
|
410
....*....|.
gi 41322919 1759 KVRAEMEVLLA 1769
Cdd:COG3064 392 LAAAGGGGLLG 402
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3797-3833 |
7.89e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.89e-05
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 3797 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3833
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2168-2646 |
7.94e-05 |
|
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: 49.07 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2168 EKHKKFAEQTLRQKAQVEQELTTLRLQL-EETDHQKNLLDEELQRLKAEATEAARQRSQV---EEELFSVRVQMEELSKL 2243
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2244 KARIEAENRAlilrdkdntQRFLQEEAEKMKQVAEEAARlsvaaqeaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT 2323
Cdd:pfam12128 477 REEQEAANAE---------VERLQSELRQARKRRDQASE---------ALRQASRRLEERQSALDELELQLFPQAGTLLH 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2324 RLKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA------ 2395
Cdd:pfam12128 539 FLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsare 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2396 -QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2473
Cdd:pfam12128 619 kQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKH 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2474 EEMQTVQQEQLLQETQALQQSFL---SEKDSLLQR-----ERFIEQEKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQER 2545
Cdd:pfam12128 699 QAWLEEQKEQKREARTEKQAYWQvveGALDAQLALlkaaiAARRSGAKAELKAL-ETWYKRDLASLGVDPDVIAKLKREI 777
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2546 QRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEE----VTASQVA 2621
Cdd:pfam12128 778 RTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMerkaSEKQQVR 857
|
490 500 510
....*....|....*....|....*....|...
gi 41322919 2622 ATKTLPNGRD--------ALDGPAAEAEPEHSF 2646
Cdd:pfam12128 858 LSENLRGLRCemsklatlKEDANSEQAQGSIGE 890
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2209-2422 |
8.15e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2209 LQRLKAEATEAARQRSQVEEElfsvrvQMEELSKLKARIEAENRALilrdkdnTQRFLQEEAEKmKQvAEEAARLSVAAQ 2288
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL-------EKERLAAQEQK-KQ-AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2289 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQGFQRT 2367
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2368 LEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2422
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1339-1534 |
8.23e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEER---LAEQQRAEererlaeveaaLEKQRQLAEAHAQAKAQAEREAKELQQRMQ----------EEVVRRE 1405
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE-----------LDASRALAEKQKHELDTEKRCAEELKEAMQmamegharmlEQYADLE 1120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1406 EAAVDAQQQKRSIQEELQQLRQsseAEIQAKARQAE-------AAERSRLRI--EEEIRVVRLQLEATERQ-RGGAE--- 1472
Cdd:PLN03188 1121 EKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVerEKERRYLRDENKSLQAQlRDTAEavq 1197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1473 --GELQALRARAEEA--EAQKR--QAQEEAERLRRQVqDESQRKRQAEVELASRVKAEAEAAREKQRA 1534
Cdd:PLN03188 1198 aaGELLVRLKEAEEAltVAQKRamDAEQEAAEAYKQI-DKLKRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1681-2002 |
8.46e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1840
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1841 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQR 1920
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1921 RQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEA 2000
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 41322919 2001 AR 2002
Cdd:COG4372 368 AD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1403-1741 |
8.69e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1403 RREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1482
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1483 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1562
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1563 VQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1642
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1643 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1722
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330
....*....|....*....
gi 41322919 1723 EQGEQQRQLLEEELARLQR 1741
Cdd:COG4372 323 ELAKKLELALAILLAELAD 341
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1339-1833 |
9.18e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.50 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1418
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1419 QEELQQLRQSSEAEIQAKARQAEAAERSRlrieeeirvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1498
Cdd:COG3064 83 EKAAAEAEKKAAAEKAKAAKEAEAAAAAE------------KAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1499 LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAEL 1578
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1579 QSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1658
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1659 QAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELAR 1738
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1739 LQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQ 1818
Cdd:COG3064 391 ILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVA 470
|
490
....*....|....*
gi 41322919 1819 LAEEDAARQRAEAER 1833
Cdd:COG3064 471 LDGGAVLADLLLLGG 485
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2213-2403 |
9.20e-05 |
|
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: 47.92 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2213 KAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAAR 2292
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2293 LRQLAEEDLAQQrALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGfQRTLEAER 2372
Cdd:TIGR02794 126 AKQAAEAKAKAE-AEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK-AKAEAAKA 203
|
170 180 190
....*....|....*....|....*....|.
gi 41322919 2373 QRQLEMSAEAERLKLRVAEMsRAQARAEEDA 2403
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAA-EAERKADEAE 233
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1792-1911 |
9.39e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.79 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1792 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAE 1862
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1863 NERLRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA---SDSE-LERQKG 1911
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKAgweADSKtLRFSKG 261
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1677-1799 |
9.58e-05 |
|
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: 47.51 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQR-----EAAAATQKR 1750
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1751 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1799
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1102-1818 |
9.81e-05 |
|
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: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1102 EEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAqqptfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1180
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1181 VAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplGAWLQDARRRQEQIQAMpLADSQavrEQLRQEQALLEEIER 1260
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQ-LSKTQ---EELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1261 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTHYSELTTLTSQY 1333
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1334 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAEREAKeLQQRMQEEvvrreeaAVDAQ 1412
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDK-------AAEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1413 QQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLrIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1492
Cdd:pfam07111 370 VERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1493 QEEAER--LRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEEL--RLQAEEAERRLRQAEVERARQVQVAle 1568
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVA-- 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1569 taqRSAEAELQSKRASFAEKTAQLERSLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1648
Cdd:pfam07111 527 ---QQLEQELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1649 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1723
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1724 QGEQQR-----QLLEEE----LARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1789
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 41322919 1790 EAEAGRFRELAEEAARLRALAEEAKRQRQ 1818
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3350-3384 |
1.09e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322919 3350 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3384
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1681-1876 |
1.16e-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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1757
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1822
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQIAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1823 DAARQRAEAERVLAEKLAAIG-EATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1876
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEaELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1695-2058 |
1.19e-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: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1695 EKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA--AATQKRQELEAELAKVRAEM--EVLLAS 1770
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAeeEAREAKAEAEQRAAELAAEAakKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1771 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1850
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1851 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILAL 1930
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1931 KASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEE 2010
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 41322919 2011 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAV 2058
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
44-141 |
1.20e-04 |
|
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: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 44 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 110
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 41322919 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4385-4422 |
1.22e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*...
gi 41322919 4385 QRFLEVQYLTGGLIEPDTPGRVPLDEALQRGTVDARTA 4422
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2177-2409 |
1.27e-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: 47.53 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2177 TLRQKAQVEQELTTLRLQleetdhQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALIL 2256
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2257 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2330
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2331 LLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2409
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3966-4000 |
1.30e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.30e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322919 3966 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 4000
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1833-2604 |
1.34e-04 |
|
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: 48.53 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1833 RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqHKADIEERLAQLRKASDSELERQKgl 1912
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGYELLKEK-- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1913 vEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAED-TLRSKEQAELEAARQRQLAAEEERRRREAEERVQ 1991
Cdd:TIGR02169 233 -EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1992 KSLAAEEEAARQRKAALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFAVQQKE 2062
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2063 QELQQtlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE-RLKQSAEEqaqaraqaqaaaeklrke 2141
Cdd:TIGR02169 389 DYREK--------LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEaKINELEEE------------------ 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2142 aeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEA---TE 2218
Cdd:TIGR02169 443 ------------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQArasEE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2219 AARQRSQVEEELFS----VRVQMEELSKLKAR------IEAENR--ALILRDKDNTQR---FLQEEA---------EKMK 2274
Cdd:TIGR02169 505 RVRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMR 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2275 QVAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAE 2328
Cdd:TIGR02169 585 DERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRG 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2329 AELLQQQKElaqEQARRLQEDKEQMAQQLAeetqGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRK 2408
Cdd:TIGR02169 665 GILFSRSEP---AELQRLRERLEGLKRELS----SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2409 QAEEIGEKLhrtelatqekvtlvQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ-----EAKLLQLKSEEMQtvQQEQ 2483
Cdd:TIGR02169 738 RLEELEEDL--------------SSLEQEIENVKSELKELEARIEELEEDLHKLEEalndlEARLSHSRIPEIQ--AELS 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2484 LLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAE 2563
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 41322919 2564 E---GVRRKQEELQQLEQQRRQQEELLAEENQRLREQLQLLEEQ 2604
Cdd:TIGR02169 882 SrlgDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1481-1605 |
1.38e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1481 RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalQALEELRL------QAEEAERRLRQ 1554
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK--QAEEAAKQaalkqkQAEEAAAKAAA 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1555 AEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQ 1605
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1794-2040 |
1.40e-04 |
|
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: 47.97 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1794 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1873
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1874 AFQRRRLEEQAAQHKADIEE------RLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELE 1947
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1948 LGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAeervqKSLAAEEEAARQRKAALEE-VERLKAKVEEARRLRE 2026
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN-----EALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 41322919 2027 RAEQESAR-QLQLAQ 2040
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2157-2459 |
1.40e-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: 47.75 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2157 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQknlldeeLQRLKAEATEAARQRSQVEEELFSVRVQ 2236
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2237 MEELSKLKARIEAENRALILRDKDNTQRFLQEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2315
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2316 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLAEETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2392
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2393 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2459
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1702-2106 |
1.75e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.59 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1702 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1781
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1782 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1861
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1862 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGK 1941
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1942 AELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEA 2021
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2022 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAE 2101
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
....*
gi 41322919 2102 REAAQ 2106
Cdd:COG5278 513 AEAAL 517
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1426-1579 |
1.75e-04 |
|
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: 47.03 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1426 RQSSEAEIQAKARQAEA-AERSRLRIE-EEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1503
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1504 QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQ 1579
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1668-1831 |
1.81e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.56 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1668 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQREAAAA 1746
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1747 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEedAA 1825
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 41322919 1826 RQRAEA 1831
Cdd:COG2268 371 EAAAKP 376
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4275-4308 |
1.82e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|....
gi 41322919 4275 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4308
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1472-1606 |
1.92e-04 |
|
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: 46.67 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1472 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERR 1551
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1552 LRQ--AEVERARQvQVALETAQRSAEAELQSK----RASFAEKTAQLERSLQEEHVAVAQL 1606
Cdd:pfam09787 141 IKDreAEIEKLRN-QLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1351-1482 |
2.14e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 46.96 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ-AKAQAERE-AKELQQRMQEEVvrrEEAAVDAQQqkrsiQEELQQLRQS 1428
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlAAAQAQLDlAQRELERYQALY---KKGAVSQQE-----LDEARAALDA 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1429 SEAEIQAkARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARA 1482
Cdd:COG1566 160 AQAQLEA-AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1682-2052 |
2.15e-04 |
|
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: 47.33 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1682 QAVRQRELAEQELEKQRQ-------LAEGTAQQRLAAEQELIRLRAETEQgeqqrqlLEEELARLQREAAAATQkrqelE 1754
Cdd:pfam05701 32 QTVERRKLVELELEKVQEeipeykkQSEAAEAAKAQVLEELESTKRLIEE-------LKLNLERAQTEEAQAKQ-----D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1755 AELAKVRA-EMEVLLASKARAeeESRSTSEKSKQRLEAEAGRFRELAEEaarLRALAEEakRQRQLAEEDAARQRAEaER 1833
Cdd:pfam05701 100 SELAKLRVeEMEQGIADEASV--AAKAQLEVAKARHAAAVAELKSVKEE---LESLRKE--YASLVSERDIAIKRAE-EA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1834 VLAEKlaAIGEATRLKTEAEIALKEK---------EAENERLR----------------RLAEDEAfqrRRLEEQAA--- 1885
Cdd:pfam05701 172 VSASK--EIEKTVEELTIELIATKESlesahaahlEAEEHRIGaalareqdklnwekelKQAEEEL---QRLNQQLLsak 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1886 --QHKADIEERLAQLRKAS-----DSELERQKGLVEDTLRQRRQVEEEILALKASFE--KAAAGKAELELELGRIrsnAE 1956
Cdd:pfam05701 247 dlKSKLETASALLLDLKAElaaymESKLKEEADGEGNEKKTSTSIQAALASAKKELEevKANIEKAKDEVNCLRV---AA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1957 DTLRS---KEQAELEAARQRQ-LAAEEERRRREAEERVQKSLAAEEEAArqrKAALEEVERLKAKVEEARRLRERAE--- 2029
Cdd:pfam05701 324 ASLRSeleKEKAELASLRQREgMASIAVSSLEAELNRTKSEIALVQAKE---KEAREKMVELPKQLQQAAQEAEEAKsla 400
|
410 420 430
....*....|....*....|....*....|...
gi 41322919 2030 ----------QESARQLQLAQEAAQKRLQAEEK 2052
Cdd:pfam05701 401 qaareelrkaKEEAEQAKAAASTVESRLEAVLK 433
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2272-2621 |
2.34e-04 |
|
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: 47.66 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2272 KMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALaekmLKEKMQAvqeatrlKAEAELLQQQKELAQEQARRLQEDKE 2351
Cdd:pfam02463 166 RLKRKKKEALK--KLIEETENLAELIIDLEELKLQE----LKLKEQA-------KKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2352 QMAQQLAEEtqgFQRTLEAERQRQLEMSAEAErlklrvaemsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlV 2431
Cdd:pfam02463 233 KLNEERIDL---LQELLRDEQEEIESSKQEIE-----------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---E 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2432 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVqqeqlLQETQALQQSFLSEKDSLLQRERFIEQ 2511
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE-----LKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2512 EKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEA-----EEGVRRKQEELQQLEQQRRQQEEL 2586
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350
....*....|....*....|....*....|....*
gi 41322919 2587 LAEENQRLREQLQLLEEQHRAALAHSEEVTASQVA 2621
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2159-2432 |
2.36e-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: 46.84 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2159 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVR 2234
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2235 VQMEELSKL-----KARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE------DLAQ 2303
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdelraKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2304 QRALAEKMLKEKMQAVQEATRL----KAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMS 2379
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRqelqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 41322919 2380 AEAERLklrvaEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2432
Cdd:pfam13868 293 RELEKQ-----IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1348-1512 |
2.37e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1348 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQ 1427
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1428 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1507
Cdd:PRK12678 158 ADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRR 236
|
....*
gi 41322919 1508 QRKRQ 1512
Cdd:PRK12678 237 DARGD 241
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1348-1599 |
2.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1348 ERLAEQQRAEERERLAEVEaalekqrqlaeahaqakaQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQE---E 1421
Cdd:pfam10174 453 ERLKEQREREDRERLEELE------------------SLKKENKDLKEKvsaLQPELTEKESSLIDLKEHASSLASsglK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1422 LQQLRQSSEAEIQA-------------KARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQ 1488
Cdd:pfam10174 515 KDSKLKSLEIAVEQkkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1489 K---------------RQAQEEAERLR--RQVQDESQRKRQAEVELASRVK-AEAEAAREKQRA--LQALEELRLQAEEA 1548
Cdd:pfam10174 595 KndkdkkiaelesltlRQMKEQNKKVAniKHGQQEMKKKGAQLLEEARRREdNLADNSQQLQLEelMGALEKTRQELDAT 674
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1549 ERRLRQAEV--------------ERARQVQVALETAQRSAEAELQSKRASFA--EKTAQLERSLQEE 1599
Cdd:pfam10174 675 KARLSSTQQslaekdghltnlraERRKQLEEILEMKQEALLAAISEKDANIAllELSSSKKKKTQEE 741
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2158-2465 |
2.44e-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: 46.73 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2158 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQM 2237
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2238 EELSKLKARIEAENRAlilrdkDNTQRflqeeaekmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2317
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2318 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2397
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2398 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQE 2465
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1066-1282 |
2.52e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1066 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLRAHEEQLKEAQAVPATLPELEATKASLkklraqaEAQQPT 1145
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1146 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLGAWLQD 1225
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1226 ARRRQEQIQAMPladsQAVREQLRQEQ-ALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1282
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERIdALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
181-258 |
2.52e-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: 43.06 E-value: 2.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 181 DNFTSSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 258
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2284-2562 |
2.56e-04 |
|
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: 47.52 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2284 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLAEeTQG 2363
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLAA-ISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2364 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2443
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2444 DAE---RLREAIAE--LEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSllqrerfiEQEKAKLEQ 2518
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41322919 2519 LFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRR-QHEA 2562
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1407-1588 |
2.60e-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: 45.69 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1407 AAVDAQQQKRSIQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE 1486
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRL-EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1487 AQKRQA--QEEAERLRRQVQDESQRKRQAEvELASRVKAEAEAAREKQRALQA-LEELRLQAEEAERRLRQAEVERARQv 1563
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIESLKRRISDLE-DEILELMERIEELEEELAELEAeLAELEAELEEKKAELDEELAELEAE- 157
|
170 180
....*....|....*....|....*
gi 41322919 1564 qvaletaqrsaEAELQSKRASFAEK 1588
Cdd:COG1579 158 -----------LEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2099-2465 |
2.73e-04 |
|
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: 46.81 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2099 QAEREAAQSRRQVEEAERLKQSAEEQAQARAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTL 2178
Cdd:pfam07888 70 QWERQRRELESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2179 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRAL--IL 2256
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2257 RDKDNTQRFLQEEAEKMKQVAEEAARlSVAAQEAAR--LRQLAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQ 2334
Cdd:pfam07888 202 AQRDTQVLQLQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2335 QKELAQ------EQARRLQEDKEQMAQqlaeETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrk 2408
Cdd:pfam07888 278 RLQAAQltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER--- 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 2409 qaeeigEKLhRTELATQEKVTLVQTLEIQRQQSDhdaerLREAIAELEREKEKLQQE 2465
Cdd:pfam07888 342 ------EKL-EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3685-3720 |
2.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.97e-04
10 20 30
....*....|....*....|....*....|....*.
gi 41322919 3685 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVA 3720
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3425-3456 |
3.03e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.03e-04
10 20 30
....*....|....*....|....*....|..
gi 41322919 3425 QLLSAEKAVTGYRDPYSGSTISLFQAMQKGLV 3456
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1059-1925 |
3.15e-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: 47.35 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1059 AAPTLRsELELTLGKLEQVRSLSAIYLEKLKTISLVIRGT--------QGAEEVLRAHE-------EQLKEAQAVPATLP 1123
Cdd:TIGR00606 187 ALETLR-QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYEneldplkNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1124 ELEATKASLKKLRAQAEAQQPTFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRERVaqllerwqavlaqtdvrQREL 1202
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVDC-----------------QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1203 EQLGRQLRYYRESADPL----GAWLQDARRRQEQIQAMplaDSQAVREQLRQEQALLEE---IER-----HGEKVEECQR 1270
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELlveqGRLQLQADRHQEHIRAR---DSLIQSLATRLELDGFERgpfSERqiknfHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1271 FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTHYSELTTLT--SQYIKFISETLRRMEE 1346
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLEgsSDRILELDQELRKAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1347 EERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREaKELQQRMQEEVVRREEAAVDAQQQK---RSIQEELQ 1423
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLN-HHTTTRTQMEMLTKDKMDKDEQIRKiksRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1424 QLRQSSEAEIQAKARQAEAAERSRLRieEEIRVVRLQLEATERQRGGAEGELQALRARAEEAE-----AQKRQAQE-EAE 1497
Cdd:TIGR00606 565 LLGYFPNKKQLEDWLHSKSKEINQTR--DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdVCGSQDEEsDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1498 RLRRQVqdESQRKRQAEVELASRVKAE--AEAAREKQ-------RALQALEELRLQAEEAERRLRQA------------E 1556
Cdd:TIGR00606 643 RLKEEI--EKSSKQRAMLAGATAVYSQfiTQLTDENQsccpvcqRVFQTEAELQEFISDLQSKLRLApdklksteselkK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1557 VERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQL 1636
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1637 KANEALRlrlqaeEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLaaeQELI 1716
Cdd:TIGR00606 800 ELKDVER------KIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT---NELK 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1717 RLRAETEQGEQQRQLLEEELARLQREA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEESRSTSEKS 1785
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKV 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1786 KQRLEAEAGRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLaaigeaTRL 1848
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL------TLR 1024
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1849 KTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEE 1925
Cdd:TIGR00606 1025 KRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2179-2477 |
3.23e-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: 46.45 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2179 RQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRD 2258
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2259 KDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEatRLKAEAELLQQQKEL 2338
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAE--REEEREAEREEIEEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2339 AQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLH 2418
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2419 RTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQ 2477
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1691-1922 |
3.27e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1691 EQELeKQRQLAEGTAQ----QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAaaatqkRQELEAELAKVRA---- 1762
Cdd:PRK10929 29 TQEL-EQAKAAKTPAQaeivEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAEL------RQQLNNERDEPRSvppn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1763 ------EMEVLLAS-------------KARAEEESRSTSEKSKQRLEAEagrfRELAEEAARLRALAE----EAKRQRQL 1819
Cdd:PRK10929 102 mstdalEQEILQVSsqlleksrqaqqeQDRAREISDSLSQLPQQQTEAR----RQLNEIERRLQTLGTpntpLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1820 AEEDAARQRAEAERVLAEKLAAIG--EATRLKteAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1897
Cdd:PRK10929 178 LQAESAALKALVDELELAQLSANNrqELARLR--SELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD 255
|
250 260
....*....|....*....|....*
gi 41322919 1898 LRKASDSELERQKGLvEDTLRQRRQ 1922
Cdd:PRK10929 256 LPKSIVAQFKINREL-SQALNQQAQ 279
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1941-2620 |
3.29e-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: 47.27 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1941 KAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEE 2020
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2021 ARRLRERAEQESARQLQLAQEAAQ-KRLQAEEKAHAFAV----QQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEE 2095
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQerinRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2096 ARVQAEREAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAeKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAE 2175
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2176 QTLRQKAQVEQELTTLRlqleetdhqknllDEELQRLKAEATEAARQRSQVEEELFSvrvqMEELSKLKARIEAENRAli 2255
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-------------DLQGQLAHAKKQQELQQRYAELCAAAI----TCTAQCEKLEKIHLQES-- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2256 lrdkdntQRFLQEEAEKMKQVA----EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2331
Cdd:TIGR00618 465 -------AQSLKEREQQLQTKEqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2332 LQQQKELAQEQARrLQEDKEQmAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAE 2411
Cdd:TIGR00618 538 AQLETSEEDVYHQ-LTSERKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ---NITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2412 EigekLHRTELATQEKVTLVQTLEIQRQQSdhdaERLREAIAELEREKEKL----QQEAKLLQLKSEEMQTVQQEQLLQE 2487
Cdd:TIGR00618 613 E----QHALLRKLQPEQDLQDVRLHLQQCS----QELALKLTALHALQLTLtqerVREHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2488 TQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVR 2567
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2568 RKQEELQQLEQQRRQQEELLAEENQRLRE------QLQLLEEQHRAALAHSEEVTASQV 2620
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLreedthLLKTLEAEIGQEIPSDEDILNLQC 823
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2207-2415 |
3.43e-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: 46.38 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2207 EELQRLKAEATEAARQRSQVEEELfsvRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKM-----KQVAEEAA 2281
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2282 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLA 2358
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 2359 EETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2415
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3350-3384 |
3.45e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 3.45e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322919 3350 LLQGSGCLAGIYLEDTKEKVSIYEAMRRGLLRATT 3384
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2172-2339 |
3.75e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 46.38 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2172 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKNLLDEElqrlkAEATEAARQRSQVEEELFSVRVQMEELSKlkarieaen 2251
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALRS--------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2252 ralILRDKDNTQRFLQEEAEKM-KQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2329
Cdd:COG3524 243 ---YLSPNSPQVRQLRRRIAALeKQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 41322919 2330 EllQQQKELA 2339
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2174-2358 |
3.84e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2174 AEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAarQRSQVEEELFSVRVQME-ELSKLKARIEAENR 2252
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2253 ALilrdkdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2332
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|....*.
gi 41322919 2333 QQQKELAQEqarRLQEDKEQMAQQLA 2358
Cdd:COG3206 364 RELYESLLQ---RLEEARLAEALTVG 386
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1602-2057 |
3.87e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 46.93 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1602 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1681
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1682 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVR 1761
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1762 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1841
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1842 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR 1921
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1922 QVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAA 2001
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 2002 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFA 2057
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1258-1598 |
4.11e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1258 IERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaSPAKKPKVQSGSESVIQEY-VDLRTHYSELTTLTSQYIKF 1336
Cdd:COG5185 154 GEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI-SELKKAEPSGTVNSIKESEtGNLGSESTLLEKAKEIINIE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 ISETLRRMEEEERLAEQQRAEERERLAEVEAAL--EKQRQLAEAHAQAKAQAEREAKELQQrmQEEVVRREEAAVDAQQQ 1414
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLrlEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1415 KRSIQEELQQLRQSSEAEIQAKARQAEAAERSRlRIEEEIRVVRLQLEATERQRGGAEGElQALRARAEEAEAQKRQAQE 1494
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTA-EIEQGQESLTENLEAIKEEIENIVGE-VELSKSSEELDSFKDTIES 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1495 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElrlQAEEAERRLRQAEVERARQVQVA-------L 1567
Cdd:COG5185 389 TKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATS---SNEEVSKLLNELISELNKVMREAdeesqsrL 465
|
330 340 350
....*....|....*....|....*....|.
gi 41322919 1568 ETAQRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:COG5185 466 EEAYDEINRSVRSKKEDLNEELTQIESRVST 496
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1677-1824 |
4.13e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1677 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQREAAAATQKRQELEA 1755
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1756 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1824
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2241-2475 |
4.17e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2241 SKLKARIEAENRALILRdkdntQRFlqeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQ 2320
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK-----ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2321 EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV 2389
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2390 -AEMSRAQAR---AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREK-EKLQQ 2464
Cdd:PRK05035 583 aAAIARAKAKkaaQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKaRKAAQ 662
|
250
....*....|.
gi 41322919 2465 EAKLLQLKSEE 2475
Cdd:PRK05035 663 QQANAEPEEAE 673
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1341-1505 |
4.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1341 LRRMEEEERLAEQQRAEERERLAEVEAA--LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSI 1418
Cdd:pfam00038 136 LKKNHEEEVRELQAQVSDTQVNVEMDAArkLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1419 QEELQQLR---QSSEAEIQAKARQAEAAERSRLRIEEeirvvrlqleaterqRGgaEGELQALRARAEEAEAQKRQAQEE 1495
Cdd:pfam00038 216 KEEITELRrtiQSLEIELQSLKKQKASLERQLAETEE---------------RY--ELQLADYQELISELEAELQETRQE 278
|
170
....*....|
gi 41322919 1496 AERLRRQVQD 1505
Cdd:pfam00038 279 MARQLREYQE 288
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1345-1606 |
4.24e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1345 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAK-------ELQQRMQEEVVRREEAAVDAQQQKRS 1417
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqgglDEEEAFLDRTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1418 IQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEI--RVVRLQLEATE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1494
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1495 EAERLRRQV-----QDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQvqvALET 1569
Cdd:pfam02029 165 EAEEVPTENfakeeVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE---EEAE 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41322919 1570 AQRSAEAELQSKRASFAEKTAQ----LERSLQEEHVAVAQL 1606
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESEefekLRQKQQEAELELEEL 282
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1368-1539 |
4.34e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1368 ALEKQRQLA--------EAHAQAKAQA-EREAKEL--QQRMQEEVvrreeaavDAQQQKRsiqeELQQLRQSSEAEIQAK 1436
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARGRleRQKMHDKA--------KAEEQRT----KLLELQAESAAVESSG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1437 ARQAEA-AERSRLRIEEEirvvrlqleaterqrggAEGELQALRARAEEAEAQKrqaqeEAERLR-RQVQDESQRKRQAE 1514
Cdd:PTZ00491 716 QSRAEAlAEAEARLIEAE-----------------AEVEQAELRAKALRIEAEA-----ELEKLRkRQELELEYEQAQNE 773
|
170 180
....*....|....*....|....*
gi 41322919 1515 VELasrvkaeaeaarEKQRALQALE 1539
Cdd:PTZ00491 774 LEI------------AKAKELADIE 786
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1678-1837 |
4.43e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEA 1755
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1756 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1831
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 41322919 1832 ERVLAE 1837
Cdd:COG1842 207 EDELAA 212
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2729-2762 |
4.72e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|....
gi 41322919 2729 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2762
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1336-1398 |
4.77e-04 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 46.79 E-value: 4.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1336 FISETLRRmeEEERLAEQQraEERERLAEVEAALEKQRQLAEA-HAQAKAQAEREAKELQQRMQ 1398
Cdd:PLN02316 249 FLLEEKRR--ELEKLAKEE--AERERQAEEQRRREEEKAAMEAdRAQAKAEVEKRREKLQNLLK 308
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2175-2432 |
4.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2175 EQTLR---QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRS------QVEEELFSVRVQmeeLSKLKA 2245
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2246 RIEAENRALIlrdkdnTQRFLQEEAEkmkqvaeeaARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQEATrl 2325
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2326 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLAEETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2398
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 41322919 2399 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2432
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1343-1702 |
4.97e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1343 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEEL 1422
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQsseaEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1502
Cdd:COG4372 83 EELNE----QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1503 VQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKR 1582
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1583 ASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1662
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 41322919 1663 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE 1702
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1356-1598 |
5.26e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.98 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1356 AEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQeevvrreeaavDAQQQKRSIQEELQQLRQSSEAEIQA 1435
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEAAPKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1436 KARqaeaaersrlrieeeirvvRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEV 1515
Cdd:pfam12795 74 ILA-------------------SLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1516 ELASRVKAEAEAAREKQRALQA--------LEELRLQAEEAERR--LRQAEVERARQVQVALETAQRSAEAELQSKRASF 1585
Cdd:pfam12795 135 RLNGPAPPGEPLSEAQRWALQAelaalkaqIDMLEQELLSNNNRqdLLKARRDLLTLRIQRLEQQLQALQELLNEKRLQE 214
|
250
....*....|....
gi 41322919 1586 AEKT-AQLERSLQE 1598
Cdd:pfam12795 215 AEQAvAQTEQLAEE 228
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2206-2426 |
5.40e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.74 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2206 DEELQRLKAEATEAARQRSQveEELfsVRVQMEELSKLKARIEAENRALILRDKDNTqrflqEEAEKMKQVAEEAARLSV 2285
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEAR--KRL--VAKHGAEISKLEEENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2286 AAQEAARLRQLAEEDLAQQRALAekmlkekmqavqeATRLKAEAELLQQQKELAQEQARrlQEDKEQMAQQLAEETQGfq 2365
Cdd:PRK07735 75 AKQKREGTEEVTEEEKAKAKAKA-------------AAAAKAKAAALAKQKREGTEEVT--EEEKAAAKAKAAAAAKA-- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 2366 RTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQE 2426
Cdd:PRK07735 138 KAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE 198
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1359-1468 |
5.52e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 45.36 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1359 RERLAEVEAALEKQRQLAEAH-AQAKAQAEREAKELQQRMQEEVVRREEAavDAQQQKRSIQEELQQLRQSSEAEIQAKA 1437
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEkAIEAERAKAEAAEAEQELLREKQKEEEQ--MMEAQERSYQEHVKQLIEKMEAEREQLL 260
|
90 100 110
....*....|....*....|....*....|.
gi 41322919 1438 RQAEAAERSRLRIEEEIRVVRLQLEATERQR 1468
Cdd:pfam02841 261 AEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1695-1970 |
5.56e-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: 45.62 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1695 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASK 1771
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1772 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1831
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1832 ErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLRKASDS 1904
Cdd:pfam03148 159 D--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1905 ELERQKGLVEDTLRQRrqVEEeilalkasFEKAaagKAELELELGRIRSNAEDTlrSKEQAELEAA 1970
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1375-1581 |
5.79e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1375 LAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKarqaeaaersrlrieeei 1454
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1455 rvvrlQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrqaeveLASRVKAEAEAarekqRA 1534
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERAR-------LTGASGGDSLA-----SL 284
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 41322919 1535 LQALEELRLQAEEAERRLRQAeverarqvQVALETAQrsAEAELQSK 1581
Cdd:COG3524 285 LAEYERLELEREFAEKAYTSA--------LAALEQAR--IEAARQQR 321
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1021-1564 |
5.91e-04 |
|
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: 46.50 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1021 QRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQG 1100
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1101 AEEVLRAHEEQLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQE-------VGERLQQRHGERDVE 1173
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRI 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1174 VERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1253
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1254 LLEEIERHGEKVEECQR---FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLT 1330
Cdd:pfam02463 605 LAQLDKATLEADEDDKRakvVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1331 SQYIKFISETLRRMEEEERlaEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEA--- 1407
Cdd:pfam02463 685 AESELAKEEILRRQLEIKK--KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeek 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1408 ---AVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEE 1484
Cdd:pfam02463 763 eeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1485 AEAQKRQ--AQEEAERLrrqvQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1562
Cdd:pfam02463 843 KEEQKLEklAEEELERL----EEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
..
gi 41322919 1563 VQ 1564
Cdd:pfam02463 919 IE 920
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3760-3796 |
5.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.97e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 3760 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPTEEA 3796
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2157-2321 |
6.04e-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: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2157 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQ 2236
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2237 mEELSKLKARIEAENRALILRDKDnTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2316
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 41322919 2317 QAVQE 2321
Cdd:COG1579 167 ELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2273-2472 |
6.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2273 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2351
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2352 ----QMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2427
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41322919 2428 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLK 2472
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3131-3167 |
7.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.13e-04
10 20 30
....*....|....*....|....*....|....*..
gi 41322919 3131 LRLLDAQLSTGGIVDPSKSHRVPLDVACARGCLDEET 3167
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3057-3091 |
7.20e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.20e-04
10 20 30
....*....|....*....|....*....|....*
gi 41322919 3057 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPEF 3091
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1381-1596 |
7.41e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1381 QAKAQAEREAKELQQR---MQEEVVRREEAAVDAQQQKRSIQEELQQLRQ------SSEAEIQAK--------ARQAEAA 1443
Cdd:PRK11637 54 QDIAAKEKSVRQQQQQrasLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelnASIAKLEQQqaaqerllAAQLDAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1444 ERsrlriEEEIRVVRLQLEATERQRG------------GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1511
Cdd:PRK11637 134 FR-----QGEHTGLQLILSGEESQRGerilayfgylnqARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1512 QAEVELASRVK--AEAEAAREKQRalQALEELRLQaeeaERRLR----QAEVE-RARQVQVALEtAQRSAEAELQSKRAS 1584
Cdd:PRK11637 209 KLEQARNERKKtlTGLESSLQKDQ--QQLSELRAN----ESRLRdsiaRAEREaKARAEREARE-AARVRDKQKQAKRKG 281
|
250
....*....|..
gi 41322919 1585 FAEKTAQLERSL 1596
Cdd:PRK11637 282 STYKPTESERSL 293
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
32-147 |
7.58e-04 |
|
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: 42.28 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 32 WAQDEQDERdrvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQN 102
Cdd:cd21330 5 WSSIEGETR---EERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLEN 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41322919 103 VQIALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 147
Cdd:cd21330 78 CNYAVELGKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2159-2359 |
7.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2159 QKQAADAEMEKHKKFAEQT--LRQKAQVEQElttlRLQLEEtdhQKNLLDEELQRLKAEATEAARQRSQVEEElfsVRVQ 2236
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAeeLQQKQAAEQE----RLKQLE---KERLAAQEQKKQAEEAAKQAALKQKQAEE---AAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2237 MEELSKLKAriEAENRALilrdkdntqrflqeeAEKMKQVAEEAARLSVAAQEAarlrQLAEEdlAQQRALAEkmlkEKM 2316
Cdd:PRK09510 141 AAAAAKAKA--EAEAKRA---------------AAAAKKAAAEAKKKAEAEAAK----KAAAE--AKKKAEAE----AAA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 41322919 2317 QAVQEAtRLKAEAELLQQQKELAQEQARRlqEDKEQMAQQLAE 2359
Cdd:PRK09510 194 KAAAEA-KKKAEAEAKKKAAAEAKKKAAA--EAKAAAAKAAAE 233
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1428-1562 |
7.95e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.67 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1428 SSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1507
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1508 QRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQ 1562
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1678-1974 |
8.40e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQElekQRQLAEGTAQqrlaaeqelIRLRAETEQGEQQRQLLEE--ELARLQREAAAATQKRQ-ELE 1754
Cdd:COG5185 279 RLNENANNLIKQFENT---KEKIAEYTKS---------IDIKKATESLEEQLAAAEAeqELEESKRETETGIQNLTaEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1755 AELAKVRAEMEVLLASKARAEEESRstSEKSKQRLEAEAGRFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERV 1834
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVE--LSKSSEELDSFKDTIESTKES---LDEIPQNQRGYAQEILATLEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1835 LAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA-----QHKADIEERLAQLRKASDS---EL 1906
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEInrsvrSKKEDLNEELTQIESRVSTlkaTL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1907 ERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNA--EDTLRSKEQAELEAARQRQ 1974
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELiqASNAKTDGQAANLRTAVID 571
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1096-1547 |
8.61e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1096 RGTQGAEEVLRAHEEQLKEAQAVPA----------------TLPELEATKASLKKLRAQAEAQQP-------TFDALrdE 1152
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALNEmrqrykektqqladvkTICEQEARIKDLEAQRAQLQAGQPcplcgstSHPAV--E 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1153 LRGAQEVGERlQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQ 1232
Cdd:PRK10246 519 AYQALEPGVN-QSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDD 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1233 IQamPLADSQAVRE----QLRQEQALLEEIERHGEKVEEcqrfakqyinaikdYELQLVTYKAQLEPVASPAKKPKVQSG 1308
Cdd:PRK10246 598 IQ--PWLDAQEEHErqlrLLSQRHELQGQIAAHNQQIIQ--------------YQQQIEQRQQQLLTALAGYALTLPQED 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1309 SESviqeyvdlrthySELTTltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAER 1388
Cdd:PRK10246 662 EEA------------SWLAT----------------RQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEET 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 EAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1468
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1469 GGAegelQALRARAEEAEAQKRQAQEE-------AERLRRQVQDESQRKRQ---AEVELASRVKAEAEAAREKQRALQAL 1538
Cdd:PRK10246 794 QQA----QTLVTQTAQALAQHQQHRPDgldltvtVEQIQQELAQLAQQLREnttRQGEIRQQLKQDADNRQQQQALMQQI 869
|
....*....
gi 41322919 1539 EELRLQAEE 1547
Cdd:PRK10246 870 AQATQQVED 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2161-2414 |
8.67e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2161 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKA-----EATEAARQRSQVEEELFSVRV 2235
Cdd:PRK04863 431 GLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevSRSEAWDVARELLRRLREQRH 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2236 QMEELSKLKARI-EAENRaliLRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKE 2314
Cdd:PRK04863 511 LAEQLQQLRMRLsELEQR---LRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2315 KMQAVQEATRLKAEAELLQQqkelAQEQARRLQE---DKEQMAQQLaeeTQGFQRTLEAERQRQLEMSAEAERLKLRVAE 2391
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLA----AQDALARLREqsgEEFEDSQDV---TEYMQQLLERERELTVERDELAARKQALDEE 660
|
250 260
....*....|....*....|...
gi 41322919 2392 MSRAQARAEEDAQRFRKQAEEIG 2414
Cdd:PRK04863 661 IERLSQPGGSEDPRLNALAERFG 683
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1678-1871 |
9.03e-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: 44.91 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAEL 1757
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1758 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1837
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 41322919 1838 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1871
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1485-1933 |
9.64e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.52 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1485 AEAQKRQAQEEAERLRRQVQDES-QRKRQAEVElASRVKAEAEAAREKQRALQALEElrlqAEEAERRLRQAEVERA-RQ 1562
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSgVSSEVAEEE-KEATKDAAEAKAQLPKSEQEKEK----ALEEVLKEAISKAESAtAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1563 VQVALETAQRSAEAELQSKRASFA-EKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1641
Cdd:pfam09731 148 AKEAKDDAIQAVKAHTDSLKEASDtAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1642 LRLRLQAEEVAQQKSLAQAEAEKQkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQqrLAAEQELIRLRAE 1721
Cdd:pfam09731 228 LDNVEEKVEKAQSLAKLVDQYKEL------------VASERIVFQQELVSIFPDIIPVLKEDNLL--SNDDLNSLIAHAH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1722 TEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASkaraeeesrstsEKSKQRLEAEagrfrelae 1801
Cdd:pfam09731 294 REIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAA------------DEAQLRLEFE--------- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1802 eaarlRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR-RRL 1880
Cdd:pfam09731 353 -----REREEIRESYEEKLRTELERQAEAHEEHLKDVLVE--QEIELQREFLQDIKEKVEEERAGRLLKLNELLANlKGL 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 1881 EEQAAQHKADIEERLA--QLRKASDSelerqkglVEDTLR------QRRQVEEEILALKAS 1933
Cdd:pfam09731 426 EKATSSHSEVEDENRKaqQLWLAVEA--------LRSTLEdgsadsRPRPLVRELKALKEL 478
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2291-2466 |
9.72e-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: 45.38 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2291 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLAEETQG 2363
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2364 FQRTLEAERQRQLemsaeAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2443
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 41322919 2444 DAERLREAIAELEREKEKLQQEA 2466
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1339-1443 |
9.84e-04 |
|
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: 43.93 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQ-------AEREAKELQQRMQEEVVRREEA-- 1407
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKqkaaesaSKSLAKPERKVSQEEAKEVLQEwe 148
|
90 100 110
....*....|....*....|....*....|....*..
gi 41322919 1408 -AVDAQQQKRsiQEELQQLRQSSEAEIQAKARQAEAA 1443
Cdd:pfam13904 149 rKKLEQQQRK--REEEQREQLKKEEEEQERKQLAEKA 183
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2159-2367 |
1.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2159 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqknlLDEELQRLKAEATEAAR--QRSQVEEELFSVRVQ 2236
Cdd:COG3883 38 ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2237 MEELSKLKARIEAENRaLILRDKD--NTQRFLQEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2313
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKaELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2314 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRT 2367
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2260-2429 |
1.01e-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: 44.99 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2260 DNTQRFLQEEAEKMKQVAEEAarlSVAAQEAARLRQlaEEDLAQqrALAEKMLKEKMQAVQEATRLKAEAElLQQQKEla 2339
Cdd:pfam05262 202 DLKERESQEDAKRAQQLKEEL---DKKQIDADKAQQ--KADFAQ--DNADKQRDEVRQKQQEAKNLPKPAD-TSSPKE-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2340 qeqARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRkqaEEIGEKLHR 2419
Cdd:pfam05262 272 ---DKQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR---EPVAEDLQK 339
|
170
....*....|
gi 41322919 2420 TELATQEKVT 2429
Cdd:pfam05262 340 TKPQVEAQPT 349
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2112-2433 |
1.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2112 EEAERLKQSAEEQAQARAQAQAAAEKLRkeaeqeAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLrqkaqvEQELTTL 2191
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIA------EYTKSIDIKKATESLEEQLAAAEAEQELEESKR------ETETGIQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2192 RLQlEETDHQKNLLDEELQRLKAEATE--AARQRSQVEEELFSVRVQMEElskLKARIEAENRALilrdKDNTQRFLQEE 2269
Cdd:COG5185 340 NLT-AEIEQGQESLTENLEAIKEEIENivGEVELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2270 AEKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQ 2347
Cdd:COG5185 412 EDTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLN 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2348 EDKEQMAQQLAEETQGFQrTLEAERQRQLE-----MSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2422
Cdd:COG5185 485 EELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAA 563
|
330
....*....|.
gi 41322919 2423 ATQEKVTLVQT 2433
Cdd:COG5185 564 NLRTAVIDELT 574
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1254-1747 |
1.07e-03 |
|
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: 45.48 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1254 LLEEIERHGEKVEECQRFAKQYI---NAIKDY---ELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELT 1327
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLkelIEKKDHltkELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1328 TLTSQYIKFISE---TLRRMEEEERlAEQQRAEERE-RLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvr 1403
Cdd:pfam05483 342 KAKAAHSFVVTEfeaTTCSLEELLR-TEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAED--- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1404 reEAAVDAQQQKRSIQEELQQ-------LRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-------------- 1462
Cdd:pfam05483 418 --EKLLDEKKQFEKIAEELKGkeqelifLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEkeklknieltahcd 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1463 --ATERQRGGAEGELQALRARAEEAEAQKRQAQEEA--------ERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1532
Cdd:pfam05483 496 klLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlkqienlEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1533 RALQ---------------ALEELRLQAEEAERRLRQAEVE-RARQVQVALETAQRSA--------EAELQSKRASFAEK 1588
Cdd:pfam05483 576 RSIEyevlkkekqmkilenKCNNLKKQIENKNKNIEELHQEnKALKKKGSAENKQLNAyeikvnklELELASAKQKFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1589 TAQLERSLQEEHVAVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEE 1668
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKLLEE---------------------VEKAKAIADEAVKLQKEIDKRCQHK-----------IA 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1669 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAT 1747
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1368-1881 |
1.07e-03 |
|
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: 45.12 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1368 ALEKQRQLAEAHAQA---KAQAEREAKELQQrMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEA---EIQAKARQAE 1441
Cdd:pfam05557 22 ELEHKRARIELEKKAsalKRQLDRESDRNQE-LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAlnkKLNEKESQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1442 AAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ---DESQRKRQAEVELA 1518
Cdd:pfam05557 101 DAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSslaEAEQRIKELEFEIQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1519 SRV-------KAEAEAAR--EKQRALQALEE--------------LRLQAEEAERRLRQaeVERARQVQVALETAQRSAE 1575
Cdd:pfam05557 181 SQEqdseivkNSKSELARipELEKELERLREhnkhlnenienkllLKEEVEDLKRKLER--EEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1576 AELQSkrasfAEKTAQ---------------LERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQ 1635
Cdd:pfam05557 259 QELQS-----WVKLAQdtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLkkiedLNKK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1636 LKANEALRLRLQAEEVAQQKS-------LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA--- 1705
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKErdgyraiLESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELggy 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1706 -QQRLAAEQELIRLRAETEQGEQQRQllEEELARLQREAaaatqkrQELEAELAKVRAEMEVLLASKARAEEESRSTSEK 1784
Cdd:pfam05557 414 kQQAQTLERELQALRQQESLADPSYS--KEEVDSLRRKL-------ETLELERQRLREQKNELEMELERRCLQGDYDPKK 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1785 SK---QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervlAEKLAAIGEATRLKTEAEIA--LKEK 1859
Cdd:pfam05557 485 TKvlhLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD------------LEQVLRLPETTSTMNFKEVLdlRKEL 552
|
570 580
....*....|....*....|..
gi 41322919 1860 EAENERLRRLaeDEAFQRRRLE 1881
Cdd:pfam05557 553 ESAELKNQRL--KEVFQAKIQE 572
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1342-1598 |
1.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1342 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAEREakelqqrmqeevvrREEAAVDAQQQKRSIQE 1420
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1421 ELQqLRQSSEAEIQAKARQAEAAERSRLRIEEEIrvvrlqleaterqrggaegelQALRaraEEAEAQKRQAQEEAERLR 1500
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARVDLEAKI---------------------ESLK---EELAFLKKNHEEEVRELQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1501 RQVQDESqrkRQAEV------ELAS-----RVKAEAEAAREKQRA----LQALEELRLQAEEAERRLRQAEVERA---RQ 1562
Cdd:pfam00038 149 AQVSDTQ---VNVEMdaarklDLTSalaeiRAQYEEIAAKNREEAeewyQSKLEELQQAAARNGDALRSAKEEITelrRT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 41322919 1563 VQ-------------VALETAQRSAEAELQSKRASFAEKTAQLERSLQE 1598
Cdd:pfam00038 226 IQsleielqslkkqkASLERQLAETEERYELQLADYQELISELEAELQE 274
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1337-1442 |
1.12e-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: 44.21 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAK------AQ--AEREAKELQQRMQEEV-V 1402
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEvakiqmQQkiMEKEAEKKISEIEDEMhL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41322919 1403 RREEAAVDAQQQKRSIQEELQQLRQSSE----AEIQAKARQAEA 1442
Cdd:cd03406 237 AREKARADAEYYRALREAEANKLKLTPEylelKKYQAIANNTKI 280
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3685-3723 |
1.12e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|....*....
gi 41322919 3685 YLYGTGSVAGVYLPGSRQTLSIYQALKKGLLSAEVARLL 3723
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1359-1564 |
1.14e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 45.28 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1359 RERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEelqQLRQSSEAEIQAKAR 1438
Cdd:PRK12678 56 KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAE---AASAPEAAQARERRE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1439 QAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEgelqaLRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAEVELA 1518
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEE-----EERDERRRRGDREDRQAEAERGERG--RREERGRDGDDRDR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 41322919 1519 SRVKAEAEAAREKQRALQALE-ELRLQAEEAERRLRQAEVERARQVQ 1564
Cdd:PRK12678 206 RDRREQGDRREERGRRDGGDRrGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1705-2002 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1705 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1776
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1777 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1852
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1853 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKA 1932
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1933 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAAR 2002
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2264-2476 |
1.30e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2264 RFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ-EATRLKA---EAELLQQQKELA 2339
Cdd:PRK10929 123 RQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQaESAALKAlvdELELAQLSANNR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2340 QEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQARA----EEDAQRFRKQAEEIG 2414
Cdd:PRK10929 203 QELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQAQRMD 282
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2415 EKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIAELErEKEKLQQ------EAKLLQLKSEEM 2476
Cdd:PRK10929 283 LIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLP-EMPKPQQldtemaQLRVQRLRYEDL 355
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2269-2404 |
1.34e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2269 EAEKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2344
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2345 RLQEDKEQmaQQLAEetqgfqrtLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2404
Cdd:PTZ00491 761 QELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1706-1968 |
1.34e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1706 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKS 1785
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK----EL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1786 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQR--------------AEAERVLAEKLAaigeatRLKTE 1851
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGG--SIDKLRKEierlewrqqtevlsPEEEKELVEKIK------ELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1852 AEIALKEKEAENERLRRLAEDEAFQrrrleEQAAQHKADIEERLAQLRKASDS------ELERQKGLVEDTLRQRRQVEE 1925
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELR-----KEAEEIHKKIKELAEEAQELHEEmielykEADELRKEADELHKEIVEAQE 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41322919 1926 EILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1968
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2172-2626 |
1.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2172 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAEN 2251
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2252 RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2331
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2332 LQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2411
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2412 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQAL 2491
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2492 QQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQE 2571
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2572 ELQQLEQQRRQQEELLAEENQRLREQLQLLEEQHRAALAHSEEVTASQVAATKTL 2626
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1681-1824 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1761 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1824
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1441-1557 |
1.41e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1441 EAAerSRLRIE-----EEIRVVRLQLEATERQRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQdesqrkrqAE 1514
Cdd:COG0542 397 EAA--ARVRMEidskpEELDELERRLEQLEIEKEALKKEQdEASFERLAELRDELAELEEELEALKARWE--------AE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41322919 1515 VELASRV---KAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1557
Cdd:COG0542 467 KELIEEIqelKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
1369-1579 |
1.42e-03 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 44.47 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1369 LEKQRQLAEAHAQAKAqAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKaRQAEAAERSRL 1448
Cdd:pfam08017 31 LERRQRDAENRSQGNV-LERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLER-RQRDAENRSQG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1449 RIEEEIR---VVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEA 1525
Cdd:pfam08017 109 NVLERRQrdaENKSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENKSQG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1526 EAAREKQRAlqalEELRLQAEEAERRLRQAEVERARQVqvaLETAQRSAEAELQ 1579
Cdd:pfam08017 189 NVLERRQRD----AENRSQGNVLERRQRDAENRSQGNV---LERRQRDAENRSQ 235
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1990-2425 |
1.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1990 VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR--QLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQq 2067
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEER- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2068 tlqqeqsvLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEA-ERLKQSAEEQAQARAQAQAAAEKLRKEAEQEA 2146
Cdd:COG4717 155 --------LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2147 ARRAQAeqaalrQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQV 2226
Cdd:COG4717 227 EELEQL------ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2227 EEELFSVRVQmEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEA--ARLRQLAEEDLAQQ 2304
Cdd:COG4717 301 GKEAEELQAL-PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2305 RALAEKMLKEKMQAVQEATRLKAEAELLQQQkeLAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAER 2384
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQ--LEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 41322919 2385 LKLRVAEMSRAQ--ARAEEDAQRFRKQAEEIGEKLHRTELATQ 2425
Cdd:COG4717 458 LEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALE 500
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
38-141 |
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 41322919 38 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 95
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41322919 96 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 141
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1351-1544 |
1.61e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1351 AEQQRAEERERlaEVEAALEKQRqlaeahAQAKAQAEREAKELQQrmqeevVRREEAAVDAQQQKRsiqeelqqlrqsSE 1430
Cdd:PTZ00491 667 AARHQAELLEQ--EARGRLERQK------MHDKAKAEEQRTKLLE------LQAESAAVESSGQSR------------AE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 AEIQAKARQAEAaersrlriEEEIRVVRLQLEAterQRGGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQr 1509
Cdd:PTZ00491 721 ALAEAEARLIEA--------EAEVEQAELRAKA---LRIEAEAELEKLRKRQElELEYEQAQNELEIAKAKELADIEAT- 788
|
170 180 190
....*....|....*....|....*....|....*..
gi 41322919 1510 KRQAEVELASR--VKAEAEAAREKQRALqaLEELRLQ 1544
Cdd:PTZ00491 789 KFERIVEALGRetLIAIARAGPELQAKL--LGGLGLK 823
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
964-1389 |
1.67e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 964 HYQQLLQSLEQGAQEESRCQRCISELKDIRLQLEACE-----TRTVHRLRLPLDKEPAR--ECAQRIAEQQKAQAEVEGL 1036
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERleELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1037 GKGVARLSAEAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRGTQGAEEVLR------AHEE 1110
Cdd:COG4717 169 EAELAELQEELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEneleaaALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1111 QLKEAQAVPATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA 1190
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1191 VLAQTDVRQREleqlgrQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQAL--LEEIERHGEKVEEC 1268
Cdd:COG4717 324 LLAALGLPPDL------SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVedEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1269 QRFAKQYINAikdyelqlvtyKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISET---LRRME 1345
Cdd:COG4717 398 QELKEELEEL-----------EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLE 466
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 41322919 1346 EEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAERE 1389
Cdd:COG4717 467 EDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1686-2371 |
1.70e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1686 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR---QLLEEELARLQREAAAATQKRQELEAELAKVR- 1761
Cdd:PRK10246 232 EKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEKaqpQLAALSLAQPARQLRPHWERIQEQSAALAHTRq 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1762 --AEMEVLLASKARAEEESRSTSEKSKQRLEAEAG----------RFRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1829
Cdd:PRK10246 312 qiEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslntwlaehdRFRQWNNELAGWRAQFSQQTSDRE--QLRQWQQQL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1830 EAERvlaEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLaedeafqRRRLEEQAAQHkADIEERLAQLrKASDSELERQ 1909
Cdd:PRK10246 390 THAE---QKLNALPAITLTLTADEVA--AALAQHAEQRPL-------RQRLVALHGQI-VPQQKRLAQL-QVAIQNVTQE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1910 KGLVEDTLRQRRQveeeilALKASFEKAAAGKAELELElGRIRSNAEdtlrskEQAELEAARQRQLAAEEERRRreaeer 1989
Cdd:PRK10246 456 QTQRNAALNEMRQ------RYKEKTQQLADVKTICEQE-ARIKDLEA------QRAQLQAGQPCPLCGSTSHPA------ 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1990 VQKSLAAEEEAARQRKAALE-EVERLKakvEEARRLRERAEQeSARQLQLAQEAAQkRLQAEEKAHAFAVQQKEQELQQT 2068
Cdd:PRK10246 517 VEAYQALEPGVNQSRLDALEkEVKKLG---EEGAALRGQLDA-LTKQLQRDESEAQ-SLRQEEQALTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2069 LQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQsrRQVEEAErlKQSAEEQAQARAQAQAAAEKLRKEAEQEAAR 2148
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHN--QQIIQYQ--QQIEQRQQQLLTALAGYALTLPQEDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2149 RAqaeqaalrqkQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--ATEAARQRSQ 2225
Cdd:PRK10246 668 AT----------RQQEAQSWQQRQNELTALQNRiQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQclSLHSQLQTLQ 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2226 VEEELFSVRVQmeelsKLKARIEAENRALILRDKDNTQRFLQEEaEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQR 2305
Cdd:PRK10246 738 QQDVLEAQRLQ-----KAQAQFDTALQASVFDDQQAFLAALLDE-ETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQ 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 2306 ALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAE 2371
Cdd:PRK10246 812 QHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2255-2462 |
1.74e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2255 ILRDKDNTQRFLQEEAEKmKQVAEEAARLSVAAQEAARLRQLAE------EDLAQQRALAEKMLKEKMQAVQEATRLKAE 2328
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-KEEKDLHERLNGLESELAELDEEIEryeeqrEQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2329 AELLQQQKELAQ---EQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQR 2405
Cdd:PRK02224 260 IEDLRETIAETErerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 2406 FRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL 2462
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1631-1841 |
1.75e-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: 43.98 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1631 LERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAvrQRELAEQELEKQRQLAegTAQQRLA 1710
Cdd:COG4942 43 LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLR--ALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1711 AEQELIRLRAET-EQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1789
Cdd:COG4942 119 QPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1790 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1841
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2216-2641 |
1.78e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 44.60 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2216 ATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQ 2295
Cdd:COG5281 2 AALAAAAALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2296 LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKElaQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQ 2375
Cdd:COG5281 82 AALAEDAAAAAAAAEAALAALAAAALALAAAALAEAALAAAA--AAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2376 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAEL 2455
Cdd:COG5281 160 AAAAAAAAAAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2456 EREKEKLQQEAKLLQLKSEEmQTVQQEQLLQETQALQQSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAQQLREEQQ 2535
Cdd:COG5281 240 ASAAAQALAALAAAAAAAAL-ALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2536 RQQQQMEQERQRLVASMEEARRRQHEAEEGVRRKQEELQQLEQQRRQQEELLAEENQRLREQL--QLLEEQHRAALAHSE 2613
Cdd:COG5281 319 AAAQALRAAAQALAALAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWaaGAKAALAEYADSATN 398
|
410 420
....*....|....*....|....*...
gi 41322919 2614 EVTASQVAATKTLPNGRDALDGPAAEAE 2641
Cdd:COG5281 399 VAAQVAQAATSAFSGLTDALAGAVTTGK 426
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1686-2464 |
1.80e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1686 QRELAEQE-----LEKQRQLAE---GTAQQRLAAEQELIRLRAE----TEQGEQQRQLLE---EELARLQREAAAATQKR 1750
Cdd:PRK04863 313 ARELAELNeaesdLEQDYQAASdhlNLVQTALRQQEKIERYQADleelEERLEEQNEVVEeadEQQEENEARAEAAEEEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1751 QELEAELAKVRAEMEVLlASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQ-----RQLAEEDAA 1825
Cdd:PRK04863 393 DELKSQLADYQQALDVQ-QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsleQKLSVAQAA 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1826 RQRAEAERVLAEKLAaiGEATRlkTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASD 1903
Cdd:PRK04863 472 HSQFEQAYQLVRKIA--GEVSR--SEAWDVARELLRRLREQRHLAEQLQQLRMRLSelEQRLRQQQRAERLLAEFCKRLG 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1904 SELERqkglvEDTLRQ-RRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEdTLRSKEQAELEA----ARQRQLAAE 1978
Cdd:PRK04863 548 KNLDD-----EDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQ-RLAARAPAWLAAqdalARLREQSGE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1979 EERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKakvEEARRLRERAEQESARQLQLA-----------------QE 2041
Cdd:PRK04863 622 EFEDSQDVTEYMQQLLERERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALAerfggvllseiyddvslED 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2042 AAQKRLQAEEKAHAFAVQQKEQELQQTLQqeqsvLDQLRGEAEAARRAAEEAEEARVQA-EREAAQSRRQVEEAERLKQS 2120
Cdd:PRK04863 699 APYFSALYGPARHAIVVPDLSDAAEQLAG-----LEDCPEDLYLIEGDPDSFDDSVFSVeELEKAVVVKIADRQWRYSRF 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2121 AEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE---QAALRQKQAADAEMEKHKKFAEQtlrqkAQVEQELTTLRLQLEE 2197
Cdd:PRK04863 774 PEVPLFGRAAREKRIEQLRAEREELAERYATLSfdvQKLQRLHQAFSRFIGSHLAVAFE-----ADPEAELRQLNRRRVE 848
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2198 TDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEElsKLKARIEaENRALILRDKDNtQRFLQEEAEKMKQVA 2277
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE--TLADRVE-EIREQLDEAEEA-KRFVQQHGNALAQLE 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2278 EEAARLSVAAQEAARLRQLAEEDLAQQRALAEKM--LKEKMQ-----AVQEATRLKAEA----ELLQQQKELAQEQARRL 2346
Cdd:PRK04863 925 PIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAfaLTEVVQrrahfSYEDAAEMLAKNsdlnEKLRQRLEQAEQERTRA 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2347 QEDKEQMAQQLAEETQgFQRTLEAERQRQLEMSAEAERlklrvaEMSRAQARAEEDA-QRFRKQAEEIGEKLHRTELATQ 2425
Cdd:PRK04863 1005 REQLRQAQAQLAQYNQ-VLASLKSSYDAKRQMLQELKQ------ELQDLGVPADSGAeERARARRDELHARLSANRSRRN 1077
|
810 820 830
....*....|....*....|....*....|....*....
gi 41322919 2426 EkvtLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQ 2464
Cdd:PRK04863 1078 Q---LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1399-1740 |
1.81e-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: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1399 EEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKAR------QAEAAERSRLRIEEEIRVvrLQLEATERQRGGAE 1472
Cdd:COG3206 97 ERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNvieisyTSPDPELAAAVANALAEA--YLEQNLELRREEAR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaevelasrVKAEAEAAREKQRALQA-LEELRLQAEEAERR 1551
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-------------LSEEAKLLLQQLSELESqLAEARAELAEAEAR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1552 LRQAEVERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAerraqqqaeaerareeaerel 1631
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI--------------------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1632 erwqlkanEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgKAEEQAVRQRElaeQELEKQRQLAEGTAQQRLAA 1711
Cdd:COG3206 301 --------AALRAQLQQEAQRILASL--------------------EAELEALQARE---ASLQAQLAQLEARLAELPEL 349
|
330 340
....*....|....*....|....*....
gi 41322919 1712 EQELIRLRAETeqgEQQRQLLEEELARLQ 1740
Cdd:COG3206 350 EAELRRLEREV---EVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1729-2041 |
1.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1729 RQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESrstsEKSKQRLEAEAGRFRELAEEAARLRA 1808
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1809 LAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1888
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1889 ADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1968
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1969 AARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQE 2041
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1471-1580 |
1.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1471 AEGELQALRARAE-EAEAQKR----QAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEElRLQA 1545
Cdd:PRK12704 36 AEEEAKRILEEAKkEAEAIKKeallEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-ELEK 114
|
90 100 110
....*....|....*....|....*....|....*
gi 41322919 1546 EEAERRLRQAEVERARQVqvaLETAQRSAEAELQS 1580
Cdd:PRK12704 115 KEKELEQKQQELEKKEEE---LEELIEEQLQELER 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2371-2695 |
1.84e-03 |
|
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: 44.66 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2371 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2431
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2432 QTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDSLLQRERFIEQ 2511
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2512 EKAKLEQLfQDEVAKAQQLREEQQRQQQQMEQERQRLVASMEEARRRQHEAEEGVRRkqeelqqleqQRRQQEELLAEEN 2591
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----------LRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2592 QrLREQLQLLEEQ-HRAALAHSEEVTASQVAATKTLPNGRDALDGPAAEAEPEHSFDGLRRKVSAQRLQEAGILSAEELQ 2670
Cdd:TIGR02168 397 S-LNNEIERLEARlERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340
....*....|....*....|....*
gi 41322919 2671 RLAQGHTTVDELARREDVRHYLQGR 2695
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQEN 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1738-1970 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1738 RLQREAAAATQKRQELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSKQRLEaeagRFRELAEEAARLRALAEEAKR 1815
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQ----QLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1816 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkekeaeneRLRRLAEDEAFQRRRLEEQaaqhKADIEERL 1895
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELA---------ELSARYTPNHPDVIALRAQ----IAALRAQL 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1896 AQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAA 1970
Cdd:COG3206 308 QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1998-2522 |
1.86e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1998 EEAARQRKAALEEVERLKAKVEEARRLRERAEQ--ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSV 2075
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2076 LDQLRGEAEAARRAAEEAEEARVQAEREAAQS-RRQVEEAER----LKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRA 2150
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2151 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAE--------------- 2215
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlaealgldeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2216 ------ATEAARQRSQVEEEL----FSVRVQMEELSKLKARIEAENRALILRdkdnTQRFLQEEAEKMKQVAEE---AAR 2282
Cdd:COG4913 464 gelievRPEEERWRGAIERVLggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2283 LSVAAQEAAR-LRQL-----------AEEDLAQ-QRAL-AEKMLKEKMQAVQEATRLKAEAELL-----QQQKELAQEQA 2343
Cdd:COG4913 540 LDFKPHPFRAwLEAElgrrfdyvcvdSPEELRRhPRAItRAGQVKGNGTRHEKDDRRRIRSRYVlgfdnRAKLAALEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2344 RRLQEDKEQMAQQLAEetqgfqrtLEAERQRQLEMSAEAERLklrvaemsRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2423
Cdd:COG4913 620 AELEEELAEAEERLEA--------LEAELDALQERREALQRL--------AEYSWDEIDVASAEREIAELEAELERLDAS 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2424 TQEkvtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2503
Cdd:COG4913 684 SDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL 759
|
570 580
....*....|....*....|....*....
gi 41322919 2504 QRERF----------IEQEKAKLEQLFQD 2522
Cdd:COG4913 760 GDAVErelrenleerIDALRARLNRAEEE 788
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1688-1862 |
1.86e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.93 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1688 ELAEQELEKQRQLAEGTAqqrLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAE-LAKVRAEMEV 1766
Cdd:PHA03247 1552 ERVDQSPVKDTAYAEYVA---FVARRDLAEAKDALVRAKQQRAEATDRVTAALREALAAHERRAQSEAEsLANLKTLLRV 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1767 --LLASKARAEEESRSTSEKSKQrLEAeagrFRELAEEAARLRALA----EEAKRQRQLAEEDAARQRAEAERV-LAEKL 1839
Cdd:PHA03247 1629 aaIPATAAKTLDQARSVAEIVDQ-IEL----LLEQTEKAAELDVAAvdwlEHARRVFEAHPLTAARGGGPDPLArLHARL 1703
|
170 180
....*....|....*....|...
gi 41322919 1840 AAIGEATRLKTEAEIALKEKEAE 1862
Cdd:PHA03247 1704 DALGETRRRTEALRRSLEAAEAE 1726
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2157-2378 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2157 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQ-VEEELFSVRV 2235
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2236 QMEELSKLKARIEAENRALILRDKdntQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML--- 2312
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQK---EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEdee 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 2313 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEM 2378
Cdd:pfam13868 276 IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1345-1598 |
1.98e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.28 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1345 EEEERLAEQQRAEERERLAEVEA--ALEKQRQLAEAHAQAKAQAEREAKelQQRMQEEVVRREEAAVDAqqqkrsiqeEL 1422
Cdd:pfam04747 72 KSEKKKAQKQIAKDHEAEQKVNAkkAAEKEARRAEAEAKKRAAQEEEHK--QWKAEQERIQKEQEKKEA---------DL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEAEIQAKARQAEAAERSR-----LRIEEEIRVVRLqleATERQRGGAEGELQALRARAEEAEaqkrQAQEEAE 1497
Cdd:pfam04747 141 KKLQAEKKKEKAVKAEKAEKAEKTKkastpAPVEEEIVVKKV---ANDRSAAPAPEPKTPTNTPAEPAE----QVQEITG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1498 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAE 1577
Cdd:pfam04747 214 KKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQ 293
|
250 260
....*....|....*....|.
gi 41322919 1578 LQSKRasfAEKTAQLERSLQE 1598
Cdd:pfam04747 294 KKNKK---DKKKSESEKVVEE 311
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1791-2301 |
2.05e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.46 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1791 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 1870
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1871 edeafQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGR 1950
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1951 IRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2030
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2031 ESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQ 2110
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2111 VEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2190
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2191 LRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEA 2270
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 41322919 2271 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL 2301
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2238-2366 |
2.06e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2238 EELSKLKARIEAENRALILRDKDNTQrfLQEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2317
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41322919 2318 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ----------QLAEETQGFQR 2366
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAKiadlgrrlnvALAQRVQELNR 194
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1318-1653 |
2.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1318 DLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRM 1397
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1398 QEEVVRREEAAvDAQQQKRSIQEELQQLrqssEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQA 1477
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEEL----QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1478 LRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEV 1557
Cdd:COG4372 169 LEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1558 ERARQVQVALETAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1637
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....*.
gi 41322919 1638 ANEALRLRLQAEEVAQ 1653
Cdd:COG4372 327 KLELALAILLAELADL 342
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1510-1744 |
2.10e-03 |
|
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: 44.17 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1510 KRQAEVELASRVKAEaeaaREKQRALQAleELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASFAEkt 1589
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1590 aqlERSLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1669
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 1670 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAA 1744
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1190-1449 |
2.10e-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: 43.98 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1190 AVLAQTDVR---QRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVE 1266
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1267 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYVDLRthyseLTTLTSQYIKFISETLRRMEE 1346
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ-----YLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1347 EERLAEQQRAEERERLAEVEAALEKQRQLAEahaQAKAQAEREAKELQQRMQEEvvrrEEAAVDAQQQKRSIQEELQQLR 1426
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAEL----AAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 41322919 1427 QSSEAEIQAKARQAEAAERSRLR 1449
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2206-2358 |
2.23e-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: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2206 DEELQRLKAEATEAARQRSQVEEELfSVRVQMEELSKLKARIEAENRALILR---DKDNTQRFLQEEAEKMKQVAEEAAR 2282
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEAEL-AKKKAEERREAETARAEAEAAYEIAEanaEREVQRQLEIAEREREIELQEKEAE 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 2283 LSVAAQEAA-RLRQLAEEDLAQQRALAE-KMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLA 2358
Cdd:COG2268 301 REEAELEADvRKPAEAEKQAAEAEAEAEaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2180-2522 |
2.24e-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: 44.24 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2180 QKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKLKARIEAENralilrDK 2259
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI------DK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2260 DNTQRFLQEEaekmkqvaeeaaRLSVAAQEAARLRQLAEE--DLAQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQ-K 2336
Cdd:TIGR04523 192 IKNKLLKLEL------------LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE---KTTEISNTQTQlN 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2337 ELAQEQarrlQEDKEQMAQQLAEETQGFQRTLEAERQRQlEMSAEAERLKlrvaemsraqaraeedaqrfrKQAEEIGEK 2416
Cdd:TIGR04523 257 QLKDEQ----NKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEISDLN---------------------NQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2417 LHRTELATQEKVtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKSEEMQTvqqeqllqetqaLQQSFL 2496
Cdd:TIGR04523 311 ELKSELKNQEKK--LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN------------EIEKLK 376
|
330 340
....*....|....*....|....*.
gi 41322919 2497 SEKDSLLQRERFIEQEKAKLEQLFQD 2522
Cdd:TIGR04523 377 KENQSYKQEIKNLESQINDLESKIQN 402
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1372-1534 |
2.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1372 QRQLAEAHAQAK---AQAEREAKELQQRM----QEEVVR-REEAAVDAQQQKRSIQEELQQLRQSSEAEiqakARQAEAA 1443
Cdd:PRK12704 30 EAKIKEAEEEAKrilEEAKKEAEAIKKEAlleaKEEIHKlRNEFEKELRERRNELQKLEKRLLQKEENL----DRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1444 ERSrlriEEEIRVVRLQLEATERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQVQDESQRkrqae 1514
Cdd:PRK12704 106 EKR----EEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKVEEEARH----- 169
|
170 180
....*....|....*....|..
gi 41322919 1515 vELASRVKAEAEAARE--KQRA 1534
Cdd:PRK12704 170 -EAAVLIKEIEEEAKEeaDKKA 190
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2333-2614 |
2.34e-03 |
|
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: 44.34 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2333 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrTLEAERQRQlemsAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2412
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERRRK----LEEAEKARQ----AEMDRQAAIYAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2413 I-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQA 2490
Cdd:pfam17380 360 ReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2491 LQQsflsekdslLQRERFIEQEKAKLEQLFQDEvakaqqlREEQQRQQQQMEQERQRlvaSMEEARRRQHEAEEgVRRKQ 2570
Cdd:pfam17380 437 VRR---------LEEERAREMERVRLEEQERQQ-------QVERLRQQEEERKRKKL---ELEKEKRDRKRAEE-QRRKI 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 41322919 2571 EELQQLEQQRRQQeellaeENQRLREQLQLLEEQHRAALAHSEE 2614
Cdd:pfam17380 497 LEKELEERKQAMI------EEERKRKLLEKEMEERQKAIYEEER 534
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1687-2120 |
2.38e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.13 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1687 RELAEQELEKQRQLAEGTAQQRlaaeQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEV 1766
Cdd:COG5278 85 RAEIDELLAELRSLTADNPEQQ----ARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1767 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1846
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1847 RLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEE 1926
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1927 ILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKA 2006
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2007 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSVLDQLRGEAEAA 2086
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430
....*....|....*....|....*....|....
gi 41322919 2087 RRAAEEAEEARVQAEREAAQSRRQVEEAERLKQS 2120
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAE 514
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1336-1552 |
2.40e-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: 42.74 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1336 FISETLRRMEEEERLAEQQRAEERERLAEVEaalekqRQLAEAHAQAKaQAEREAKELQQRMQEEVVRREEAAVDAQQQ- 1414
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQAIRDMQSELVKAR------QALAQTIARQK-QLERRLEQQTEQAKKLEEKAQAALTKGNEEl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1415 KRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQE 1494
Cdd:pfam04012 85 AREALAEKKSLEKQAEALETQLAQQRSAVEQ-----------LRKQLAALETKIQQLKAKKNLLKARLKAAKAQEAVQTS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1495 EAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQaLEELRLQAEEAERRL 1552
Cdd:pfam04012 154 LGSLSTSSATDSFERIEEKIEEREARADAAAELASAVDLDAK-LEQAGIQMEVSEDVL 210
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1544-1941 |
2.61e-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: 43.73 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1544 QAEEAERRLRQAEVERARQVQvALETAQRSAEAELQ---SKRASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEA 1620
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQ-AQEAANRQREKEKErykRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1621 ERAREeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE--EQAVRQRELAEQELEKQR 1698
Cdd:pfam07888 107 SASSE---------ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKEraKKAGAQRKEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1699 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1778
Cdd:pfam07888 178 AKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1779 RSTSEKSKQR--LEAEAGRFR-ELAEEAARLR--ALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAigEATRLkteaE 1853
Cdd:pfam07888 258 EELSSMAAQRdrTQAELHQARlQAAQLTLQLAdaSLALREGRARWAQERETLQQSAEADKDRIEKLSA--ELQRL----E 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1854 IALKEKEAENERLR-RLAEDEAFQRRRLEEQaaqhkadieERLAQLRKASDSELERQKglvEDTLRQRRQVEEEILALKA 1932
Cdd:pfam07888 332 ERLQEERMEREKLEvELGREKDCNRVQLSES---------RRELQELKASLRVAQKEK---EQLQAEKQELLEYIRQLEQ 399
|
....*....
gi 41322919 1933 SFEKAAAGK 1941
Cdd:pfam07888 400 RLETVADAK 408
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
50-140 |
2.65e-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: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 50 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 122
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 41322919 123 DDIADGNPKLTLGLIWTI 140
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1471-1554 |
2.69e-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: 40.88 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1471 AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVElasrvKAEAEAAREKQralQALEELRLQAEEAER 1550
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKEEILA-----EAKEEAERILE---QAKAEIEQEKEKALA 113
|
....
gi 41322919 1551 RLRQ 1554
Cdd:cd06503 114 ELRK 117
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1369-1547 |
2.90e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1369 LEKQRQLAEAHAQAKAQAEREAKELQQRMQEEvvRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrl 1448
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1449 rieeeirvvrlqLEATERQRGGAEgelQALRARAEEAEAQKRQAQEEAERLrrqvqdESQRKRQAEVELASRVKAEAEaa 1528
Cdd:PRK12705 100 ------------LDNLENQLEERE---KALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 41322919 1529 REK-QRALQALEELRLQAEE 1547
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1475-1599 |
2.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1475 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELasrvKAEAEaarekQRALQALEELRLQAEEAERRLRQ 1554
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 41322919 1555 AEVERARQVqvaletaqrsAEAELQSKRASFAEKTAQLERSLQEE 1599
Cdd:PRK00409 596 LQKGGYASV----------KAHELIEARKRLNKANEKKEKKKKKQ 630
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1864-2045 |
2.97e-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: 42.60 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1864 ERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASDsELERQKGLVEDTLRQRRQVEEEIlalkasfEKAAAGKAE 1943
Cdd:COG1579 7 RALLDLQELDS-ELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEI-------EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1944 LELELGRIRSNAE-DTLrskeQAELEAARQRQlaaeeerrrREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2022
Cdd:COG1579 78 YEEQLGNVRNNKEyEAL----QKEIESLKRRI---------SDLEDEILELMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180
....*....|....*....|...
gi 41322919 2023 RLRERAEQESARQLQLAQEAAQK 2045
Cdd:COG1579 145 AELDEELAELEAELEELEAEREE 167
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1803-1947 |
3.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1803 AARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIAlkEKEAENERLRRLAEDEAFQRRRLEE 1882
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1883 QAAQ------HKADIEERLAQLRKASDSELERQKGLVEDTLRQR--RQVEEEILALKASFEKAAAGKAELELE 1947
Cdd:PRK12705 103 LENQleerekALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1726-1936 |
3.11e-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: 42.60 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1726 EQQRQLLEeeLARLQREAAAATQKRQELEAELAKVRAEMEvllaskaraeeesrstsekskqrleaeagrfrELAEEAAR 1805
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELA--------------------------------ALEARLEA 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1806 LRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIgeatrlKTEAEI-ALKEKEAENERLRRLAEDEAFQRRRLEEQA 1884
Cdd:COG1579 50 AKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNV------RNNKEYeALQKEIESLKRRISDLEDEILELMERIEEL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41322919 1885 AQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALKASFEK 1936
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1884-2060 |
3.13e-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: 43.21 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1884 AAQHKADIEERLAQLRKasdsELERQKGLVEDTLRQRRQVEEEILALKASFEKAAAGKAELELELGRIRSNAEDTLRSKE 1963
Cdd:COG4942 18 QADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1964 QAELEAARQRQLAAEEERRRREAEER--------------VQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRErAE 2029
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE-AE 172
|
170 180 190
....*....|....*....|....*....|.
gi 41322919 2030 QESARQLQLAQEAAQKRLQAEEKAHAFAVQQ 2060
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR 203
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2157-2421 |
3.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2157 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEE 2229
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2230 LFSVRVQMEEL-------SKLKARIEA-------------ENRALILRDKDntqrfLQEEAEKMKQVAEEAARLSVAAQE 2289
Cdd:COG1340 94 LDELRKELAELnkaggsiDKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2290 AARLRQLAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeetqgfqr 2366
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2367 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2421
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1409-1555 |
3.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1409 VDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERsrlrieeeirvvrlqleaterqrggAEGELQALRARAEEAEAQ 1488
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1489 KRQAQEEAERLRRQVQDESQRKRQaevelasrvkaeaeaaREKQRALQALEELRLqaEEAERR------LRQA 1555
Cdd:PRK11448 193 QQELEAQLEQLQEKAAETSQERKQ----------------KRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1686-1779 |
3.29e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1686 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEME 1765
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 41322919 1766 VLLASKARAEEESR 1779
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
35-145 |
3.36e-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: 40.75 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 35 DEQDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYL 110
Cdd:cd21337 12 DHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELM 91
|
90 100 110
....*....|....*....|....*....|....*
gi 41322919 111 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 145
Cdd:cd21337 92 QDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1360-1531 |
3.40e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 41.48 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1360 ERLAEVEAALEK-QRQLAEAHAQAKAQAEREAKELQQRMQ---EEVVRREEAAVDAQQQKrsIQEELQQLRQsseaeiQA 1435
Cdd:pfam01442 4 DSLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQkdlEEVRAKLEPYLEELQAK--LGQNVEELRQ------RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1436 KARQAEAAERSRLRIEEEIRVVRlqlEATERQRGGAEGELQALRARAEEAEAQKRQ-----AQEEAERLRRQVQDESQRK 1510
Cdd:pfam01442 76 EPYTEELRKRLNADAEELQEKLA---PYGEELRERLEQNVDALRARLAPYAEELRQklaerLEELKESLAPYAEEVQAQL 152
|
170 180
....*....|....*....|.
gi 41322919 1511 RQAEVELASRVKAEAEAAREK 1531
Cdd:pfam01442 153 SQRLQELREKLEPQAEDLREK 173
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1342-1431 |
3.42e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1342 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAH-------AQAKAQAEREAKE-LQQRMQEEVVRREEAAVDAQ 1412
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARkqaqaviAEAEAEADKLAAEaLAEAQAEAQASKEKARREIE 111
|
90
....*....|....*....
gi 41322919 1413 QQKrsiQEELQQLRQSSEA 1431
Cdd:PRK07353 112 QQK---QAALAQLEQQVDA 127
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2689-2726 |
3.44e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.44e-03
10 20 30
....*....|....*....|....*....|....*...
gi 41322919 2689 RHYLQGRSSIAGLLLKATNEKLSVYAALQRQLLSPGTA 2726
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1632-2115 |
3.51e-03 |
|
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: 43.58 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1632 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1694
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1695 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQREAAAATQKRQELEAELAKVRAEM 1764
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1765 EVLLASKarAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1840
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1841 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASDSE---LERQKGLVE 1914
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1915 DTLRQRRQVEEEILALKA---SFEKAAAGKAELELELGRIRSNAEDTLRSKEQ-AELEAARQRQLAAEEERRRREAEERV 1990
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAEDMTQKMQAHnEEMEAQLSVAEEELGGYKQQAQTLER 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1991 QKSLAAEEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQEAAQKR---LQAEEKAHAFAVQQK 2061
Cdd:pfam05557 423 ELQALRQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQQR 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2062 EQELQQTLQQEQSVLDQLRGEAEAARRAAEEAEEARVQAEREAAQSRRQVEEAE 2115
Cdd:pfam05557 503 KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1096-1767 |
3.55e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.66 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1096 RGTQGAEEVLRAHEEQLKEAQAVPATLPEleatkaslkklrAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVE 1175
Cdd:NF041483 569 RQAEAAEELTRLHTEAEERLTAAEEALAD------------ARAEAERIRREAAEETERLRTEAAERIRTLQAQAEQEAE 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1176 RWRERVAQLLERWQAVLAQTDVRQR-----ELEQLGRQLRyyrESADPLGAWLQDARRR--QEQIQAMPLADSQAVREQL 1248
Cdd:NF041483 637 RLRTEAAADASAARAEGENVAVRLRseaaaEAERLKSEAQ---ESADRVRAEAAAAAERvgTEAAEALAAAQEEAARRRR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1249 RQEQALL-------EEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESV--IQEYVDl 1319
Cdd:NF041483 714 EAEETLGsaraeadQERERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVagLQEQAE- 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1320 rthySELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEvEAALEKQRQLAEAHAqAKAQAER----------- 1388
Cdd:NF041483 793 ----EEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASE-DANRLRREAQEETEA-AKALAERtvseaiaeaer 866
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 ---EAKELQQRMQEEVV-RREEAAVDAQQQKRSIQEELQQLRqsSEAEIQAKARQAEAAErsrlrieEEIRVVRLQLEAT 1464
Cdd:NF041483 867 lrsDASEYAQRVRTEASdTLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATS-------EAERLTAEARAEA 937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1465 ERQRGGAEGELQALRARA-EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVEL---ASRVKAEAEAAREKQRALQALEE 1540
Cdd:NF041483 938 ERLRDEARAEAERVRADAaAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIrteAERVKAEAAAEAERLRTEAREEA 1017
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1541 LRL----QAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSKRASfAEKTAQLERSLQEEHVAVAQLREEAERRAQQ 1616
Cdd:NF041483 1018 DRTldeaRKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT-TEAEAQADTMVGAARKEAERIVAEATVEGNS 1096
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1617 QAEAERAREEAERELERWQLKAN----EALRLRLQAE-----EVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1687
Cdd:NF041483 1097 LVEKARTDADELLVGARRDATAIreraEELRDRITGEieelhERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKE 1176
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1688 ELAEQELE----------KQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEElarlQREAAAATQKRQELEAEL 1757
Cdd:NF041483 1177 LVSDANSEaskvriaavkKAEGLLKEAEQKKAELVREAEKIKAEAEA--EAKRTVEEG----KRELDVLVRRREDINAEI 1250
|
730
....*....|
gi 41322919 1758 AKVRAEMEVL 1767
Cdd:NF041483 1251 SRVQDVLEAL 1260
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1681-1846 |
3.60e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKV 1760
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1840
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 41322919 1841 AIGEAT 1846
Cdd:COG3883 275 GAAAAS 280
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1389-1527 |
3.61e-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: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 EAKELQQRMQEevVRREEAAVDAQQQKRSiQEELQQLRQSsEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQR 1468
Cdd:COG0542 412 ELDELERRLEQ--LEIEKEALKKEQDEAS-FERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41322919 1469 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEVELASRVKAEAEA 1527
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1357-1587 |
3.83e-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: 42.98 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1357 EERERLAEVEAAL-------EKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSS 1429
Cdd:pfam13868 3 ENSDELRELNSKLlaakcnkERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1430 EAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---------- 1499
Cdd:pfam13868 83 EEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREederileylk 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1500 -----RRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQaEEAERRLRQAEVERARQVQVALETAQRSA 1574
Cdd:pfam13868 163 ekaerEEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ-EEQERKERQKEREEAEKKARQRQELQQAR 241
|
250
....*....|...
gi 41322919 1575 EAELQSKRASFAE 1587
Cdd:pfam13868 242 EEQIELKERRLAE 254
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1102-1598 |
3.93e-03 |
|
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: 43.56 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1102 EEVLRAHEEQLKEAQAVPATL-PELEATKASL-------KKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVE 1173
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLtKELEDIKMSLqrsmstqKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1174 VERWRERVAQLLERWQAVLAQTdvrQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMpLADSQAVREQLRQEQA 1253
Cdd:pfam05483 354 FEATTCSLEELLRTEQQRLEKN---EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1254 LLEEIErhgEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqEYVDLRTHYSELTTLTSQY 1333
Cdd:pfam05483 430 IAEELK---GKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL--KNIELTAHCDKLLLENKEL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1334 IKFISE-TLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRM---QEEVVRREEAAV 1409
Cdd:pfam05483 505 TQEASDmTLELKKHQEDIINCKKQEER-MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLdksEENARSIEYEVL 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1410 DAQQQKRSIQEELQQLRQS--------SEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLE-ATERQRGG-------AEG 1473
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQienknkniEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEeiidnyqKEI 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1474 ELQALRARAEEAEAQKRQA-QEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERrl 1552
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAiADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAK-- 741
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 41322919 1553 rqaeverarqvqVALETAQRSAEAELQSKRASFA---EKTAQLERSLQE 1598
Cdd:pfam05483 742 ------------AALEIELSNIKAELLSLKKQLEiekEEKEKLKMEAKE 778
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2159-2527 |
3.95e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2159 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKnlldEELQRLKAEATEAARQrsQVEEELFSVRVQME 2238
Cdd:pfam09731 98 SSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKA----ESATAVAKEAKDDAIQ--AVKAHTDSLKEASD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2239 --ELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA------LAEK 2310
Cdd:pfam09731 172 taEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLaklvdqYKEL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2311 MLKEKMQAVQEATRLkaEAELLQQQKELAQEQARRL-------QEDKEQMAQQLAE-ETQGFQRTLEAERQRQLEMSAEA 2382
Cdd:pfam09731 252 VASERIVFQQELVSI--FPDIIPVLKEDNLLSNDDLnsliahaHREIDQLSKKLAElKKREEKHIERALEKQKEELDKLA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2383 ERLKLR---VAEMSRAQARAEEDAQRFRkQAEEIGEKLhRTELATQEKV---TLVQTLEIQRQQSDHDAERLREAIAELE 2456
Cdd:pfam09731 330 EELSARleeVRAADEAQLRLEFEREREE-IRESYEEKL-RTELERQAEAheeHLKDVLVEQEIELQREFLQDIKEKVEEE 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2457 REKEKLQQEAKLLQLKSEEMQTVQQEQLLQETQALQQ---------SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA 2527
Cdd:pfam09731 408 RAGRLLKLNELLANLKGLEKATSSHSEVEDENRKAQQlwlavealrSTLEDGSADSRPRPLVRELKALKELASDDEVVKA 487
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1344-1424 |
3.95e-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: 40.50 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1344 MEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAH-------AQAKAQAEREAKELQQRMQEEVVR-REEAAVDAQQQ 1414
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEyEEKLAEARaeaqeiiEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQE 107
|
90
....*....|
gi 41322919 1415 KRSIQEELQQ 1424
Cdd:cd06503 108 KEKALAELRK 117
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2168-2376 |
4.00e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2168 EKHKKFAEQTLrqkAQVEQELTTLRLQLE-----ETDHQKNLLDEELQRLKAEATEAAR-QRSQVEEElfsVRVQMEELS 2241
Cdd:COG2268 147 EDREKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGRRKIAEIIRDARiAEAEAERE---TEIAIAQAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2242 KLKARIEAENRALIL--------RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMlK 2313
Cdd:COG2268 221 REAEEAELEQEREIEtariaeaeAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-A 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 2314 EKMQAVQEAT-RLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQL 2376
Cdd:COG2268 300 EREEAELEADvRKPAEAEKQAAEAE-AEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLML 362
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2255-2470 |
4.02e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.40 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2255 ILRDKDNTQRFLQEeaeKMKQVAEEAARLSVAAQEAARLRQLAE---EDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2331
Cdd:pfam06008 17 INYNLENLTKQLQE---YLSPENAHKIQIEILEKELSSLAQETEelqKKATQTLAKAQQVNAESERTLGHAKELAEAIKN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2332 LQQQKELAQEQARRLQEDKEQMA-QQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAE--MSRAQARAEEDAQRFRK 2408
Cdd:pfam06008 94 LIDNIKEINEKVATLGENDFALPsSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQdlLSRIQTWFQSPQEENKA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41322919 2409 QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQ 2470
Cdd:pfam06008 174 LANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1226-1562 |
4.20e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.30 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1226 ARRRQEQIQAMpLADSQAVREQLRQE-QALLEEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVaspakkpk 1304
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELK---DKYRELRKTLLANRFSYGPAIDEL-------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1305 vqsgsESVIQEYVDLRTHYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1383
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1384 AQ--------AEREAKELQQRMQEEVVRREEAAVD-AQQQKRSIQEELQQLRQSSEAEIQAKArqaeaaersrlRIEEEI 1454
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKK-----------YVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1455 RVVRLQLEATERQRGGAEGELQALRAR---AEEAEAQKRQAQEEAERLRRQVQDESQR---KRQAEVELASRVKaeaeaa 1528
Cdd:pfam06160 294 PEIEDYLEHAEEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERleeKEVAYSELQEELE------ 367
|
330 340 350
....*....|....*....|....*....|....
gi 41322919 1529 rEKQRALQALEELRLQAEEAERRLRQAEvERARQ 1562
Cdd:pfam06160 368 -EILEQLEEIEEEQEEFKESLQSLRKDE-LEARE 399
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1345-1528 |
4.25e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1345 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAV-DAQQQKRSIQEELQ 1423
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1424 QLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1503
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*.
gi 41322919 1504 QDESQRKrqAEVELA-SRVKAEAEAA 1528
Cdd:PRK05035 671 EAEDPKK--AAVAAAiARAKAKKAAQ 694
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1364-1753 |
4.25e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1364 EVEAALEKqrqlaeahaqakaqaEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeaeiqAKARQAEAA 1443
Cdd:pfam02029 4 EEEAARER---------------RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1444 ERSRLRIEEEIRVVRLQlEATERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKA 1523
Cdd:pfam02029 64 FLDRTAKREERRQKRLQ-EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1524 EAEAAREKqralqalEELRLQAEEAERRLRQAEVERA-RQVQVALETAQRSAEAELQSKRASfaEKTAQLERSLQEEHVA 1602
Cdd:pfam02029 140 YQENKWST-------EVRQAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1603 VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQ 1682
Cdd:pfam02029 211 NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL-------------------------------------EEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1683 AVRQRELAEQELEKQRQlaegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELAR-----LQREAAA 1745
Cdd:pfam02029 254 RRRRQEKESEEFEKLRQ-----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRrmkeeIERRRAE 328
|
....*...
gi 41322919 1746 ATQKRQEL 1753
Cdd:pfam02029 329 AAEKRQKL 336
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2271-2365 |
4.38e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2271 EKMKQVAEEAARLSVAAQEAARLRQLAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2344
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 41322919 2345 RLQEDKEQMAQQLAEETQGFQ 2365
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1546-1882 |
4.61e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1546 EEAERRLRQAEVERARqvqvaLETAQRSAEAELQSKRASFAE----KTAQLERS---LQEEHVAVAQLREEAERRAQQQA 1618
Cdd:pfam03528 4 EDLQQRVAELEKENAE-----FYRLKQQLEAEFNQKRAKFKElylaKEEDLKRQnavLQEAQVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1619 EAERAREEAerelERWQLKANEALRLRLQaEEVAqqkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL-EKQ 1697
Cdd:pfam03528 79 NIKAVATVS----ENTKQEAIDEVKSQWQ-EEVA---SLQAIMKETVREYEVQFHRRLEQERAQWNQYRESAEREIaDLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1698 RQLAEGTAQQRLaaEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAelAKVRAEMEVLLASKA-RAEE 1776
Cdd:pfam03528 151 RRLSEGQEEENL--EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEA--SKMKELNHYLEAEKScRTDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1777 ESR-STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL---AEKLAAIGEATRLKTEA 1852
Cdd:pfam03528 227 EMYvAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLmrdMQRMESVLTSEQLRQVE 306
|
330 340 350
....*....|....*....|....*....|
gi 41322919 1853 EIALKEKEaENERLRRLAEDEAFQRRRLEE 1882
Cdd:pfam03528 307 EIKKKDQE-EHKRARTHKEKETLKSDREHT 335
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2178-2475 |
4.63e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2178 LRQKAQVEQ-ELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFsvrvQMEELSKLKARIEAEnraliL 2256
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALN----ELSSLEDMKNRYESE-----I 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2257 RDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2336
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2337 ELAQEQARRLQEDKEQMAQQLAEET--QGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2414
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2415 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2462
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 41322919 2463 QQEAKllQLKSEE 2475
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2208-2469 |
4.64e-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: 43.36 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2208 ELQRLKAEATEAARQRSQVEEElfsvrvqmEELSKLKARIEAEN-RALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVA 2286
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEE--------ANFEKTKALIQCEQlKSELERQKERLEKELASQQEKRAQEKEALRKEMKK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2287 AQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLAEETQgf 2364
Cdd:pfam15964 397 EREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLASQEMDVTKVCGEmRYQLNQTKMKKDEAEKEH-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2365 qRTLEAERQRQLEMS-AEAERLKL-------RVAEMSRAQARAEEDAQRFrkqAEEIGEKLHRTELATQEKVTLVQTL-- 2434
Cdd:pfam15964 473 -REYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREECLKL---TELLGESEHQLHLTRLEKESIQQSFsn 548
|
250 260 270
....*....|....*....|....*....|....*..
gi 41322919 2435 --EIQRQQSDHDAERLREAIAELEREKEKLQQEAKLL 2469
Cdd:pfam15964 549 eaKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL 585
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1108-1606 |
4.83e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1108 HEEQLKEAQAVPATLPELEatkaslkklrAQAEAQQPTFDAlRDElrGAQEVGERLQQRHGERDVEVERWrERVAQLLEr 1187
Cdd:pfam10174 125 HERQAKELFLLRKTLEEME----------LRIETQKQTLGA-RDE--SIKKLLEMLQSKGLPKKSGEEDW-ERTRRIAE- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1188 WQAVLAQTDVrqrELEQLGRQLRYYRESAdplgawlqdarRRQEQIQAMPlADSQAVREQLRQEQALLEEIERHGEKVEE 1267
Cdd:pfam10174 190 AEMQLGHLEV---LLDQKEKENIHLREEL-----------HRRNQLQPDP-AKTKALQTVIEMKDTKISSLERNIRDLED 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1268 CQRFAKQyiNAIKDYELQLVTYKaQLEPVASPAK--KPKVQSGSESVIQEYVDLRTHYSELTTLTS------QYIKFISE 1339
Cdd:pfam10174 255 EVQMLKT--NGLLHTEDREEEIK-QMEVYKSHSKfmKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckQHIEVLKE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1340 TLRRMEEEERLAEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKAQA-------------EREAKELQQRMQ--EEVVR 1403
Cdd:pfam10174 332 SLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmldvkERKINVLQKKIEnlQEQLR 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1404 reeaavDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEA-------AERSRLRIEEEIRVVRLQLEATERQRGGAEGELQ 1476
Cdd:pfam10174 412 ------DKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVS 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1477 ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAER-RLRQA 1555
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQ 565
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1556 EV----ERARQVQVALE---TAQRSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1606
Cdd:pfam10174 566 EVarykEESGKAQAEVErllGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1372-1537 |
4.84e-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: 42.41 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1372 QRQLAEAHAQAKAQAeREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAER-SRLRI 1450
Cdd:pfam00529 53 PTDYQAALDSAEAQL-AKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDlARRRV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1451 EEEIRVV-RLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqAEVElASRVKAEAEAAR 1529
Cdd:pfam00529 132 LAPIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQI-AEAE-AELKLAKLDLER 209
|
....*...
gi 41322919 1530 EKQRALQA 1537
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1423-1903 |
5.01e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1423 QQLRQSSEAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEA-TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR 1501
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1502 QVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQVQVALETAQRSAEAELQSK 1581
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1582 RASFAEKTAQLERSLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAE 1661
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1662 AEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELiRLRAETEQGEQQRQLLEEELARLQR 1741
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGL-VLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1742 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1821
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1822 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA 1901
Cdd:COG3064 401 LGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
..
gi 41322919 1902 SD 1903
Cdd:COG3064 481 LL 482
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2174-2347 |
5.16e-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: 43.40 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2174 AEQTLRQKAQVEQELTTLRLQL-------EETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEELSKlkar 2246
Cdd:COG3096 524 LEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA---- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2247 ieaenRALILRDkdntqrflqeeaekmkqvaeeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMlkekMQAVQEATRLK 2326
Cdd:COG3096 600 -----RAPAWLA---------------------------AQDALERLREQSGEALADSQEVTAAM----QQLLEREREAT 643
|
170 180
....*....|....*....|.
gi 41322919 2327 AEAELLQQQKELAQEQARRLQ 2347
Cdd:COG3096 644 VERDELAARKQALESQIERLS 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1717-1825 |
5.19e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1717 RLRAETEQGEQQRQLLEEELARLQREAAAAT--------QKRQELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQR 1788
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKkeqdeasfERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEE 479
|
90 100 110
....*....|....*....|....*....|....*....
gi 41322919 1789 LEAEAGRFRELAEEAARLRALAEEAKRQRQLA--EEDAA 1825
Cdd:COG0542 480 LEQRYGKIPELEKELAELEEELAELAPLLREEvtEEDIA 518
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2255-2417 |
5.25e-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: 41.83 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2255 ILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKmLKEKMQAVQ---EATRLKAEAEL 2331
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2332 LQQQKELAQEQARRLQEDKEQMAQQLAEETQgfqrtleaerqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2411
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEA--------------ELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 41322919 2412 EIGEKL 2417
Cdd:COG1579 167 ELAAKI 172
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1689-1974 |
5.67e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1689 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLL 1768
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1769 ASKARAEEESRSTSEKSKQRLEAEagrFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAtRL 1848
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAA---FRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA-RQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1849 KTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVedtlrqrrqveeeil 1928
Cdd:PRK11637 170 ETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT--------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1929 ALKASFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-------ARQRQ 1974
Cdd:PRK11637 223 GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarvrDKQKQ 276
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1312-1579 |
5.70e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1312 VIQEYVDLRThYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEererLAEVEAALEKQRQLAEAHAQAKAQAEREAK 1391
Cdd:COG1538 78 VAQAYFDLLA-AQEQLALAEENLALAEELLELARARYEAGLASRLD----VLQAEAQLAQARAQLAQAEAQLAQARNALA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1392 ELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSeAEIQAKARQAEAAERsRLRIEEEIRVVRLQLEATERQRGGA 1471
Cdd:COG1538 153 LLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERR-PDLRAAEAQLEAAEA-EIGVARAAFLPSLSLSASYGYSSSD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1472 EGELQ-------------------ALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1532
Cdd:COG1538 231 DLFSGgsdtwsvglslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1533 RALQALEEL-------RLQAEEAERRLRQAEVERarqvqVALETAQRSAEAELQ 1579
Cdd:COG1538 311 EALELARARyraglasLLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1484-1583 |
5.71e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.08 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1484 EAEAQKRQAQEEAERLR--RQVQDESQRK-------RQAEVELASRVKAEAEA-AREKQRALQA-LEELRLQAeEAERRL 1552
Cdd:PTZ00491 671 QAELLEQEARGRLERQKmhDKAKAEEQRTkllelqaESAAVESSGQSRAEALAeAEARLIEAEAeVEQAELRA-KALRIE 749
|
90 100 110
....*....|....*....|....*....|..
gi 41322919 1553 RQAEVERARQVQVA-LETAQRSAEAELQSKRA 1583
Cdd:PTZ00491 750 AEAELEKLRKRQELeLEYEQAQNELEIAKAKE 781
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1346-1606 |
5.95e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1346 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRmQEEVVRR-----------EEAAVDAQQQ 1414
Cdd:PRK10811 514 SEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAAAPKAAAATPPA-QPGLLSRffgalkalfsgGEETKPQEQP 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1415 KRSIQE--ELQQLRQSSeaeiqakaRQAEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQA 1492
Cdd:PRK10811 593 APKAEAkpERQQDRRKP--------RQNNRRDRNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEK 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1493 QEEAERLRRQVQDESQRKRQAEVELASrvkAEAEAarekqralQALEELRLQAEEAERRLRQAEVERA-RQV--QVALET 1569
Cdd:PRK10811 665 ARTQDEQQQAPRRERQRRRNDEKRQAQ---QEAKA--------LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQ 733
|
250 260 270
....*....|....*....|....*....|....*..
gi 41322919 1570 AQrSAEAELQSKRASFAEKTAQLERSLQEEHVAVAQL 1606
Cdd:PRK10811 734 SV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1679-1779 |
6.17e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1679 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELA 1758
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 41322919 1759 KvRAEMEVLLaskarAEEESR 1779
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1708-2054 |
6.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1708 RLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQ 1787
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1788 RLEAEAgRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1867
Cdd:COG4372 96 LAQAQE-ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1868 RLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDSELERQKGLVEDTLRQRR--QVEEEILALKASFEKAAAGKAELE 1945
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEakLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1946 LELGRIRSNAEDTLRSKEQAELEAARQRQLAAEEERRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLR 2025
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
330 340
....*....|....*....|....*....
gi 41322919 2026 ERAEQESARQLQLAQEAAQKRLQAEEKAH 2054
Cdd:COG4372 335 LLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1701-1844 |
6.31e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1701 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1780
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41322919 1781 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1844
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1353-1556 |
6.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1353 QQRAEERERLAEVEAALEKQRQLAEAHAQAK---AQAEREAKELQQRMQEEVVRRE------------EAAVDAQQQKRS 1417
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLEWRQQTEVLSPEeekelvekikelEKELEKAKKALE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1418 IQEELQQLRqsseAEIQAKARQAEAAERSRLRIEEEIRVVRLQLEATERQRggaegelQALRARAEEAEAQKRQAQEEAE 1497
Cdd:COG1340 158 KNEKLKELR----AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEA-------DELRKEADELHKEIVEAQEKAD 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 1498 RLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRalqalEELRLQAEEAERRLRQAE 1556
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEK-----EELEEKAEEIFEKLKKGE 280
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-258 |
6.54e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.62 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 36 EQDERDRVQKKTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQI 105
Cdd:COG5069 372 EFDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENY 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 106 ALDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMVEGY--- 175
Cdd:COG5069 450 AVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLGLKGdke 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 176 QGLRCDNFTSSWRDGRLFNAIIHRHKPLLIDMNKVyRQTNLENLDQA-------FSVAERDLGVTRLLDPEDVDVPQPdE 248
Cdd:COG5069 522 EGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLV-TRGFTEFDDIAdarslaiSSKILRSLGAIIKFLPEDINGVRP-R 599
|
250
....*....|
gi 41322919 249 KSIITYVSSL 258
Cdd:COG5069 600 LDVLTFIESL 609
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1726-1841 |
6.78e-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: 40.16 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1726 EQQRQLLEEELARLQREAAAATQKRQELEAELAKVRAEMEVLLaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1805
Cdd:COG0711 30 DERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII---AEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIE 106
|
90 100 110
....*....|....*....|....*....|....*.
gi 41322919 1806 lralAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1841
Cdd:COG0711 107 ----QERAKALAELRAEVADLAVAIAEKILGKELDA 138
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1339-1506 |
7.00e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRA---EERERLAEVEAALEKQRQLAEAHAQ----AKAQAEREAKELqqrmqeevvrreeaavda 1411
Cdd:PRK00409 492 EIAKRLGLPENIIEEAKKligEDKEKLNELIASLEELERELEQKAEeaeaLLKEAEKLKEEL------------------ 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1412 QQQKRSIQEELQQLRQSSEAEIQAKARQAEAAersrlrIEEEIRVVRL--QLEATERQRGGAEGELQALRARAEEAEAQK 1489
Cdd:PRK00409 554 EEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKE------ADEIIKELRQlqKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
170
....*....|....*..
gi 41322919 1490 RQAQEEAERLrrQVQDE 1506
Cdd:PRK00409 628 KKQKEKQEEL--KVGDE 642
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2287-2469 |
7.01e-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: 41.45 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2287 AQEAARLRQLAEED--LAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETqgf 2364
Cdd:COG1579 3 PEDLRALLDLQELDseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2365 qrtleaERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTElatqekvtlvQTLEIQRQQSDHD 2444
Cdd:COG1579 80 ------EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEK 143
|
170 180
....*....|....*....|....*
gi 41322919 2445 AERLREAIAELEREKEKLQQEAKLL 2469
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREEL 168
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1460-1585 |
7.03e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1460 QLEATERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQAL 1538
Cdd:PRK09039 67 DLLSLERQGnQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 1539 EELR---------LQAEEAERRLRQAEVER-ARQVQVALetAQRSaeAELQSKRASF 1585
Cdd:PRK09039 147 AALRrqlaaleaaLDASEKRDRESQAKIADlGRRLNVAL--AQRV--QELNRYRSEF 199
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1234-1512 |
7.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1234 QAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVAspakkpkvqsgsesvi 1313
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET---------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1314 qeyvdlRTHYSELttltsqyikfiseTLRRMEE--EERLAEQQRAeererlaeveaalekQRQLAEAHAQ---AKAQAER 1388
Cdd:PRK11281 115 ------RETLSTL-------------SLRQLESrlAQTLDQLQNA---------------QNDLAEYNSQlvsLQTQPER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1389 EAKEL---QQRMQEevVRREEAAVDAQQqkRSIQEELQQLRQSSEAEIQAKA--RQAEAAERSRLrieeeIRVVRLQLEA 1463
Cdd:PRK11281 161 AQAALyanSQRLQQ--IRNLLKGGKVGG--KALRPSQRVLLQAEQALLNAQNdlQRKSLEGNTQL-----QDLLQKQRDY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1464 TERQRGGAEGELQALRA-----RAEEAEAQKRQAQEEAERLRRQ----VQDESQRKRQ 1512
Cdd:PRK11281 232 LTARIQRLEHQLQLLQEainskRLTLSEKTVQEAQSQDEAARIQanplVAQELEINLQ 289
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1120-1563 |
7.39e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1120 ATLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDVRQ 1199
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1200 RELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQALLEEIERHGEKVEECQRFAKQYINAI 1279
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1280 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTHYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1359
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1360 ERLAEVEAALEKQRQLAEAHAQAKAQAEREAKELQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQ 1439
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1440 AEAAERSRLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEVELAS 1519
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 41322919 1520 RVKAEAEAAREKQRALQALEELRLQAEEAERRLRQAEVERARQV 1563
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1784-1931 |
7.49e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1784 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1851
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1852 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASDSELERQKGLVEDTLRQRRQVEEEILALK 1931
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1681-1941 |
7.51e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1681 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQreaaaatQKRQELEAELAKV 1760
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1761 RAEMEVLLASKARAEEESRSTSEKSKqRLEAEAGRF----------RELAEEAARLRALAEEAKRQRQLAEE-DAARQRA 1829
Cdd:COG1340 91 REELDELRKELAELNKAGGSIDKLRK-EIERLEWRQqtevlspeeeKELVEKIKELEKELEKAKKALEKNEKlKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1830 EAERVLAEKL-----AAIGEATRLKTEAeIALKEKEaenERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASDS 1904
Cdd:COG1340 170 KELRKEAEEIhkkikELAEEAQELHEEM-IELYKEA---DELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250 260 270
....*....|....*....|....*....|....*....
gi 41322919 1905 ElerqKGLVEDTLRQRRQVEEEILALKAS--FEKAAAGK 1941
Cdd:COG1340 246 L----KKLRKKQRALKREKEKEELEEKAEeiFEKLKKGE 280
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1447-1564 |
7.53e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1447 RLRIEEEIRVVRLQLEATERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL---RRQVQDESQR-KRQAEVELASRVK 1522
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLeqkRQEAEEEKERlEESAEMEAEEKEQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 41322919 1523 AEAEaAREKQRALQALEELRLQAEEAERRLrQAEVERARQVQ 1564
Cdd:pfam20492 81 LEAE-LAEAQEEIARLEEEVERKEEEARRL-QEELEEAREEE 120
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1678-1818 |
7.67e-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: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1678 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAATQKRQELEA-- 1755
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41322919 1756 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1818
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2320-2398 |
7.82e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 42.01 E-value: 7.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41322919 2320 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLAEETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2398
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1687-1854 |
7.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1687 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQREAAAAtqkRQELEAELAKVRAEmev 1766
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKE--- 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1767 llaskARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEAT 1846
Cdd:PRK00409 582 -----AKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNK-ANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVL 655
|
....*...
gi 41322919 1847 RLKTEAEI 1854
Cdd:PRK00409 656 SIPDDKEA 663
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1339-1440 |
8.01e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1339 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAEREAKELQQrmqeevvRREEAAVDAQQQKRSI 1418
Cdd:PRK11448 152 LTLKQQLELQAREKAQSQALAEAQQQELVALEG---LAAELEEKQQELEAQLEQLQE-------KAAETSQERKQKRKEI 221
|
90 100
....*....|....*....|....*.
gi 41322919 1419 QEELQQLRQSSEAE----IQAKARQA 1440
Cdd:PRK11448 222 TDQAAKRLELSEEEtrilIDQQLRKA 247
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1528-1582 |
8.30e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 1528 AREKQRALQaleelRLQAEEAERRlRQAEVERARQVQVALETAQRS-AEAELQSKR 1582
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| PRK01294 |
PRK01294 |
lipase secretion chaperone; |
1393-1566 |
8.30e-03 |
|
lipase secretion chaperone;
Pssm-ID: 234937 [Multi-domain] Cd Length: 336 Bit Score: 41.97 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1393 LQQRMQEEVVRREEAAVDAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAaersrlrieeeirvvrLQLEATERQRGGAE 1472
Cdd:PRK01294 187 YQRYALERLRIAQDPSLSDAQKAARLAALEAQLPEDLRAALQESQRQQAL----------------LQQLAQLQASGASP 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1473 GELQALRARAEEAEAqkrqaqeeAERLRRQVQDESQRKRQAEVELASRVKAEAEAAREKQRALQALEELRLQAEEAERRL 1552
Cdd:PRK01294 251 QELRLMRAQLVGPEA--------AQRLEQLDQQRAAWQQRYDDYLAQRAQILNAAGLSPQDRQAQIAQLRQQRFSPQEAL 322
|
170
....*....|....
gi 41322919 1553 RQAEVERARQVQVA 1566
Cdd:PRK01294 323 RLAALERIHDAGQT 336
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1431-1598 |
8.68e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 42.20 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1431 AEIQAKARQAEAAERSRLRIEEEIrvvrlqlEATERQRGGAEGElQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1510
Cdd:PRK12678 29 PELRALAKQLGIKGTSGMRKGELI-------AAIKEARGGGAAA-AAATPAAPAAAARRAARAAAAARQAEQPAAEAAAA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1511 RQAEVELASRVKAEAEAAREKQRALQALEelRLQAEEAERRLRQAEVERARQVQVALE---TAQRSAEAELQSKRASFAE 1587
Cdd:PRK12678 101 KAEAAPAARAAAAAAAEAASAPEAAQARE--RRERGEAARRGAARKAGEGGEQPATEAradAAERTEEEERDERRRRGDR 178
|
170
....*....|.
gi 41322919 1588 KTAQLERSLQE 1598
Cdd:PRK12678 179 EDRQAEAERGE 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2303-2503 |
8.81e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2303 QQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLaeETQGFQRTLEAERQRQLEMSAEA 2382
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2383 ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVtlvqtleiqrqqsdhdaERLREAIAELEREKEKL 2462
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL-----------------QDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 41322919 2463 QQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDSLL 2503
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1995-2498 |
8.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1995 AAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQS 2074
Cdd:COG3899 738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2075 VLDQLRGEAEAARRAAEEAEEARVQAER-EAAQSRRQVEEAERLKQSAEEQAQARAQAQAAAEKLRKEAEQEAARRAQAE 2153
Cdd:COG3899 818 ALAERLGDRRLEARALFNLGFILHWLGPlREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLL 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2154 QAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSV 2233
Cdd:COG3899 898 AAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2234 RVQMEELSKLKARIEAENRALILRDKDNTQRFLQEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2313
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2314 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMS 2393
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2394 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQQEAKLLQLKS 2473
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*
gi 41322919 2474 EEMQTVQQEQLLQETQALQQSFLSE 2498
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRL 1242
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2333-2467 |
8.88e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2333 QQQKELAQEQARRLQEDKEQMAQQLAEETQgfQRTLEAERQRQLEMSAEAERLKLRVAEMSR------AQARAEEDAQRF 2406
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41322919 2407 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLQQEAK 2467
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
1337-1440 |
9.07e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 40.69 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1337 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA----QAEREAKELQQRMQEEVVRREEAA---- 1408
Cdd:pfam06391 63 VEETEKKIEQYEKENKDLILKNKMKLSQEEEELEELLELEKREKEERRkeekQEEEEEKEKKEKAKQELIDELMTSnkda 142
|
90 100 110
....*....|....*....|....*....|....
gi 41322919 1409 --VDAQQQKRSIQEELQQLRQSSEAEIQAKARQA 1440
Cdd:pfam06391 143 eeIIAQHKKTAKKRKSERRRKLEELNRVLEQKPT 176
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2194-2470 |
9.36e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2194 QLEETDHQKNLLDEELQRLKAEATEAARQRSQVEEELFSVRVQMEEL-SKLKARIEAENRALILRDKDNTQrfLQEEAEK 2272
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELNEK--VKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2273 MKQVAEEAARLSvaaQEAARLRQLAEEDLAQQRALAEkmLKEKMQAVQ-----EATRLKAEAELLQQQKELAQE-QARRL 2346
Cdd:COG1340 80 RDELNEKLNELR---EELDELRKELAELNKAGGSIDK--LRKEIERLEwrqqtEVLSPEEEKELVEKIKELEKElEKAKK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2347 QEDKEQMAQQLAEETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA--QARAEEDA-----QRFRKQAEEIGEKLHR 2419
Cdd:COG1340 155 ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADElhkeiVEAQEKADELHEEIIE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 41322919 2420 T-----ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLQ-QEAKLLQ 2470
Cdd:COG1340 235 LqkelrELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTtEELKLLQ 291
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1345-1532 |
9.49e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 42.29 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1345 EEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAER----------EAKELQQRMQEEVVRRE-----EAAV 1409
Cdd:TIGR00927 649 GERPTEAEGENGEESGGEAEQE---GETETKGENESEGEIPAERkgeqegegeiEAKEADHKGETEAEEVEhegetEAEG 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1410 DAQQQKRSIQEELQQLRQSSEAEIQAKARQAEAAERSRLRIEEEirvvrlqlEATERQRGGAEGELQA---LRARAEEAE 1486
Cdd:TIGR00927 726 TEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGE--------TEAEGKEDEDEGEIQAgedGEMKGDEGA 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41322919 1487 AQKRQAQEEAERlRRQVQDESQRKRQAEVELASRVKAEAEAAREKQ 1532
Cdd:TIGR00927 798 EGKVEHEGETEA-GEKDEHEGQSETQADDTEVKDETGEQELNAENQ 842
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4281-4311 |
9.69e-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: 9.69e-03
10 20 30
....*....|....*....|....*....|.
gi 41322919 4281 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4311
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
2185-2412 |
9.75e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2185 EQELTTLRLQLEETDHQKNLLD-------EELQRLKAEATEAARQRSQVEEELFSVRVQMEELSklKARIEAENRAlilr 2257
Cdd:pfam00038 53 EKEIEDLRRQLDTLTVERARLQleldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEAT--LARVDLEAKI---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 2258 dkdntqRFLQEEAEKMKQVAEEaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK- 2336
Cdd:pfam00038 127 ------ESLKEELAFLKKNHEE--EVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKl 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41322919 2337 ELAQEQARRLQEDKEQMAQQLAEETQGFQRtLEAERQRQLEMSAEAERlklRVAEMSRAQARAEEDAQRFRKQAEE 2412
Cdd:pfam00038 199 EELQQAAARNGDALRSAKEEITELRRTIQS-LEIELQSLKKQKASLER---QLAETEERYELQLADYQELISELEA 270
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1098-1262 |
9.83e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1098 TQGAEEVLRAHEEQLKEAQAvpaTLPELEATKASLKKLRAQAEAQQPTFDALRDELRGAQEVGERLQQRHGERDVEVERW 1177
Cdd:COG4913 663 VASAEREIAELEAELERLDA---SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41322919 1178 ----RERVAQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLGAWLQDARRRQEQIQAMPLADSQAVREQLRQEQA 1253
Cdd:COG4913 740 edlaRLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
....*....
gi 41322919 1254 LLEEIERHG 1262
Cdd:COG4913 820 LLDRLEEDG 828
|
|
| |
