|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1006-1117 |
1.20e-80 |
|
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: 258.06 E-value: 1.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1006 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGI 1085
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 564397587 1086 KSTLDINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1000-1118 |
3.65e-78 |
|
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: 251.92 E-value: 3.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1000 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQA 1079
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 564397587 1080 AESVGIKSTLDINEMARTERPDWQNVMLYVTAIYKYFET 1118
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1006-1117 |
3.40e-72 |
|
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: 234.92 E-value: 3.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1006 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGI 1085
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 564397587 1086 KSTLDINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1015-1116 |
9.46e-36 |
|
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: 131.31 E-value: 9.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINE 1093
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 564397587 1094 MARTE-RPDWQNVMLYVTAIYKYF 1116
Cdd:cd21200 83 MVRMGnRPDWKCVFTYVQSLYRHL 106
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1013-1116 |
4.07e-33 |
|
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: 124.01 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1013-1114 |
4.08e-31 |
|
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: 118.17 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKhADCPQLLDV 80
|
90 100
....*....|....*....|...
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYK 1114
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1018-1116 |
9.99e-30 |
|
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: 114.06 E-value: 9.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGIKSTLDINEMART 1097
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 564397587 1098 ERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1009-1116 |
1.32e-29 |
|
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: 113.78 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1009 EYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQ-AAESVGIKS 1087
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 564397587 1088 TLDINEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1013-1116 |
1.67e-29 |
|
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: 113.28 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21194 82 EDVD-VARPDEKSIMTYVASYYHYF 105
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1016-1116 |
4.04e-29 |
|
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: 111.99 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1016 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINEM 1094
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 564397587 1095 ARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1015-1114 |
1.91e-28 |
|
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: 110.56 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVG-IKSTLDINE 1093
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 564397587 1094 MARTERPDWQNVMLYVTAIYK 1114
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1013-1116 |
6.84e-28 |
|
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: 108.94 E-value: 6.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1013-1116 |
1.39e-27 |
|
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: 107.87 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21248 82 EDVN-VEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1013-1116 |
2.46e-27 |
|
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: 107.44 E-value: 2.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 564397587 1092 NEMA-RTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21258 81 EDMMiMGKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1017-1117 |
3.38e-27 |
|
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: 106.66 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1017 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINEMA 1095
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 564397587 1096 RTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1013-1116 |
6.08e-27 |
|
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: 106.10 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLDP 83
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21249 84 EDVA-VPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1013-1116 |
1.90e-26 |
|
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: 104.66 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESV-GIKSTLDI 1091
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 564397587 1092 NEMARTER-PDWQNVMLYVTAIYKYF 1116
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1014-1116 |
2.99e-26 |
|
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: 104.16 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1014 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDIN 1092
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 564397587 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1013-1117 |
7.02e-26 |
|
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: 102.94 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGIKSTLDIN 1092
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 564397587 1093 EMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1018-1116 |
1.58e-24 |
|
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: 99.16 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGIKSTLDINEMART 1097
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 564397587 1098 ERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1011-1117 |
9.32e-24 |
|
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: 97.03 E-value: 9.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1011 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTL 1089
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 564397587 1090 DINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1013-1116 |
2.01e-23 |
|
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: 95.92 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTErPDWQNVMLYVTAIYKYF 1116
Cdd:cd21189 81 EDVDVPE-PDEKSIITYVSSLYDVF 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1014-1116 |
2.12e-23 |
|
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: 96.10 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1014 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDIN 1092
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 564397587 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1015-1116 |
4.42e-23 |
|
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: 94.94 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINE 1093
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 564397587 1094 MARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1018-1114 |
7.64e-23 |
|
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: 94.03 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAA-ESVGIKSTLDINEMAr 1096
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPEDVN- 83
|
90
....*....|....*...
gi 564397587 1097 TERPDWQNVMLYVTAIYK 1114
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1013-1117 |
1.61e-22 |
|
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: 93.47 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1013-1116 |
1.29e-21 |
|
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: 91.30 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1013-1116 |
1.83e-20 |
|
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: 88.19 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1013-1116 |
2.37e-20 |
|
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: 87.82 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1013-1116 |
2.48e-20 |
|
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: 88.19 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDi 1091
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1013-1116 |
3.75e-20 |
|
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: 87.47 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1012-1117 |
5.91e-20 |
|
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: 85.94 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1012 GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 564397587 1091 INEMArTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1013-1116 |
6.56e-20 |
|
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: 85.86 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGIKSTLDIn 1092
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDA- 82
|
90 100
....*....|....*....|....
gi 564397587 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1013-1116 |
1.13e-19 |
|
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: 85.91 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1015-1118 |
2.12e-19 |
|
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: 84.65 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1015 RNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKR--NFTLAFQAAE-SVGIKSTL- 1089
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLi 83
|
90 100 110
....*....|....*....|....*....|..
gi 564397587 1090 ---DINEmarterPDWQNVMLYVTAIYKYFET 1118
Cdd:pfam00307 84 epeDLVE------GDNKSVLTYLASLFRRFQA 109
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1013-1116 |
2.98e-19 |
|
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: 84.00 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21320 82 EDIS-VDHPDEKSIITYVVTYYHYF 105
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1017-1116 |
2.43e-17 |
|
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: 78.66 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1017 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINEMa 1095
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDV- 82
|
90 100
....*....|....*....|.
gi 564397587 1096 RTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1013-1116 |
3.57e-17 |
|
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: 78.10 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAESVGIKSTLDiN 1092
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 564397587 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1016-1109 |
8.68e-17 |
|
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: 76.97 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1016 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY----QELNSQEKKRNFTLAFQAAESVGIKSTL-- 1089
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLfe 80
|
90 100
....*....|....*....|..
gi 564397587 1090 --DINEMarteRPDWQNVMLYV 1109
Cdd:smart00033 81 peDLVEG----PKLILGVIWTL 98
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1015-1114 |
5.74e-16 |
|
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: 74.68 E-value: 5.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY---QELNSQEKKRNFTLAFQAAESVGIKST--L 1089
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 564397587 1090 DINEMarTERPDWQNVMLYVTAIYK 1114
Cdd:cd00014 81 EPEDL--YEKGNLKKVLGTLWALAL 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1013-1116 |
8.91e-16 |
|
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: 73.81 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQnidITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQEKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|....*.
gi 564397587 1091 INEMARTErPDWQNVMLYVTaiykYF 1116
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLS----YF 98
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1018-1114 |
5.05e-15 |
|
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: 72.27 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKK-RNFTLAFQAAE-SVGIKSTLDINEMA 1095
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLDPEDVA 84
|
90
....*....|....*....
gi 564397587 1096 rTERPDWQNVMLYVTAIYK 1114
Cdd:cd21233 85 -TAHPDKKSILMYVTSLFQ 102
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1011-1116 |
5.95e-15 |
|
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: 71.97 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1011 GGSKRnALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTL 1089
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLL 82
|
90 100
....*....|....*....|....*..
gi 564397587 1090 DiNEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21243 83 D-PEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1013-1118 |
8.04e-15 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 79.21 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQN-IDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--EKKRNFTLAFQAAE-SVGIKST 1088
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 564397587 1089 LDINEMARTERPDWQNVMLYVTAIYKYFET 1118
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
500-816 |
1.29e-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: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 500 AENARFEREQLLGVQQH----LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQI 575
Cdd:TIGR02169 700 IENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKAQL--EKEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyr 653
Cdd:TIGR02169 780 ALNDLEARLshSRIPEIQAELSKLEE--EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-- 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 654 afQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLEREN 733
Cdd:TIGR02169 856 --IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 734 KTLHRRLREESAE------WRQFQADLQ---TAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:TIGR02169 934 SEIEDPKGEDEEIpeeelsLEDVQAELQrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
330
....*....|..
gi 564397587 805 RGRVYNYMNAVE 816
Cdd:TIGR02169 1014 KKKREVFMEAFE 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-824 |
1.37e-14 |
|
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: 78.95 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 558 ALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKS--DIQDLLESVRLDKEKAETLASSLQEDLAHTR 635
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 636 NDANRLQDTIAKVE---DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLII 712
Cdd:TIGR02168 316 RQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 713 SDLENTVKKLQDQKHDLERENKTLHRRLREESAEwrqfqadlqtavvIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKE 792
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKK-------------LEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 564397587 793 LEEIKSRKQEEERGRVynymnAVERDLAALRQ 824
Cdd:TIGR02168 463 LEELREELEEAEQALD-----AAERELAQLQA 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-802 |
4.09e-14 |
|
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: 77.40 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 501 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 580
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 581 KAQLEKEKQKVAELYS-IHNSGDKS--------DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDE 651
Cdd:TIGR02168 760 EAEIEELEERLEEAEEeLAEAEAEIeeleaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 652 YRAFQEEAKK----------QIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKK 721
Cdd:TIGR02168 840 LEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 722 LQDQKHDLE-RENKTLHRRLREESAEWRQFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLTKELEEIK 797
Cdd:TIGR02168 920 LREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAIEEYEELK 999
|
....*
gi 564397587 798 SRKQE 802
Cdd:TIGR02168 1000 ERYDF 1004
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1013-1113 |
8.77e-13 |
|
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: 65.81 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 564397587 1092 NEMARTERPDWQNVMLYVTAIY 1113
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1018-1114 |
1.07e-12 |
|
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: 65.36 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDINEMAr 1096
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPEDVA- 83
|
90
....*....|....*...
gi 564397587 1097 TERPDWQNVMLYVTAIYK 1114
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1011-1089 |
1.09e-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: 65.45 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1011 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTL 1089
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
524-805 |
1.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 524 AEQDNKEAQEMIGALKERshhmERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnSGDK 603
Cdd:COG1196 220 EELKELEAELLLLKLREL----EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-----QAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 604 SDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSELEEKETE 683
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE----LEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 RSDMKETIFELEDEVEQHRAVKLhdnliiSDLENTVKKLQDQKHDLERENKTLHRRLREESAewrqfQADLQTAVVIAND 763
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELL------EALRAAAELAAQLEELEEAEEALLERLERLEEE-----LEELEEALAELEE 435
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564397587 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-800 |
2.53e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 605 DIQDLLESVRLDKEKAETLA--SSLQEDLAHTRNDANRLQDTIAKVEDeYRAFQ--EEAKKQIEDLNMTLEKLRSELEEK 680
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRL-WFAQRrlELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 681 ETERSDMKETIFELEDEVEQHravklhDNLIISDLENTVKKLQDQKHDLERENKTLHRRLR-------EESAEWRQFQAD 753
Cdd:COG4913 315 EARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564397587 754 LQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRK 800
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
529-804 |
3.50e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 529 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdKSDIQD 608
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--------EQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 609 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMK 688
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 689 ETIFELEDEVEQHRAvklhdnliisDLENTVKKLQDQKHDLERENKTLHRRLREESAEwRQFQADLQTAVVIANDIKSEA 768
Cdd:COG1196 386 EELLEALRAAAELAA----------QLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 564397587 769 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1016-1111 |
3.85e-12 |
|
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: 63.48 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1016 NALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTyLPAHIP-YQELNSQEKKRNFTLAFQAAESVGIKSTLDINEM 1094
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 564397587 1095 ArteRPDWQN--VMLYVTA 1111
Cdd:cd21185 80 A---DPEVEHlgIMAYAAQ 95
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1013-1116 |
8.92e-12 |
|
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: 62.93 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLEP 84
|
90 100
....*....|....*....|....*
gi 564397587 1092 NEMARTErPDWQNVMLYVTAIYKYF 1116
Cdd:cd21244 85 EDVDVVN-PDEKSIMTYVAQFLQYS 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
568-822 |
1.41e-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: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 568 ATVASDQIEMNRLKAQLEKEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQD 643
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIID--EKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 644 TIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDM--------KETIFELEDEVEQHRAVKLHDNLIISDL 715
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 716 ENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKE 792
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|....*....
gi 564397587 793 LEEIK---------SRKQEEERGRVYNYMNAVERDLAAL 822
Cdd:TIGR02169 401 INELKreldrlqeeLQRLSEELADLNAAIAGIEAKINEL 439
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
530-805 |
1.93e-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: 68.56 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 530 EAQEMIGALK-ERSHHMERIIESEQKGKAALAAtLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSihnsgDKSDIQD 608
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-----DLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 609 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIA-----KVEDEYRAFQEEAKKQ----------IEDLNMTLEKL 673
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 674 RSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQAD 753
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 754 LQTAVVIANDIK---SEAQEEIGDLKRRLHEAQEKNEKlTKELEEIKSRKQEEER 805
Cdd:TIGR02169 912 IEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
178-826 |
1.98e-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: 68.54 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 178 KAALEAKVKDLLTLaktkdvEILHLRNELRDMRAQLGISEDHCEGEDR----SEEKETIIAHQPTDVESTLLQLQEQNTA 253
Cdd:TIGR02168 219 KAELRELELALLVL------RLEELREELEELQEELKEAEEELEELTAelqeLEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 254 IREELNQLKNENRMLKDRLNALGFSLEQRLDNSEKLfgyqslspeitpGNQSDGggtltssvegsapgSVEDLLSQDENT 333
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEEL------------ESKLDE--------------LAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 334 LMAHQHSNSMDNLDSECSEVYQPLTSSDDALDAPSSSESEGVPSIER---------SRKGSSGNASEVSVACLTERIHQM 404
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiaslnneiERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 405 EENQHSTseELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhhisyvidedv 484
Cdd:TIGR02168 427 LKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS----------- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 485 ksgrYMELEQRYMDLAENARF---EREQLLGVQQHLSNTLKMAEQDNKEAQEMIGA-----LKERSHHMERIIESEQKGK 556
Cdd:TIGR02168 494 ----LERLQENLEGFSEGVKAllkNQSGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 557 AALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKSdIQDLLESVR-----------LDKEKAETLAS 625
Cdd:TIGR02168 570 LGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA-LSYLLGGVLvvddldnalelAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 626 SLQEDLAH------------------TRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSELEEKETER 684
Cdd:TIGR02168 649 TLDGDLVRpggvitggsaktnssileRRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 685 SDMKETIFELEDEVEQHRAVKLHDNLIISDLEN---------------------TVKKLQDQKHDLERENKTLHRRLREE 743
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAeieeleerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 744 SAEWRQFQADLQTAVVIANDI---KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKS--RKQEEERGRVYNYMNAVERD 818
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEEliEELESELEALLNERASLEEA 888
|
....*...
gi 564397587 819 LAALRQGM 826
Cdd:TIGR02168 889 LALLRSEL 896
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1016-1109 |
3.24e-11 |
|
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: 61.93 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1016 NALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIP----------------------------------- 1060
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 1061 -YQELNSQEkKRNFTLAFQAAESVGikstlDINEMARTE-----RPDWQNVMLYV 1109
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELG-----GVPALLRASdmsntIPDEKVVILFL 130
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
397-823 |
5.99e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.99 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDehhi 476
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 syviDEDVKSGrymELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALK--------ERSHHMERI 548
Cdd:PRK02224 402 ----DAPVDLG---NAEDFLEELRE----ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 549 IESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQkvaelysihnsgdksdiqdlLESVRLDKEKAETLASSLQ 628
Cdd:PRK02224 471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------------------IERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 629 EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLnmtlEKLRSELEEKETERSDMKETIFELEDEVEQHRAvklhd 708
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA----- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 709 nliISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAvviandikseaqeeigdlkrRLHEAQEKNEK 788
Cdd:PRK02224 601 ---IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA--------------------RIEEAREDKER 657
|
410 420 430
....*....|....*....|....*....|....*..
gi 564397587 789 LTKELEEI--KSRKQEEERGRVYNYMNAVERDLAALR 823
Cdd:PRK02224 658 AEEYLEQVeeKLDELREERDDLQAEIGAVENELEELE 694
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1017-1116 |
6.29e-11 |
|
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: 60.19 E-value: 6.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1017 ALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQEKKRNFTLAFQAA-ESVGIKSTLDINEMA 1095
Cdd:cd21245 7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLEPEDVM 85
|
90 100
....*....|....*....|.
gi 564397587 1096 rTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21245 86 -VDSPDEQSIMTYVAQFLEHF 105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-826 |
2.26e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 399 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFGRQIEYFRSLLDEHhiSY 478
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 479 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 554
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 555 GKAALAATLEEYKatvasdqiEMNRLKAQLEKEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 634
Cdd:PRK03918 353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 635 RNDANRLQDTIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERS------- 685
Cdd:PRK03918 418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 686 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDLERENKTLHR 738
Cdd:PRK03918 498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 739 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 800
Cdd:PRK03918 578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
|
490 500
....*....|....*....|....*.
gi 564397587 801 QEEERGRVYNYMNAVERDLAALRQGM 826
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAEL 682
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-805 |
2.93e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 610 LESVRLDKEKAE---TLASSLQE-DLAHTRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSELEEKET 682
Cdd:COG1196 202 LEPLERQAEKAEryrELKEELKElEAELLLLKLRELEAELEELEAELEELEaelEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 683 ERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIAN 762
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564397587 763 DIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-749 |
3.06e-10 |
|
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: 64.69 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmesLCQQSDKLEHFGRQIEYFRSLLDEHHI 476
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 SYVIDEDVKSGRYMELEQRYMDLAENARfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK 556
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 557 AALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYS--IHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 634
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESelEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 635 RNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLN----MTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLhdnL 710
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL---A 990
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564397587 711 IISDLENTVKKLQD---QKHDLERENKTLHRRLREESAEWRQ 749
Cdd:TIGR02168 991 AIEEYEELKERYDFltaQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
413-825 |
2.52e-09 |
|
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: 61.62 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 413 EELQATLQELADLQQITQELNSENERLGEEKvilmeslcqqsdklehfgRQIEYFRSLLDEHhisyvidEDVksgRYMEL 492
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRER------------------EKAERYQALLKEK-------REY---EGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 493 EQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQkgkAALAATLEEYKATVAS 572
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 573 --DQIEMNRLKAQ-LEKEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVE 649
Cdd:TIGR02169 306 leRSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 650 DEYRAFQEEakkqiedlnmtLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDL 729
Cdd:TIGR02169 385 DELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 730 ERENKTLHRRLREESAewrqfqadlqtavviandIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVY 809
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAA------------------DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410
....*....|....*.
gi 564397587 810 NYmnAVERDLAALRQG 825
Cdd:TIGR02169 509 GR--AVEEVLKASIQG 522
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
670-807 |
3.16e-09 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 61.03 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 670 LEKLRSELEEKETERSDMKETIFELEDEVEQHRavklhdnliISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQ 749
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEE---------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 564397587 750 FQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:COG2433 453 ARSEERREIRKDREISRL-DREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
621-824 |
2.10e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 621 ETLASSLQEDLAH---TRNDANRLQDTIAKVEDEYRAFQEEakkqIEDLNMTLEKLRSELEEKETERSDMKETIFELEDE 697
Cdd:PRK02224 212 ESELAELDEEIERyeeQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 698 VEQHRAvKLHDNLIISDLEN-TVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE------ 770
Cdd:PRK02224 288 LEELEE-ERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaa 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 771 ----EIGDLKRRLHEAQEKNEKLTKELEEIKSR--KQEEERGRVYNYMNAVERDLAALRQ 824
Cdd:PRK02224 367 elesELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRE 426
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
524-805 |
2.49e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 524 AEQDNKEAQEMIGALKERSHHMERiieseqkgkaaLAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdK 603
Cdd:PRK02224 232 ARETRDEADEVLEEHEERREELET-----------LEAEIEDLRETIAETEREREELAEEVRDLRERLEEL--------E 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 604 SDIQDLLESVRLDKEKAETLA----------SSLQEDLAHTR-------NDANRLQDTIAKVEDEYRAFQEEAkkqiEDL 666
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEarreeledrdEELRDRLEECRvaaqahnEEAESLREDADDLEERAEELREEA----AEL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 667 NMTLEKLRSELEEKETERSDMKETIFELEDEVE----QHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLH--RRL 740
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaEAL 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564397587 741 REESA--EWRQFQADLQTAVVIAndiksEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:PRK02224 449 LEAGKcpECGQPVEGSPHVETIE-----EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-809 |
2.77e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 413 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDEdvKSGRYMEL 492
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE--LPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 493 EQRYMDLAEnARFEREQLLGVQQHLSNTLKMAEQDNKEA--QEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATV 570
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEE-LEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 571 asDQIEMNRLKAQLEKEKQKVAELYSIHN-----SGDKSDIQDLLESV----------------RLDKEKAETLASSLQE 629
Cdd:COG4717 230 --EQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIagvlflvlgllallflLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 630 DLAHTRNDANRLQdtIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSdmketifELEDEVEQHRAVKLHDN 709
Cdd:COG4717 308 QALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 710 LIISDLENTVKKLQ--DQKHDLERENKTLHRRLREESAEWRQFQADLQtavviandiKSEAQEEIGDLKRRLHEAQEKNE 787
Cdd:COG4717 379 AGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELE 449
|
410 420
....*....|....*....|..
gi 564397587 788 KLTKELEEIKSRKQEEERGRVY 809
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-830 |
2.88e-08 |
|
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: 58.14 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 631 LAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---------------------QIEDLNMTLEKLRSELEEKETERSDMKE 689
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 690 TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTA---VVIANDIKS 766
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELA 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564397587 767 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGrvynyMNAVERDLAALRQGMGLSR 830
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLN 399
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
507-804 |
4.82e-08 |
|
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: 4.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 507 REQLLGVQQHLSNtLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEk 586
Cdd:TIGR04523 193 KNKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 587 EKQKVAELYSIHNSGDKSDIQDL-LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEdeyrafqeeakKQIED 665
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNN-----------KIISQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 666 LNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESA 745
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564397587 746 EWRQF---QADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELE----EIKSRKQEEE 804
Cdd:TIGR04523 420 EKELLekeIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrSINKIKQNLE 485
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
500-700 |
9.58e-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: 55.54 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 500 AENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKErshhMERIIESEQKGKAALAATLEEYKATVASDQIEMNR 579
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 580 LKAQLEKEKQKVAE-LYSIHNSGDKSDIQDLLES----------------VRLDKEKAETLASSLQEdLAHTRNDANRLQ 642
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPedfldavrrlqylkylAPARREQAEELRADLAE-LAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564397587 643 DTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQ 700
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-697 |
1.07e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 344 DNLDSECSEVYQPLTSSDDALDAPSSSESEGVPSIERSRKgssgnasevsvaclteRIHQMEENQHSTSEE-------LQ 416
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----------------EIEQLEQEEEKLKERleeleedLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 417 ATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL-EHFGRQIEYFRSLLDEHHISYvidedvkSGRYMELEQR 495
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRI-------EARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 496 ymdlaENARFEREQLLgvqqhlsntlkmaEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATV----- 570
Cdd:TIGR02169 821 -----LNRLTLEKEYL-------------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdles 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 571 --ASDQIEMNRLKAQLEKEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN---------DAN 639
Cdd:TIGR02169 883 rlGDLKKERDELEAQLRELERKIEEL--------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeeelSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564397587 640 RLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLrSELEEK----ETERSDMKETIFELEDE 697
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKraklEEERKAILERIEEYEKK 1015
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1013-1110 |
1.07e-07 |
|
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: 50.84 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1013 SKRNALLKWCQKKTEGyqnIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQEKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|
gi 564397587 1091 INEMArTERPDWQNVMLYVT 1110
Cdd:cd21230 78 PEEII-NPNVDEMSVMTYLS 96
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
603-804 |
1.07e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 603 KSDIQDLLESVRLDK--EKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEeAKKQIEDLNMTLEKLRSELEEK 680
Cdd:COG4717 36 KSTLLAFIRAMLLERleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 681 ETERSDMKETI--FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAV 758
Cdd:COG4717 115 REELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564397587 759 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
397-802 |
1.18e-07 |
|
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: 56.27 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 458
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 459 HFGRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 525
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 526 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLEKEKQKVAELYSIHNsgdksd 605
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 606 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKEte 683
Cdd:pfam05483 496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-- 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 rSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdLERENKTLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:pfam05483 573 -ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
410 420 430
....*....|....*....|....*....|....*....
gi 564397587 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
400-779 |
1.25e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 400 RIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmeslcqqsdkLEHFGRQIEyfrslldehhisyv 479
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--------------LEELELELE-------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 480 idedVKSGRYMELEQRYMDLAENARFEREQLlgvqQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAAL 559
Cdd:COG1196 285 ----EAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 560 AATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN 639
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 640 RLQDTIA--KVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE- 716
Cdd:COG1196 426 LEEALAEleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEg 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 717 -NTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVV-IANDIKSEAQEEIGDLKRRL 779
Cdd:COG1196 506 fLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnIVVEDDEVAAAAIEYLKAAK 570
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
522-805 |
1.76e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 522 KMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATvASDQIEMNRLKAQLEKEKQKVAELYSIHNSG 601
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 602 DKSDIQDLLESVRLDKE--KAETLASSLQEDLAHTRNDANRLQ--DTIAKVEDEYRAfqEEAKKQIEDLNMTLEKLRsEL 677
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKA--EEAKKAEEDKNMALRKAE-EA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 678 EEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISD---LENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADL 754
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564397587 755 QTAVVIANDIKSEAQEEIGDlKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
650-795 |
3.07e-07 |
|
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: 52.62 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 650 DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAV---------KLHDNLIISDLENTVK 720
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARikkyeeqlgNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 721 KLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 795
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
416-804 |
5.36e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 416 QATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDE---------DVKS 486
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 487 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHM---ERIIESEQKGKAALAATL 563
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkEQIHLQETRKKAVVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 564 EEYK---------------ATVASDQIEMN--RLKAQLEKEKQKVAELYSIHNSGdksdiQDLLESVRLDKEKAETLASS 626
Cdd:TIGR00618 497 LELQeepcplcgscihpnpARQDIDNPGPLtrRMQRGEQTYAQLETSEEDVYHQL-----TSERKQRASLKEQMQEIQQS 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 627 LQ----------EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKE------T 690
Cdd:TIGR00618 572 FSiltqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalhaL 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 691 IFEL--EDEVEQHRAVKLHDNLIISDLENTVKKLQDQ-------KHDLERENKTLHRRLREESAEWRQFQaDLQTAVVIA 761
Cdd:TIGR00618 652 QLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEkeqltywKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 564397587 762 ndiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:TIGR00618 731 ---GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
379-691 |
6.58e-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: 53.59 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 379 ERSRKGSSGNASEVsvacltERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLG-EEKVILMESLCQQSDKL 457
Cdd:pfam17380 299 ERLRQEKEEKAREV------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 458 EhFGRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaENARFEREQLLGVQQhlsntlKMAEQDNKEAQEMIGA 537
Cdd:pfam17380 373 E-ISRMRELERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQ------IRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 538 LKERSHHMERIIESEQKGKAALaatleeykATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKSDIQDLLESVRLDK 617
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 618 EKAETLASSLQEdlahtRNDANRLQDTIAKVEDEYRAFQE-EAKKQIEDLNMTLEKLRSELEEKETERSDMKETI 691
Cdd:pfam17380 513 RKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-703 |
7.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 465 EYFRSL-LDEHHISYVIDEDVKS-GRYMELEQRymdlAENARFEREQLLGVQQHLSntlkmAEQDNKEAQEMIGALKERS 542
Cdd:COG4913 211 DFVREYmLEEPDTFEAADALVEHfDDLERAHEA----LEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 543 HHMERiieseQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIH--NSGD-----KSDIQDL---LES 612
Cdd:COG4913 282 RLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgNGGDrleqlEREIERLereLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 613 VRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIF 692
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250
....*....|.
gi 564397587 693 ELEDEVEQHRA 703
Cdd:COG4913 437 NIPARLLALRD 447
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
620-949 |
8.34e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 620 AETLASSLQEDLAHTRNDANRLQDTIAKVEDEYrafqEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVE 699
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 700 QH--------RAVKLHDNLIIS-DLENTVKKLQDQKHDLERENKTLhRRLREESAEWRQFQADLQTAVVIANDIKSEAQE 770
Cdd:COG3883 90 ERaralyrsgGSVSYLDVLLGSeSFSDFLDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 771 EIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFD 850
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 851 SASQVPNAAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPVSTSKPLTALSDKRSNYGEIPGQEHLLRTSSTSRPASL 930
Cdd:COG3883 249 AGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASA 328
|
330
....*....|....*....
gi 564397587 931 PRVPAMESAKTISVSRRSS 949
Cdd:COG3883 329 GGGGGSGGGGGSSGGGSGG 347
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-792 |
8.54e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 360 SDDALDAPSSSESEGVPSIERSRKgssgnASEVSVACLTERIHQMEENQHSTSEEL----QATLQELADLQQITQELNSE 435
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKK-----AEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 436 NERLGEEKVILMESLcqqsDKLEHFGRQIEYFRSLLDEHHISyviDEDVKSgrymELEQRYMDLAENARFEREQllgvqQ 515
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKK---AEELKK----AEEENKIKAAEEAKKAEED-----K 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 516 HLSNTLKMAEQDNKEAQEMIGALKERSHHMERI--IESEQKGKAalaatlEEYKATVASDQIEMNRLKAQLEKEKQKVAE 593
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkKEAEEKKKA------EELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 594 LYSihNSGDKSDIQDLLE-----SVRLDKEKAETLASSLQEDLAHTRNDANRlqdTIAKVEDEYRAFQEEAKKQIEDLNM 668
Cdd:PTZ00121 1749 AKK--DEEEKKKIAHLKKeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIND 1823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 669 TLEKLRSELEEKeterSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLEREnktlhrrlREESAEWR 748
Cdd:PTZ00121 1824 SKEMEDSAIKEV----ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE--------IEEADEIE 1891
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 564397587 749 QFQADLQTAVVIANDIKSEAQEEIGD-------LKRRLHEAQEKNEKLTKE 792
Cdd:PTZ00121 1892 KIDKDDIEREIPNNNMAGKNNDIIDDkldkdeyIKRDAEETREEIIKISKK 1942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
618-823 |
8.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 618 EKAETLASSLQEDLAHTRNDANRLQDTIAKVED------EYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKET- 690
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENieelikEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELk 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 691 --IFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLhRRLREESAEWRQFQADLQTAVVIANDIKSEA 768
Cdd:PRK03918 238 eeIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564397587 769 ---QEEIGDLKRRLHEAQEKN---EKLTKELEEIKSRKQE-EERGRVYNYMNAVERDLAALR 823
Cdd:PRK03918 317 srlEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEElEERHELYEEAKAKKEELERLK 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
571-799 |
1.10e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 571 ASDQIEmnRLKAQLEKEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLahtrnDANRLQDTIAKVED 650
Cdd:COG4913 608 NRAKLA--ALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 651 EYRAFQ------EEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAV-----------------KLH 707
Cdd:COG4913 676 ELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelralleERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 708 DNLIISDLENTVKK-LQDQKHDLERENKTLHRRLREE----SAEWRQFQADLQTAV-----------VIANDIKSEAQEE 771
Cdd:COG4913 756 AAALGDAVERELREnLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLeslpeylalldRLEEDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 564397587 772 igdLKRRLHEAQEK-----NEKLTKELEEIKSR 799
Cdd:COG4913 836 ---FKELLNENSIEfvadlLSKLRRAIREIKER 865
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
657-826 |
1.18e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.84 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 657 EEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRavklhdnliisdlentvKKLQDQKHDLERENKTL 736
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLR-----------------EELEEKLEELEEEKEEI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 737 HRRLREEsaewrqfqadlqtavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE-EERGRVYNYMNAV 815
Cdd:COG1193 566 LEKAREE-----------------AEEILREARKEAEELIRELREAQAEEEELKEARKKLEELKQElEEKLEKPKKKAKP 628
|
170
....*....|.
gi 564397587 816 ERDLAALRQGM 826
Cdd:COG1193 629 AKPPEELKVGD 639
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
558-748 |
1.27e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 558 ALAATLEEYKAtvasdqiemnrLKAQLEKEKQKVAELYSIhnsgdksdiqdllESVRLDKEKAETLASSLqEDLAHTRND 637
Cdd:COG2433 337 ALAAALKAYDA-----------YKNKFERVEKKVPPDVDR-------------DEVKARVIRGLSIEEAL-EELIEKELP 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 638 ANRlqDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEV-----EQHRAVKLHDNliI 712
Cdd:COG2433 392 EEE--PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELsearsEERREIRKDRE--I 467
|
170 180 190
....*....|....*....|....*....|....*.
gi 564397587 713 SDLENTVKKLQDQKHDLERENKTLHRRLREESAEWR 748
Cdd:COG2433 468 SRLDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-803 |
1.96e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 398 TERIHQMEENQHSTSEELQATLQELADLQQITQELN--SENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhh 475
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 476 iSYVIDEDVKSGRYmELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKG 555
Cdd:COG4717 165 -LEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 556 K-----------AALAATLEEYKATVASDQIE------------------MNRLKAQLEKEKQKVAELYSIHNsGDKSDI 606
Cdd:COG4717 243 ErlkearlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEE-LEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 607 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD-----TIAKVEDEYRAFQEEAK-KQIEDLNMTLEKLRsELEEK 680
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEEleeelQLEELEQEIAALLAEAGvEDEEELRAALEQAE-EYQEL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 681 ETERSDMKETIFELEDEVEQhravkLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADlqtavvi 760
Cdd:COG4717 401 KEELEELEEQLEELLGELEE-----LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED------- 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564397587 761 anDIKSEAQEEIGDLKRRLHEAQEKN-------EKLTKELEEIKSRKQEE 803
Cdd:COG4717 469 --GELAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPP 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
379-823 |
2.35e-06 |
|
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: 51.99 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 379 ERSRKGSSGNASEVSVACLTERIHQM-EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL 457
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 458 EHFGRQIEYFRSLLDEHHISYVIDEDVksgrYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGA 537
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 538 LKERSHHMERI---IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQkvaELYSIHNsgDKSDIQDLLESVR 614
Cdd:TIGR02169 415 LQRLSEELADLnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE--EYDRVEKELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTI----------AKVEDEYRAFQE----------------EAKKQIEDLN- 667
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKr 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 668 -----MT---LEKLRSELEEKETERS----DMKETIFELEDEVEQHRAVKLHDNLIISDLEnTVKKLQDQ---------- 725
Cdd:TIGR02169 570 rkagrATflpLNKMRDERRDLSILSEdgviGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIE-AARRLMGKyrmvtlegel 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 726 ---------KHDLERENKTLHRRLREESAEWR--------------QFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEA 782
Cdd:TIGR02169 649 feksgamtgGSRAPRGGILFSRSEPAELQRLRerleglkrelsslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564397587 783 QEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALR 823
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEI-----ENVKSELKELE 764
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
397-732 |
2.98e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILmeSLCQQSDKLEHFGRQIEYFRSLLDEhhi 476
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC--PVCGRELTEEHRKELLEEYTAELKR--- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 syvIDEDVKsgrymELEQRYMDLAENARfEREQLLGVQQHLSNTLKMAEQ--------------DNKEAQEMIGALKERS 542
Cdd:PRK03918 464 ---IEKELK-----EIEEKERKLRKELR-ELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 543 HHME---RIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKE--------KQKVAELYSIHN-----SGDKSDI 606
Cdd:PRK03918 535 IKLKgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNeylelKDAEKEL 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 607 QDLLEsvRLDKEKAETLASSlqEDLAHTRNDANRLQdtiAKVEDEYRAFQEEAKKQIEDLNMTLEK----LRSELEEKET 682
Cdd:PRK03918 615 EREEK--ELKKLEEELDKAF--EELAETEKRLEELR---KELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEK 687
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 564397587 683 ERSDMKETIFELEDEVEQHRAVKLHDNLI---ISDLENTVKKLQDQKHDLERE 732
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKELEKLekaLERVEELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
616-805 |
3.35e-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: 50.53 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 616 DKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQE---EAKKQIEDLNMTLEKLRSELEEKETERSDMKETIF 692
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 693 ELEDEVEQhRAVKLHDN-------LIIS--DLENTVKKLQDQKHdLERENKTLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:COG4942 101 AQKEELAE-LLRALYRLgrqpplaLLLSpeDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564397587 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-805 |
4.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 659 AKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLII--SDLENTVKKLQDQKHDLERENKTL 736
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564397587 737 hRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG4913 688 -AALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
620-882 |
4.89e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 620 AETLASSLQEDLAHTRNDANR------------LQDTIAKVEDEYRAFQEeaKKQIEDLNMTLEKLRSELEEKETERSDM 687
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARkalefleeqlpeLRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 688 KETIFELEDEVEQHRAVKLHDNLIISDLEN--TVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTavvIANDIK 765
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA---LRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 766 SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSR-KQEEERGRVYNymnAVERDLAALRQGMG--LSRRSSTSSEptptv 842
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAELR---RLEREVEVARELYEslLQRLEEARLA----- 380
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 564397587 843 ktliksfdSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVS 882
Cdd:COG3206 381 --------EALTVGNVRVIDPAVVPLKPVSPKKLLILALG 412
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
597-820 |
5.05e-06 |
|
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: 50.79 E-value: 5.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 597 IHNSGDKSDIQDLLESVRLDKEKAE-TLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAK---KQIEDLNMTLEK 672
Cdd:TIGR04523 70 INNSNNKIKILEQQIKDLNDKLKKNkDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKenkKNIDKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 673 LRSELEEKETERSDMKETIFELEDE--------------VEQHRAVKLHDNLIISDLENTVKK---LQDQKHDLERENKT 735
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENElnllekeklniqknIDKIKNKLLKLELLLSNLKKKIQKnksLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 736 LHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEK---LTKELEEIKSRKQEEERGRVYNYM 812
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKikeLEKQLNQLKSEISDLNNQKEQDWN 309
|
....*...
gi 564397587 813 NAVERDLA 820
Cdd:TIGR04523 310 KELKSELK 317
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
576-805 |
5.09e-06 |
|
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: 50.79 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKAQLEKEKQKVA----ELYSIHNSGDKS-----DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIA 646
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDkfltEIKKKEKELEKLnnkynDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 647 KVE---DEYRAFQ---EEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEvEQHRAVKLHD--------NLII 712
Cdd:TIGR04523 205 NLKkkiQKNKSLEsqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEkqkeleqnNKKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 713 SDLENTVKKLQDQKHDLERE-NKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTK 791
Cdd:TIGR04523 284 KELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
250
....*....|....
gi 564397587 792 ELEEIKSRKQEEER 805
Cdd:TIGR04523 364 ELEEKQNEIEKLKK 377
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
576-810 |
5.43e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKaqlekeKQKVAELYSihnsgdksDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIakveDEYRAF 655
Cdd:PHA02562 167 EMDKLN------KDKIRELNQ--------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKY----DELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 656 QEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQ-HRAVKLH-DNLI-------ISDLENTVKKLQDQK 726
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfQKVIKMYeKGGVcptctqqISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 727 HDL---------------ERENK--TLHRRLREESAEWRQFQADLQTAVVIANDIKSE---AQEEIGDLKRRLHEAQEKN 786
Cdd:PHA02562 309 KELqhslekldtaideleEIMDEfnEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDEL 388
|
250 260
....*....|....*....|....
gi 564397587 787 EKLTKELEEIKsrKQEEERGRVYN 810
Cdd:PHA02562 389 DKIVKTKSELV--KEKYHRGIVTD 410
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
539-679 |
7.93e-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: 48.38 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 539 KERSHHMERIIESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAE----LYSIHNSGDKSDIQDLLESVR 614
Cdd:COG1579 24 HRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqLGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEE 679
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
389-802 |
9.21e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 389 ASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFR 468
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 469 SLLDEHH---ISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSN-----TLKMAEQDNKEAQEMIGALKE 540
Cdd:COG1196 435 EEEEEEEealEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaarlLLLLEAEADYEGFLEGVKAAL 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 541 RSHHMERIIES---EQKGKAALAATLEEYKATVASDQIEMNRLKAQ-----LEKEKQKVAELYSIHNSGDKSDIQDLLES 612
Cdd:COG1196 515 LLAGLRGLAGAvavLIGVEAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 613 VRLDkEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAF---------QEEAKKQIEDLNMTLEKLRSELEEKETE 683
Cdd:COG1196 595 GAIG-AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALrravtlagrLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 RSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 564397587 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTK-------ELEEIKSRKQE 802
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGPvnllaieEYEELEERYDF 799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-755 |
9.44e-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: 50.12 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 161 EGDIRMSKSKSDNQIsdKAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGISEDHCEG-EDRSEEKETIIAHQPTD 239
Cdd:pfam15921 244 EDQLEALKSESQNKI--ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 240 VESTLLQLqeqntaiREELNQLKnenRMLKDRLNALGFSLEqrLDNSEklfgyqsLSPEITPGNQ-SDGGGTLTSSVEGS 318
Cdd:pfam15921 322 LESTVSQL-------RSELREAK---RMYEDKIEELEKQLV--LANSE-------LTEARTERDQfSQESGNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 319 APG----SVEDLLSQDENTLMAHQ---HSNSMDNLDSECSEVYQPLTSSDDALDApSSSESEGvpSIERSRKGSSG-NAS 390
Cdd:pfam15921 383 LADlhkrEKELSLEKEQNKRLWDRdtgNSITIDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNES 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 391 EVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFGRQIEYFRSL 470
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 471 ldehhisyvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIE 550
Cdd:pfam15921 526 ---------VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVG 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 551 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---- 625
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdi 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 626 -----SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEE-----KETERSD---MKETIf 692
Cdd:pfam15921 652 kqerdQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntlKSMEGSDghaMKVAM- 730
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564397587 693 ELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQ 755
Cdd:pfam15921 731 GMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE 793
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
399-805 |
1.02e-05 |
|
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: 50.05 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 399 ERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISY 478
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 479 VIDE-------DVKSGRYMELEQRYM------------DLAENARFEREQL-------LGVQQHLSNTLKMAEQDNKEAQ 532
Cdd:TIGR00606 378 ELDGfergpfsERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQAdeirdekKGLGRTIELKKEILEKKQEELK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 533 EMIGALKERSHHMERIIESEQKGKAALA--------ATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKS 604
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERelskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 605 -----DIQDLLESVRLDKEKAETLASSLQEDLAHTRndanRLQDTIAKVEDEYRAFQE---EAKKQIEDLNMTLEKLRSE 676
Cdd:TIGR00606 538 emltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK----QLEDWLHSKSKEINQTRDrlaKLNKELASLEQNKNHINNE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 677 LEEKETERSDMKETIFE-------------LEDEVEQHRavklHDNLIISDLENTVKKLQDQKHDLERENKTLHRRLREE 743
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsqdeesdlerLKEEIEKSS----KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 744 SAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRR---------------------LHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlglapgrqsiidlkekeIPELRNKLQKVNRDIQRLKNDIEE 769
|
...
gi 564397587 803 EER 805
Cdd:TIGR00606 770 QET 772
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
615-824 |
1.48e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 48.95 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYR--AFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIF 692
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRqnAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 693 ELEDEVEqhravklhdnliiSDLENTVKKLQDQKHDLERENK-TLHRRLREESAEWRQFqadlqtavviandiKSEAQEE 771
Cdd:pfam03528 93 EAIDEVK-------------SQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQY--------------RESAERE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564397587 772 IGDLKRRLHEAQEKnEKLTKELeeiksRKQEEERGRVYNYMNAVERDLAALRQ 824
Cdd:pfam03528 146 IADLRRRLSEGQEE-ENLEDEM-----KKAQEDAEKLRSVVMPMEKEIAALKA 192
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
578-803 |
1.87e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 578 NRLKAQLEKEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEdlahtrndanrlqdtiakvedeYRAFQE 657
Cdd:PRK00409 505 EEAKKLIGEDKEKLNEL-----------IASLEELERELEQKAEEAEALLKE----------------------AEKLKE 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 658 EAKKQIEDLNMTLEKLRSELEEK-----ETERSDMKETIFEL-EDEVEQHRAVKLHDnliisdlentvkkLQDQKHDLER 731
Cdd:PRK00409 552 ELEEKKEKLQEEEDKLLEEAEKEaqqaiKEAKKEADEIIKELrQLQKGGYASVKAHE-------------LIEARKRLNK 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 732 ENKTLHRRLREESAEWRQFQA--------DLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEknEKLTKELEEIKSRKQEE 803
Cdd:PRK00409 619 ANEKKEKKKKKQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAGIMKMKVPLSDL--EKIQKPKKKKKKKPKTV 696
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
576-826 |
2.02e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKA-QLEKEKQKVAElySIHNSGdKSDIQDLLESVRLDK-EKAETLASSLQEDLAHTRNDANrLQDTIAKVEDEYR 653
Cdd:PRK05771 5 RMKKVLIvTLKSYKDEVLE--ALHELG-VVHIEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLP-KLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 654 AFQEEakKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQhraVKlhdnlIISDLENTVKKLQDQKHdLEREN 733
Cdd:PRK05771 81 VKSLE--ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER---LE-----PWGNFDLDLSLLLGFKY-VSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 734 KTLHRRLREES-AEWRQFQADLQT--------AVVIANDIKSEAQEEI-------------GDLKRRLHEAQEKNEKLTK 791
Cdd:PRK05771 150 GTVPEDKLEELkLESDVENVEYIStdkgyvyvVVVVLKELSDEVEEELkklgferleleeeGTPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564397587 792 ELEEIKSR------KQEEERGRVYNYM-NAVERDLAALRQGM 826
Cdd:PRK05771 230 ERESLLEElkelakKYLEELLALYEYLeIELERAEALSKFLK 271
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
168-837 |
2.33e-05 |
|
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: 48.89 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 168 KSKSDNQISdKAALEAKVKDLLTLAKTKDVEILHLRNEL----RDMRAQLGISEDHCEGEDRSEEKETIIAHQPTDVEST 243
Cdd:TIGR00606 342 KTELLVEQG-RLQLQADRHQEHIRARDSLIQSLATRLELdgfeRGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 244 LLQLQEQNTAIReelnqlknenrmlkDRLNALGFSLEQRldnSEKLFGYQS-LSPEITPGNQSDGGGTLTSSVEGSAPGS 322
Cdd:TIGR00606 421 ERLKQEQADEIR--------------DEKKGLGRTIELK---KEILEKKQEeLKFVIKELQQLEGSSDRILELDQELRKA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 323 VEDLLSQDENTLMA-------HQHSNSMDNLDSECSEVYQ--PLTSSDDALDAPSSSESEGVPSIERSRKGSSGNASE-V 392
Cdd:TIGR00606 484 ERELSKAEKNSLTEtlkkevkSLQNEKADLDRKLRKLDQEmeQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDElT 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 393 SVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQiEYFRSLLD 472
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 473 EhhisyvIDEDVKSGRymelEQRYMDLAENARFER--EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 550
Cdd:TIGR00606 643 R------LKEEIEKSS----KQRAMLAGATAVYSQfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 551 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELySIHNSGDKSDIQD---LLESVRLDKEKAETLASSL 627
Cdd:TIGR00606 713 STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKV-NRDIQRLKNDIEEqetLLGTIMPEEESAKVCLTDV 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 628 qedlahtrNDANRLQDTIAKVEDEYRafQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFEL----EDEVEQHRA 703
Cdd:TIGR00606 792 --------TIMERFQMELKDVERKIA--QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNrkliQDQQEQIQH 861
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 704 VKLHDN------LIISDLENTVKKLQDQKHDLERENKTLHRRL---REESAEWRQFQADLQT----AVVIANDIKSEAQE 770
Cdd:TIGR00606 862 LKSKTNelksekLQIGTNLQRRQQFEEQLVELSTEVQSLIREIkdaKEQDSPLETFLEKDQQekeeLISSKETSNKKAQD 941
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 771 EIGDLKRRLHEAQEKNEKLTKELEEIKSR---KQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSE 837
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGKDDylkQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-800 |
2.70e-05 |
|
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: 48.48 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 517 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVaelys 596
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL----- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 597 ihnsgdkSDIQDLLESVRLDKEKaetlassLQEDLAHTRNDANRLQDTIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSE 676
Cdd:TIGR04523 471 -------KVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 677 LEEKETERSDMKETIFELEDEV--EQHRAVKLHDNLIISDLENTVKKlqdqkhdLERENKTLHRRLREESAEwrqfqadl 754
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKS-------LKKKQEEKQELIDQKEKE-------- 597
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564397587 755 qtavviANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKELEEIKSRK 800
Cdd:TIGR04523 598 ------KKDLIKEIEEkekKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
399-805 |
3.50e-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: 48.18 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 399 ERIHQMEENQHSTSEELQATLQE----LADLQQITQELNSENERLG---EEKVILMESLCQQSDKLEHFGRQIEYFRSLL 471
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKVSlklEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 472 DEHHISYVIDEDVKSGRYMELEQRYMDL----------AENARFEREQLLGVQ----QHLSNTLKmAEQDNKEaqemiga 537
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqAENARLEMHFKLKEDhekiQHLEEEYK-KEINDKE------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 538 lKERSHHMERIIESEQKGKAaLAATLEEYKATV----ASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKS--------- 604
Cdd:pfam05483 240 -KQVSLLLIQITEKENKMKD-LTFLLEESRDKAnqleEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 605 DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEE-- 679
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEmt 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 680 -----KETERSDMKETIFELEDEVEQHRAV-KLHDNLIISDLENT--VKKLQDQKHDLERENKTLHRRLREESAEWRQFQ 751
Cdd:pfam05483 398 kfknnKEVELEELKKILAEDEKLLDEKKQFeKIAEELKGKEQELIflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 564397587 752 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1018-1091 |
3.77e-05 |
|
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: 44.21 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1018 LLKWCQK--KTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIP----YQELNSQEKKRNFTLAFQAAESVGIKSTL-- 1089
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLtp 94
|
...
gi 564397587 1090 -DI 1091
Cdd:cd21218 95 eDI 97
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
578-960 |
5.69e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 47.35 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 578 NRLKAQLEKEKQK-----------VAELYSIHNSGDKSDIQDL--LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDT 644
Cdd:PTZ00108 998 EYLLGKLERELARlsnkvrfikhvINGELVITNAKKKDLVKELkkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDED 1077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 645 IAKVEDEYRAFQEEAKKQIEDLNMT-LEKLRSELEEKETERSDMKET---------IFELEDEVEQHRAVKLhdNLIISD 714
Cdd:PTZ00108 1078 DEEELGAAVSYDYLLSMPIWSLTKEkVEKLNAELEKKEKELEKLKNTtpkdmwledLDKFEEALEEQEEVEE--KEIAKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 715 LENTVKKLQDQKHDLERENKTLHRRLREESAEwrqfqaDLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEK-LTKEL 793
Cdd:PTZ00108 1156 QRLKSKTKGKASKLRKPKLKKKEKKKKKSSAD------KSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSdQEDDE 1229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 794 EEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNaaaaaiPRTPLSPSPM 873
Cdd:PTZ00108 1230 EQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPD------GESNGGSKPS 1303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 874 KTPPAAAVSPMQRHSISGPVSTSKPLTALSDKRSnygeipgQEHLLRTSSTSRPASLPRVPAMESAKTISvsrrSSEEMK 953
Cdd:PTZ00108 1304 SPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKS-------KTRVKQASASQSSRLLRRPRKKKSDSSSE----DDDDSE 1372
|
....*..
gi 564397587 954 RDISASE 960
Cdd:PTZ00108 1373 VDDSEDE 1379
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-824 |
6.00e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHI 476
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 SY------VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 550
Cdd:COG1196 387 ELlealraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 551 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAET-----LAS 625
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 626 SLQEDLAHTRNDANRLQDTIAK-----------------------------------VEDEYRAFQEEAKKQIEDL---- 666
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAakagratflpldkiraraalaaalargaigaavdlVASDLREADARYYVLGDTLlgrt 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 667 ---------NMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLH 737
Cdd:COG1196 627 lvaarleaaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 738 RRLREESAEWRQ----FQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER-GRVyNyM 812
Cdd:COG1196 707 RELAEAEEERLEeeleEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlGPV-N-L 784
|
490
....*....|..
gi 564397587 813 NAVErDLAALRQ 824
Cdd:COG1196 785 LAIE-EYEELEE 795
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1011-1111 |
6.52e-05 |
|
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: 43.62 E-value: 6.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 1011 GGSKRNALLKWCQKKTEgyqNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQEKKRNFTLAFQAAES-VGIKST 1088
Cdd:cd21315 14 GPTPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDwLDVPQL 90
|
90 100
....*....|....*....|...
gi 564397587 1089 LDINEMArTERPDWQNVMLYVTA 1111
Cdd:cd21315 91 IKPEEMV-NPKVDELSMMTYLSQ 112
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
603-802 |
7.06e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.35 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 603 KSDIQDLLESvRLDKEKAEtLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQeeakkqiedlNMTLEKLRSELEEKET 682
Cdd:TIGR01612 662 KSELSKIYED-DIDALYNE-LSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ----------NMETATVELHLSNIEN 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 683 ERSDMKETIFELEDEVeqHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHrRLREESAEWRQFQADlqtAVVIAN 762
Cdd:TIGR01612 730 KKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSKISEIKNHYND---QINIDN 803
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564397587 763 DIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
482-793 |
7.55e-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: 47.14 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 482 EDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK-AALA 560
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 561 ATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKSdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN- 639
Cdd:pfam12128 308 GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS-WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKe 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 640 RLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELeeketeRSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTV 719
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATP 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564397587 720 KKLQDQKHDLERENktlhrRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL 793
Cdd:pfam12128 461 ELLLQLENFDERIE-----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
576-726 |
7.92e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.16 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKAQLEKEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYraf 655
Cdd:smart00787 155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564397587 656 qEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 726
Cdd:smart00787 221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-802 |
8.83e-05 |
|
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: 46.97 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 652 YRAFQEEAKKQIEDLNMTLEKL---RSELE----------EKETERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENT 718
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLediLNELErqlkslerqaEKAERYKELKAELRELELALLVLRLEELREEL--EELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 719 VKKLQDQKHDLERENKTLH---RRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 795
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
....*..
gi 564397587 796 IKSRKQE 802
Cdd:TIGR02168 328 LESKLDE 334
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
492-969 |
9.55e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 492 LEQRYMDLAENARFEReQLLGVQQHLSNTLKmAEQDNKEAQEMIGALKERSHHmERIIESEQKGKAALaatLEEYKATVA 571
Cdd:COG5022 798 KLQPLLSLLGSRKEYR-SYLACIIKLQKTIK-REKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFS---LLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 572 SDQIEMNRLKAQLEKEKQKVAELYSIHNSGDKsdiqdlLESVRLdkEKAETLASSLQEDLAHTRNDANRLQDTIAKVE-D 650
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKSISSLKLVNLE------LESEII--ELKKSLSSDLIENLEFKTELIARLKKLLNNIDlE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 651 EYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEveqhravklhdnliISDLENTVKKLQ---DQKH 727
Cdd:COG5022 944 EGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA--------------NSELKNFKKELAelsKQYG 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 728 DLERENKTLHRRLREesaewrqfQADLQTAVVIANDIKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSR-----K 800
Cdd:COG5022 1010 ALQESTKQLKELPVE--------VAELQSASKIISSESTELSilKPLQKLKGLLLLENNQLQARYKALKLRRENsllddK 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 801 QEEERGRVYNYMNAVERD--LAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNAaaaaiprtpLSPSPMKTPPA 878
Cdd:COG5022 1082 QLYQLESTENLLKTINVKdlEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNT---------LEPVFQKLSVL 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 879 -AAVSPMQRHSISGPVSTSKPLTALSDKRsnygeiPGQEHLLRTSSTSRPASLPrvpaMESAKTISVSRRSSEEMKRDIS 957
Cdd:COG5022 1153 qLELDGLFWEANLEALPSPPPFAALSEKR------LYQSALYDEKSKLSSSEVN----DLKNELIALFSKIFSGWPRGDK 1222
|
490
....*....|..
gi 564397587 958 ASEGASPASLMA 969
Cdd:COG5022 1223 LKKLISEGWVPT 1234
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
329-823 |
9.65e-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: 46.76 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 329 QDENTLMAHQHSNSMDNLDSECSEVYQPLtssdDALdapssseSEGVPSIERSRKGSSGNASEVSVACLtERIHQMEENQ 408
Cdd:pfam12128 335 LDADIETAAADQEQLPSWQSELENLEERL----KAL-------TGKHQDVTAKYNRRRSKIKEQNNRDI-AGIKDKLAKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 409 HSTSEELQATLQelADLQQITQELNSENE---------------RLGEEKVILMESLCQQSDKLehfgrQIEYFRSLLDE 473
Cdd:pfam12128 403 REARDRQLAVAE--DDLQALESELREQLEagklefneeeyrlksRLGELKLRLNQATATPELLL-----QLENFDERIER 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 474 hhisyvIDEdvksgrymELEQRYMDLaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKER------------ 541
Cdd:pfam12128 476 ------ARE--------EQEAANAEV-ERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhfl 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 542 -------SHHMERIIESEQKGKAALAATLEE---------YKATVASDQIEMNR---LKAQLEKEKQKVAELY-SIHNSG 601
Cdd:pfam12128 541 rkeapdwEQSIGKVISPELLHRTDLDPEVWDgsvggelnlYGVKLDLKRIDVPEwaaSEEELRERLDKAEEALqSAREKQ 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 602 DKSDIQDLLESVRLDK-EKAETLASSL----QEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIE-DLNMTLEKLRS 675
Cdd:pfam12128 621 AAAEEQLVQANGELEKaSREETFARTAlknaRLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEaQLKQLDKKHQA 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 676 ELEEKETERSDMKETIFELEDEVEQHRAVKL----------------HDNLIISDLENTVKKL---QDQKHDLERENKTL 736
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGALDAQLallkaaiaarrsgakaELKALETWYKRDLASLgvdPDVIAKLKREIRTL 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 737 HRRL------REESAEWRQFQADL-----QTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEeiKSRKQEEER 805
Cdd:pfam12128 781 ERKIeriavrRQEVLRYFDWYQETwlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERK--ASEKQQVRL 858
|
570
....*....|....*...
gi 564397587 806 GRVYNYMNAVERDLAALR 823
Cdd:pfam12128 859 SENLRGLRCEMSKLATLK 876
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
489-805 |
1.51e-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: 46.12 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 489 YMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKE------------AQEMIGALKERSHHMERIIESEQKGk 556
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAleyyqlkeklelEEEYLLYLDYLKLNEERIDLLQELL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 557 AALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 636
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE-----ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 637 DANRLQDTIAKVEdEYRAFQEEAKKQIEDLNMTLEKLRSELEEKET-ERSDMKETIFELEDEVEQHRAVKLHDNLIISDL 715
Cdd:pfam02463 322 EKKKAEKELKKEK-EEIEELEKELKELEIKREAEEEEEEELEKLQEkLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 716 ENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAqEKNEKLTKELEE 795
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL-KKSEDLLKETQL 479
|
330
....*....|
gi 564397587 796 IKSRKQEEER 805
Cdd:pfam02463 480 VKLQEQLELL 489
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
580-819 |
1.70e-04 |
|
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: 45.87 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 580 LKAQLEKEKQKVAELYSIHNSGDKSdIQDLL---ESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQ 656
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKA-IQELQfenEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 657 ---EEAKKQIEDLNMTLEKLRSELEEKETERSDMK-ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERE 732
Cdd:pfam05483 176 yerEETRQVYMDLNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 733 NKTLHRRLREESAEWRQFQAdlqtavviandiKSEAQEEigdlkrRLHEAQEKNEKLTKELEEIKSRKQeeergRVYNYM 812
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLEE------------KTKLQDE------NLKELIEKKDHLTKELEDIKMSLQ-----RSMSTQ 312
|
....*..
gi 564397587 813 NAVERDL 819
Cdd:pfam05483 313 KALEEDL 319
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-839 |
1.88e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSE--ELQATL-----QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRS 469
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNEsnELHEKQkfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 470 LldehhisyviDEDVKSGRYMELEQ-RYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMiGALKERSHHMERI 548
Cdd:pfam15921 160 L----------KEDMLEDSNTQIEQlRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHF-RSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 549 IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLEKEKQKVAELYSIHnsgdksdiqdllesvrldkekaETLASSLQ 628
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEALKSES--QNKIELLLQQHQDRIEQLISEH----------------------EVEITGLT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 629 EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEK----ETERSDMKETIFELEDEVEQHRAV 704
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 705 KLHDNLIISDLENTVKKLQDQKHDLERE-------NKT--------------LHRRLREESAEWRQFQADLQTavviand 763
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLADLHKREKElslekeqNKRlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKA------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 764 IKSEAQeeiGDLKRRLHEAQEKNE------KLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGMGLSRRS--S 833
Cdd:pfam15921 438 MKSECQ---GQMERQMAAIQGKNEslekvsSLTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAieA 514
|
....*.
gi 564397587 834 TSSEPT 839
Cdd:pfam15921 515 TNAEIT 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
607-914 |
1.93e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 607 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEE---- 679
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 680 --KETERSDMKETIF------ELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLhrrlreesaewRQFQ 751
Cdd:COG3883 95 lyRSGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-----------EALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 752 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNymNAVERDLAALRQGMGLSRR 831
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA--AAAAAAAAAAAAAAAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 832 SSTSSEPTPTVKTLIKSFDSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPVSTSKPLTALSDKRSNYGE 911
Cdd:COG3883 242 AAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGA 321
|
...
gi 564397587 912 IPG 914
Cdd:COG3883 322 VVG 324
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
534-807 |
2.05e-04 |
|
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: 45.55 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 534 MIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKekqKVAELYSIHNSGDKSDIQ--DLLE 611
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK---KEEELQAALARLEEETAQknNALK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 612 SVRldkeKAETLASSLQEDLahtrndanrlqdtiakveDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETI 691
Cdd:pfam01576 265 KIR----ELEAQISELQEDL------------------ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 692 FELEDEVEQHRAVklhdnliisdLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEE 771
Cdd:pfam01576 323 SKREQEVTELKKA----------LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392
|
250 260 270
....*....|....*....|....*....|....*.
gi 564397587 772 IGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
506-826 |
2.37e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 506 EREQLlgvqQHLSNTL-------KMAEQDNKEAQEMIGALKERSHhmeriiESEQKGKAALAATLEEYKATVASDQIEMN 578
Cdd:pfam00038 2 EKEQL----QELNDRLasyidkvRFLEQQNKLLETKISELRQKKG------AEPSRLYSLYEKEIEDLRRQLDTLTVERA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 579 RLKAQLEKekqkvaelysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLqdTIAKVEDEyrafqee 658
Cdd:pfam00038 72 RLQLELDN-------------------LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA--TLARVDLE------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 659 akKQIEDLNMTLEKLRSELEEketERSDMKETIfeledeVEQHRAVKLHDNLIIsDLENTVKKLQDQKHDLERENktlhr 738
Cdd:pfam00038 124 --AKIESLKEELAFLKKNHEE---EVRELQAQV------SDTQVNVEMDAARKL-DLTSALAEIRAQYEEIAAKN----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 739 rlREESAEWRQFQ-ADLQTAVVIANDIKSEAQEEIGDLKRRLH------EAQEK-NEKLTKELEEIKSRkQEEERGRVYN 810
Cdd:pfam00038 187 --REEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQsleielQSLKKqKASLERQLAETEER-YELQLADYQE 263
|
330
....*....|....*.
gi 564397587 811 YMNAVERDLAALRQGM 826
Cdd:pfam00038 264 LISELEAELQETRQEM 279
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1034-1081 |
2.43e-04 |
|
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: 41.60 E-value: 2.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564397587 1034 ITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQEKKRNFTLAFQAAE 1081
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAK 69
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
487-807 |
2.87e-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: 44.89 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 487 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQdnkEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEy 566
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE---LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLER- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 567 katvasdQIEMNRLKAQLEKEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIA 646
Cdd:pfam07888 149 -------ETELERMKERAKKAGAQRKEEEA-----ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 647 KVEDEYrafqEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQ--HRAVKLHDnliisdlentvKKLQD 724
Cdd:pfam07888 217 TLTQKL----TTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQrdRTQAELHQ-----------ARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 725 QKHDLERENKTLHrrLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL--EEIKSRKQE 802
Cdd:pfam07888 282 AQLTLQLADASLA--LREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELgrEKDCNRVQL 359
|
....*
gi 564397587 803 EERGR 807
Cdd:pfam07888 360 SESRR 364
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
605-738 |
2.93e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 44.28 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 605 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSElEEKE 681
Cdd:cd22656 99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564397587 682 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDLERENKTLHR 738
Cdd:cd22656 176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
656-826 |
2.96e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 656 QEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDLERENKT 735
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 736 LHRRLREesaeWRQFQADLQTAvviANDIKsEAQEEIGDLKRRLHEAQEKN-EKLTKELEEIKSRKQ--EEERGRVYNYM 812
Cdd:COG4717 151 LEERLEE----LRELEEELEEL---EAELA-ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAelEEELEEAQEEL 222
|
170
....*....|....
gi 564397587 813 NAVERDLAALRQGM 826
Cdd:COG4717 223 EELEEELEQLENEL 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
657-805 |
3.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 657 EEAKKQIEDLNMTLEKLRSELEEKETErsdMKETIFELEDEVEQhrAVKLHDnliisDLENTVKKLQDQKHDLEREnktL 736
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERE---LEQKAEEAEALLKE--AEKLKE-----ELEEKKEKLQEEEDKLLEE---A 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564397587 737 HRRLREESAEWRQfqadlqTAVVIANDIKSEAQEEIGDLKRrlHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:PRK00409 572 EKEAQQAIKEAKK------EADEIIKELRQLQKGGYASVKA--HELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
576-677 |
3.69e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 576 EMNRLKAQLekekQKVAELYSIHNSGdKSDIQDLLESVRLDKEKAETLASSLQ---EDLAHTRNDANRLQDTIAKVEDEY 652
Cdd:PRK09039 54 ALDRLNSQI----AELADLLSLERQG-NQDLQDSVANLRASLSAAEAERSRLQallAELAGAGAAAEGRAGELAQELDSE 128
|
90 100
....*....|....*....|....*
gi 564397587 653 RAFQEEAKKQIEDLNMTLEKLRSEL 677
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQL 153
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
413-802 |
4.07e-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: 44.43 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 413 EELQATLQELADLQQitqELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHhisyvideDVKSGRYMEL 492
Cdd:pfam10174 331 ESLTAKEQRAAILQT---EVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML--------DVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 493 EQRYMDLAENARFEREQLLGvqqhLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKA----ALAATLEEYKA 568
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREredrERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 569 TVASDQIEMNRLKAQLEKEKQKVAEL----YSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANR---- 640
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLkehaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpe 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 641 LQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRseleEKETERSDMKETIFELEDEVEQHravklhdnliISDLENTVK 720
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAELESLTLRQ----------MKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 721 KLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSeaQEEIGDLKRRLHEAQ----EKNEKLT------ 790
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQqslaEKDGHLTnlraer 699
|
410
....*....|...
gi 564397587 791 -KELEEIKSRKQE 802
Cdd:pfam10174 700 rKQLEEILEMKQE 712
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
491-824 |
4.24e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 491 ELEQRYMDLAEN--ARFErEQLLGVQQhLSNTLKM--AEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAAT 562
Cdd:PRK04778 68 EWRQKWDEIVTNslPDIE-EQLFEAEE-LNDKFRFrkAKHEINEIESLLDLIEEDIEQIleelQELLESEEKNREEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 563 LEEY---KATV---------ASDQIEmNRLkAQLEKEKQKVAELYSihnSGDKsdiqdllesvrldkEKAETLASSLQED 630
Cdd:PRK04778 146 KDLYrelRKSLlanrfsfgpALDELE-KQL-ENLEEEFSQFVELTE---SGDY--------------VEAREILDQLEEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 631 LAHTRND-----------ANRLQDTIAKVEDEYRAFQEE---------------AKKQIEDLNMTLEKLR-SELEEKETE 683
Cdd:PRK04778 207 LAALEQImeeipellkelQTELPDQLQELKAGYRELVEEgyhldhldiekeiqdLKEQIDENLALLEELDlDEAEEKNEE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 RSDMKETIFE-LEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENKTLHrrLRE-ESAEWRQFQADLQTAVVIA 761
Cdd:PRK04778 287 IQERIDQLYDiLEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYT--LNEsELESVRQLEKQLESLEKQY 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564397587 762 NDIkseaQEEIGDLKRRLHEAQEKNEKLTKELEEIksrkqEEERGRVYNYMNAVERDLAALRQ 824
Cdd:PRK04778 365 DEI----TERIAEQEIAYSELQEELEEILKQLEEI-----EKEQEKLSEMLQGLRKDELEARE 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-660 |
4.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 409 HSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhhisyvIDEDVKsgr 488
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 489 ymELEQRYMDLAENARFEREQLlgvQQHLSNTLKMAEQDNKE---AQEMIGALKERSHHMERIIESEQKGKAALAATLEE 565
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 566 YKATVASDQIEMNRLKAQLEKEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEdlahtrnDANRLQDTI 645
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQ-------EAEELEALI 229
|
250
....*....|....*
gi 564397587 646 AKVEDEYRAFQEEAK 660
Cdd:COG4942 230 ARLEAEAAAAAERTP 244
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
364-823 |
5.44e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 364 LDAPSSSESEGVPSIER--------SRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNS- 434
Cdd:PRK01156 206 IADDEKSHSITLKEIERlsieynnaMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKi 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 435 ENERLGEEKVILMESLCQQSDkLEHFGRQIEYFRSLLDEHHISYVIDEDVKSGR--YMELEQRYMDLAEnarfEREQLLG 512
Cdd:PRK01156 286 INDPVYKNRNYINDYFKYKND-IENKKQILSNIDAEINKYHAIIKKLSVLQKDYndYIKKKSRYDDLNN----QILELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 513 VQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVA 592
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 593 ELysihnsgdkSDIQDLLESVRLDKEKAETLASSLQEDLA-HTRNDANRLQDTIAKVEDEYRAFQEEAKKQI-------- 663
Cdd:PRK01156 441 EL---------SRNMEMLNGQSVCPVCGTTLGEEKSNHIInHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeyles 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 664 EDLNMT------LEKLRSELEEKETERSDMKETIFELEDEVEQHRAVKLHD-----------NLIISDLEntVKKLQDQK 726
Cdd:PRK01156 512 EEINKSineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDldskrtswlnaLAVISLID--IETNRSRS 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 727 HDLERENKTLHRRLREESAEWRQFQADLQTAV-VIANDIKS--EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRkqEE 803
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIrEIENEANNlnNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI--IP 667
|
490 500
....*....|....*....|
gi 564397587 804 ERGRVYNYMNAVERDLAALR 823
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSR 687
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
509-807 |
5.98e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 509 QLLGVQQHLSNTLKMAEQDN--KEAQEMIGALKE-RSHHMERIIESEQKGKAALAATleEYKATVASDQ----IEMNRLK 581
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQermaMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 582 AQLEKEKQKvAELYSIHNSGDKSDIQDLLESVRLDKEKAEtlasslqedlahtRNDANRLQDTIAKvedEYRAFQEEAKK 661
Cdd:pfam17380 351 ERIRQEERK-RELERIRQEEIAMEISRMRELERLQMERQQ-------------KNERVRQELEAAR---KVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 662 QIEDLNMTLEKLRSELEEKETERSDMKETifELEDEVEQHRAVKLhdnliisDLENTVKKLQDQKHDLERenktlhRRLR 741
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQ-------ERQQQVERLRQQEEERKR------KKLE 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564397587 742 EESAEWRQFQADLQTAVVIandikseaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKIL--------EKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
496-802 |
6.74e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 496 YMDLAENARFEREQLLGVQQHLSN---TLKMAEQDNKEAQEMIGALKERSHHMERIIESeQKGKAALAATLEEYKATVAS 572
Cdd:PRK04863 274 YMRHANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 573 DQIEMNRLKAQLEKEKQKVAElysihnsgdksdIQDLLESVRLDKEKAET----LASSL---QE--DLAHTR----NDAN 639
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEE------------ADEQQEENEARAEAAEEevdeLKSQLadyQQalDVQQTRaiqyQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 640 RLQD-----------TIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEK---------------ETERSDMKETIFE 693
Cdd:PRK04863 421 QALErakqlcglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvrkiagEVSRSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 694 LEDEVEQHRAvklhdnliisdLENTVKKLQDQKHDLER---ENKTLHRRLREESaewRQFQADLQTAVViANDIKSEAQE 770
Cdd:PRK04863 501 LLRRLREQRH-----------LAEQLQQLRMRLSELEQrlrQQQRAERLLAEFC---KRLGKNLDDEDE-LEQLQEELEA 565
|
330 340 350
....*....|....*....|....*....|..
gi 564397587 771 EIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
514-810 |
6.77e-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: 43.66 E-value: 6.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 514 QQH---LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKgkaaLAATLEEYKATVASdqiEMNRLKAQLEKEKQK 590
Cdd:pfam10174 323 KQHievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTK----QLQDLTEEKSTLAG---EIRDLKDMLDVKERK 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 591 VAELYS-IHN------SGDK--SDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK 661
Cdd:pfam10174 396 INVLQKkIENlqeqlrDKDKqlAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 662 QIEDLNMTLEKLRSELEEKETERSDMKE--------------TIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKH 727
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEE-------CSKLENQLKKAHNAEE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 728 DlERENKTLHRRLREesaewrqfqadLQTAVVIANDIKSEAQEEIGDLKRRLHEAQ-EKNEKLTK--ELEEIKSRKQEEE 804
Cdd:pfam10174 549 A-VRTNPEINDRIRL-----------LEQEVARYKEESGKAQAEVERLLGILREVEnEKNDKDKKiaELESLTLRQMKEQ 616
|
....*.
gi 564397587 805 RGRVYN 810
Cdd:pfam10174 617 NKKVAN 622
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
605-808 |
6.79e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 605 DIQDLLESVRLDKEKAETLASSLQedlahtrndanRLQDTIAKVEDEYRAFQEEAKKqiedlnmtLEKLRSELEEKETER 684
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQ-----------QHGNALAQLEPIVSVLQSDPEQ--------FEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 685 SDMKETIFELEDEVEQHRAVKLHDNLII----SDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADLQTAVVI 760
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDAAEMlaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564397587 761 ANDIKSEAQEEIGDLKRRLHE-----AQEKNEKLTKELEEIKSRKQEEERGRV 808
Cdd:PRK04863 1032 KRQMLQELKQELQDLGVPADSgaeerARARRDELHARLSANRSRRNQLEKQLT 1084
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
619-834 |
6.95e-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: 43.73 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 619 KAETLASSLQEDLaHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDlnmTLEKLRSELEEKETERSDMKETIFELE--- 695
Cdd:pfam07888 28 RAELLQNRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEeky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 696 -------DEVEQHRAVKLHDN----LIISDLENTVKKLQDQKHDLERE-------NKTLHRRLREESAEWRQFQADLQTA 757
Cdd:pfam07888 104 kelsassEELSEEKDALLAQRaaheARIRELEEDIKTLTQRVLERETElermkerAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564397587 758 VVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynyMNAVERDLAALRQGMGLSRRSST 834
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKVE 254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-679 |
7.25e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhhi 476
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 sYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERshhmERIIESEQKGK 556
Cdd:COG1196 321 -LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL----AEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 557 AALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 636
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564397587 637 DANRLQDTIAKVEDEyrafqEEAKKQIEDLNMTLEKLRSELEE 679
Cdd:COG1196 471 EAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLE 508
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
608-824 |
7.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 608 DLLESVRLDKEKAETLASSLQEDLAHTR-------------NDANRLQDTIAKVEDEYRAFQ-----EEAKKQIEDLNMT 669
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPvkgsnvieisytsPDPELAAAVANALAEAYLEQNlelrrEEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 670 LEKLRSELEEKETERSDMKET--IFELEDEVEQHRAvklhdnlIISDLENTVKKLQDQKhdleRENKTLHRRLREESAEW 747
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQ-------QLSELESQLAEARAEL----AEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564397587 748 RQFQADLQTAVVIANDIK--SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvyNYMNAVERDLAALRQ 824
Cdd:COG3206 253 PDALPELLQSPVIQQLRAqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----RILASLEAELEALQA 327
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
521-804 |
7.34e-04 |
|
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: 43.69 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 521 LKMAEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAATLEEYKAT------------VASDQIEmNRLKaQL 584
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQIleelDELLESEEKNREEVEELKDKYRELrktllanrfsygPAIDELE-KQLA-EI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 585 EKEKQKVAELysiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDanrLQDTIAKVEDEYRAFQEE------ 658
Cdd:pfam06160 159 EEEFSQFEEL---TESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE---LPDQLEELKEGYREMEEEgyaleh 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 659 ---------AKKQIEDLNMTLEKLrsELEEKETERSDMKETIFEL----EDEVEQHRAVKLHDNLIISDLENTVKKLQDQ 725
Cdd:pfam06160 233 lnvdkeiqqLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKKYVEKNLPEIEDYLEHAEEQNKEL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 726 KHDLER--ENKTLHrrlREESAEWRQFQADLQTAV----VIANDIK------SEAQEEIGDLKRRLHEAQEKNEKLTKEL 793
Cdd:pfam06160 311 KEELERvqQSYTLN---ENELERVRGLEKQLEELEkrydEIVERLEekevaySELQEELEEILEQLEEIEEEQEEFKESL 387
|
330
....*....|.
gi 564397587 794 EEIksRKQEEE 804
Cdd:pfam06160 388 QSL--RKDELE 396
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
660-799 |
7.42e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 660 KKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQ-HRAVK--LHDNLIISDLENTVKKLQDQKHDLERENKTL 736
Cdd:pfam13851 32 KEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEElRKQLEnyEKDKQSLKNLKARLKVLEKELKDLKWEHEVL 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564397587 737 HRRLREESAEWRQFQADLQTAVviandikSEAQEEIGD----LKRRLHEAQEKNEKLTKELEEIKSR 799
Cdd:pfam13851 112 EQRFEKVERERDELYDKFEAAI-------QDVQQKTGLknllLEKKLQALGETLEKKEAQLNEVLAA 171
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-805 |
9.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 521 LKMAEQDNKEAQEMIGAlkERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELYSIHNS 600
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 601 GDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEK 680
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 681 ETERSDMKETIFELEDEVEQHRAVKlhdnliisdlENTVKKLQDQKHDLERENKT--LHRRLREESAEWRQFQADLQTAV 758
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAE----------EDEKKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELKKAEEENK 1729
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564397587 759 VIANDIKSEAQEEigdlKRRLHEAQ--EKNEKLTKELEEIKSRKQEEER 805
Cdd:PTZ00121 1730 IKAEEAKKEAEED----KKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-824 |
1.12e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 657 EEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQhravklhdnlIISDLENTVKKLQDQKHDLERENKTL 736
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQ----------LEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 737 hRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVE 816
Cdd:COG4372 104 -ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*...
gi 564397587 817 RDLAALRQ 824
Cdd:COG4372 183 QALDELLK 190
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
399-809 |
1.40e-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: 42.81 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 399 ERIHQME---ENQHSTSEELQATLQELA---DLQQITQELNSENERLG----------EEKVILMESLCQQSD------- 455
Cdd:pfam05557 170 QRIKELEfeiQSQEQDSEIVKNSKSELAripELEKELERLREHNKHLNenienklllkEEVEDLKRKLEREEKyreeaat 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 456 ---KLEHFGRQIEYFRSLLDEHHISYVIDEDVkSGRYMELEQRYMDLAE-------NARFEREQLLGVQQHLSNTLKMAE 525
Cdd:pfam05557 250 lelEKEKLEQELQSWVKLAQDTGLNLRSPEDL-SRRIEQLQQREIVLKEenssltsSARQLEKARRELEQELAQYLKKIE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 526 QDNKEaqemigaLKERSHHMERIieseQKGKAALAATLEEYKATVAS--DQIEMNRLKAQLEKEKQKVAEL---YSIHNS 600
Cdd:pfam05557 329 DLNKK-------LKRHKALVRRL----QRRVLLLTKERDGYRAILESydKELTMSNYSPQLLERIEEAEDMtqkMQAHNE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 601 GDKSDIQDLLESVRLDKEKAETLASSLQedlahtrndANRlqdtiakvedeyrafQEEAKKQIEDLNMTLEKLRSELEEK 680
Cdd:pfam05557 398 EMEAQLSVAEEELGGYKQQAQTLERELQ---------ALR---------------QQESLADPSYSKEEVDSLRRKLETL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 681 ETERSDMKETIFELEDEVEQH-----------RAVKLHDNLIISDLENTvkklQDQKHDLERENKTLHRRLreesaewRQ 749
Cdd:pfam05557 454 ELERQRLREQKNELEMELERRclqgdydpkktKVLHLSMNPAAEAYQQR----KNQLEKLQAEIERLKRLL-------KK 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 750 FQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKltkeLEEIKSRKQEEERGRVY 809
Cdd:pfam05557 523 LEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQR----LKEVFQAKIQEFRDVCY 578
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
202-754 |
1.57e-03 |
|
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: 42.65 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 202 LRNELRDMRAQLGISEDHCEGEDRSEEKETIIAHQPTdVESTLLQLQEQNTAIREELNQLKNEnrmLKDRLNALgfslEQ 281
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSKMRSRAKL---LMKRAAHV----KQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 282 RLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMAHQHSNS----MDNLDSECSEVyQPL 357
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSlckeLDILQREQATI-DTR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 358 TSSDDALDAP-SSSESEGVPSIERSRKGSSgnASEVSVACLTERIHQMEENQHSTSEELQatlqELADLQQITQ------ 430
Cdd:TIGR00618 416 TSAFRDLQGQlAHAKKQQELQQRYAELCAA--AITCTAQCEKLEKIHLQESAQSLKEREQ----QLQTKEQIHLqetrkk 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 431 -------ELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEyfrSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENA 503
Cdd:TIGR00618 490 avvlarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 504 RFEREQLL-------------GVQQHLSNTLKMAEQDNKEAQEMIGA-------LKERSHHMERIIESEQKGK--AALAA 561
Cdd:TIGR00618 567 EIQQSFSIltqcdnrskedipNLQNITVRLQDLTEKLSEAEDMLACEqhallrkLQPEQDLQDVRLHLQQCSQelALKLT 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 562 TLEEYKATVASDQIEMNRLKA---QLEKEKQKVAELYSIHN-----SGDKSDIQDLLESVRLDKEKAETL---------- 623
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIrvlPKELLASRQLALQKMQSekeqlTYWKEMLAQCQTLLRELETHIEEYdrefneiena 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 624 ASSLQEDLA-------HTRNDANRLQDTI--AKVEDEYRAFQEEAKKqiEDLNMTLEKLRSELEEKETERSDMKETIFEL 694
Cdd:TIGR00618 727 SSSLGSDLAaredalnQSLKELMHQARTVlkARTEAHFNNNEEVTAA--LQTGAELSHLAAEIQFFNRLREEDTHLLKTL 804
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564397587 695 EDEVEQHRAvklHDNLIIS-DLENTVKKLQDQKHDLERENKTLH--RRLREESAEWRQFQADL 754
Cdd:TIGR00618 805 EAEIGQEIP---SDEDILNlQCETLVQEEEQFLSRLEEKSATLGeiTHQLLKYEECSKQLAQL 864
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
540-690 |
1.87e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 540 ERSHHMERII-------ESEQKGKAALAATLEEykatvasdqieMNRLKAQLEKEKQKVAELYSihnsgDKSDIQDLLES 612
Cdd:PRK11637 149 EESQRGERILayfgylnQARQETIAELKQTREE-----------LAAQKAELEEKQSQQKTLLY-----EQQAQQQKLEQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 613 VRLDKEKAET-LASSLQED---LAHTRNDANRLQDTIAKVEDEYRAFQE-EAKKQiedlnmtlEKLRSELEE-------- 679
Cdd:PRK11637 213 ARNERKKTLTgLESSLQKDqqqLSELRANESRLRDSIARAEREAKARAErEAREA--------ARVRDKQKQakrkgsty 284
|
170
....*....|...
gi 564397587 680 --KETERSDMKET 690
Cdd:PRK11637 285 kpTESERSLMSRT 297
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
626-804 |
2.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 626 SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEVEQHR 702
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaeKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 703 AVKlhdNLIISDLENtVKKLQDQKHDLERENKTLHRRLREEsaEWRQfqadlQTAVVianDIKSEAQ--EEIGDLKRRLH 780
Cdd:COG1340 85 EKL---NELREELDE-LRKELAELNKAGGSIDKLRKEIERL--EWRQ-----QTEVL---SPEEEKElvEKIKELEKELE 150
|
170 180
....*....|....*....|....*...
gi 564397587 781 EAQ---EKNEKLTKELEEIKS-RKQEEE 804
Cdd:COG1340 151 KAKkalEKNEKLKELRAELKElRKEAEE 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
485-824 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 485 KSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIEseqkgKAALAATLE 564
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 565 EYKATVASDQIEMNRLKAQLEKEKQKVAELYSIhnsgdKSDIQDLLEsvRLDKEKAETLASSLQEdLAHTRNDANRLQDT 644
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEEL-----EAELAELQE--ELEELLEQLSLATEEE-LQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 645 IAKVEDEYrafqEEAKKQIEDLNMTLEKLRSELE-EKETERSDMKETIFELEDEVEQHRAVKLHDN-------------- 709
Cdd:COG4717 208 LAELEEEL----EEAQEELEELEEELEQLENELEaAALEERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 710 -LIISDLENTVKKLQDQKHDLERENKtLHRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEK 788
Cdd:COG4717 284 gLLALLFLLLAREKASLGKEAEELQA-LPALEELEEEELEELLAALGLP-------PDLSPEELLELLDRIEELQELLRE 355
|
330 340 350
....*....|....*....|....*....|....*.
gi 564397587 789 LTKELEEIKSRKQEEERGRVYNYMNAveRDLAALRQ 824
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGV--EDEEELRA 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
539-805 |
2.36e-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: 42.04 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 539 KERSHHMERIiESEQKGkAALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdksdiqdlLESVRLDKE 618
Cdd:pfam05557 21 MELEHKRARI-ELEKKA-SALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---------------AELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 619 KAETLASSLQEDLAhTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELE--- 695
Cdd:pfam05557 84 YLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 696 ----------DEVEQHRAVKLHDNLIIsdleNTVKKLQDQKHDLERENKtlhrRLREESAEWRQFQADlqtavviandiK 765
Cdd:pfam05557 163 sslaeaeqriKELEFEIQSQEQDSEIV----KNSKSELARIPELEKELE----RLREHNKHLNENIEN-----------K 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564397587 766 SEAQEEIGDLKRRLH---EAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:pfam05557 224 LLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVK 266
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
402-795 |
2.52e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 402 HQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLD--EHHISYV 479
Cdd:PTZ00440 752 HQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQklEAHTEKN 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 480 IDEDVKSGRYMELEQRYMDLAENARFEREQllgvQQHLSNTLKMAEQDNK--EAQEMIGALKERSHHMERIIESEQKGKA 557
Cdd:PTZ00440 832 DEELKQLLQKFPTEDENLNLKELEKEFNEN----NQIVDNIIKDIENMNKniNIIKTLNIAINRSNSNKQLVEHLLNNKI 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 558 ALAATLEEYKATVASDQI----EMNRLKAQLEKEKQKV-AELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLA 632
Cdd:PTZ00440 908 DLKNKLEQHMKIINTDNIiqknEKLNLLNNLNKEKEKIeKQLSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLD 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 633 HTRNDANRLQDTIAKVEDEYRAFQEEA----KKQIEDLNMTLEKL----RSELEEKETER----SDMKETI--FELEDEV 698
Cdd:PTZ00440 988 KEKDEWEHFKSEIDKLNVNYNILNKKIddliKKQHDDIIELIDKLikekGKEIEEKVDQYisllEKMKTKLssFHFNIDI 1067
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 699 EqhravKLHDNLIisdlENTVKKLQDQKHDLErenktlhRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRR 778
Cdd:PTZ00440 1068 K-----KYKNPKI----KEEIKLLEEKVEALL-------KKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKS 1131
|
410
....*....|....*..
gi 564397587 779 LHEAQEKNEKLTKELEE 795
Cdd:PTZ00440 1132 LEKIYKQMEKTLKELEN 1148
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
617-793 |
2.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 617 KEKAETLASSLQEDLAHTRNDANRLQDTIAK-----VEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETI 691
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKealleAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 692 FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQkhdlerENKTLhrrlrEESAEWRQFQADLQtavvIANDIKSEAQEE 771
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEE------QLQEL-----ERISGLTAEEAKEI----LLEKVEEEARHE 170
|
170 180
....*....|....*....|...
gi 564397587 772 IGDLKRRLH-EAQEKNEKLTKEL 793
Cdd:PRK12704 171 AAVLIKEIEeEAKEEADKKAKEI 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-593 |
3.01e-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: 41.29 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmesLCQQSDKLEHFGRQiEYFRSLLDehhi 476
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE-------LAELLRALYRLGRQ-PPLALLLS---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 477 SYVIDEDVKSGRYMEleqrymDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK 556
Cdd:COG4942 128 PEDFLDAVRRLQYLK------YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190
....*....|....*....|....*....|....*..
gi 564397587 557 AALAATLEEYKATVASDQIEMNRLKAQLEKEKQKVAE 593
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
405-795 |
3.29e-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: 41.73 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 405 EENQH--STSEELQATLQELADLQQITQELNSENERLGEEKVILM----ESLCQQSDKLEHFGRQIEYFRSLLDEhhisy 478
Cdd:pfam10174 67 EENQHlqLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelteENFRRLQSEHERQAKELFLLRKTLEE----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 479 videdvksgryMELEQRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGAlKERSHHMERIIESEQKGKA 557
Cdd:pfam10174 142 -----------MELRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIAEA-EMQLGHLEVLLDQKEKENI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 558 ALAATLeEYKATVASDQIEMNRLKAQLEKEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDL------ 631
Cdd:pfam10174 210 HLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSL--------ERNIRDLEDEVQMLKTNGLLHTEDREEEIkqmevy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 632 -AHT---RNDANRLQDTIAKVEDEYRAFQ----------EEAKKQIEDLNMTL--------------EKLRSELEEKETE 683
Cdd:pfam10174 281 kSHSkfmKNKIDQLKQELSKKESELLALQtkletltnqnSDCKQHIEVLKESLtakeqraailqtevDALRLRLEEKESF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 RSDMKETIFELEDE--VEQHRAVKLHDNLIISD-----LENTVKKLQDQKHDLERENKTLHRR---LREESAEWRQFQAD 753
Cdd:pfam10174 361 LNKKTKQLQDLTEEksTLAGEIRDLKDMLDVKErkinvLQKKIENLQEQLRDKDKQLAGLKERvksLQTDSSNTDTALTT 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 564397587 754 LQTAVVIANDI-----------KSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 795
Cdd:pfam10174 441 LEEALSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
541-805 |
4.32e-03 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 40.58 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 541 RSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL-KAQLEKEKQKVAELYSIHNSgdksdiqdLLESVRLDKEK 619
Cdd:pfam09755 22 TREQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALrQASVNIQAKAEQEEEFISNT--------LLKKIQALKKE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 620 AETLASSLQEDLAHTRNDANR--LQDTIAKVEDEyRAFQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDE 697
Cdd:pfam09755 94 KETLAMNYEQEEEFLTNDLSRklTQLRQEKVELE-QTLEQEQEYQVNKLMRKIEKLEAETLNKQTNLEQLRREKVELENT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 698 VEQHRavklhdnliisdlENTVKKLQDQKHDLERENKTLHRRLRE---ESAEWRQFQADLQTAVVIANDIKSeAQEEIGD 774
Cdd:pfam09755 173 LEQEQ-------------EALVNRLWKRMDKLEAEKRLLQEKLDQpvsAPPSPRDSTSEGDTAQNLTAHIQY-LRKEVER 238
|
250 260 270
....*....|....*....|....*....|..
gi 564397587 775 LKRRLHEAQ-EKNEKLTKELEEIKSRKQEEER 805
Cdd:pfam09755 239 LRRQLATAQqEHTEKMAQYAQEERHIREENLR 270
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-803 |
4.84e-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: 41.16 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 517 LSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQkgkaalaatleEYKATVASDQIEMNRLKAQLEKEKQKVAELYS 596
Cdd:TIGR04523 347 LKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 597 -IHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFqeeaKKQIEDLNMTLEKLR 674
Cdd:TIGR04523 413 qIKKlQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 675 SELEEKETERSDMKETIFELEDEVeqhraVKLHDNliISDLENTVKKLQDQKHDLERENKTLHRRLREESAEWRQFQADl 754
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKV-----KDLTKK--ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE- 560
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 564397587 755 qtavvianDIKSEAQEEIgdlkRRLHEAQEKNEKLTKELEEIKSRKQEE 803
Cdd:TIGR04523 561 --------KEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
468-806 |
5.57e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 40.42 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 468 RSLLDEHHISyvideDVKSGRYMELEQRymDLAENARFEREQLLGVQqhlsNTLKMAEQDNKEAQEMIGALKERS----H 543
Cdd:smart00806 52 SYELEELSLH-----DIKDGSVLVLNVE--ELDEVKKHIDDEIDTLQ----NELDEVKQALESQREAIQRLKERQqnsaA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 544 HMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAqLEKEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETL 623
Cdd:smart00806 121 NIARPAASPSPVLASSSSAISLANNPDKLNKEQRAELKS-LQRELAVLRQTHNSFFTEIKESIKDILEKIDKFKSSSLSA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 624 ASS------------LQEDLAHTRNDANRLQDTI-AKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKE----TERSD 686
Cdd:smart00806 200 SGSsnrayvesskkkLSEDSDSLLTKVDDLQDIIeALRKDVAQRGVRPSKKQLETVQKELETARKELKKMEeyidIEKPI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 687 MK---ETifELEDEVEQHRAVKLHDNLIisdlentvkklQDQKHDLERENKTLHrrLREESAEWRQFQADLQTAVVIA-- 761
Cdd:smart00806 280 WKkiwEA--ELDKVCEEQQFLTLQEDLI-----------ADLKEDLEKAEETFD--LVEQCCEEQEKGPSKNRNKPVSlp 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 564397587 762 -------NDIKSEAQEEIGDLK----RRLhEAQEKNEKL-TKELEEIKSRKQEEERG 806
Cdd:smart00806 345 vptpgtfNDLKDQVLMEVRALKpdheSRL-EAIERAEKLrEKELEYRRVDEFEKELG 400
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
536-817 |
6.25e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 536 GALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKaqlEKEKQKVAELYSIHNSGDKSDIqdllESVRL 615
Cdd:pfam02029 56 GGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVA---ERKENNEEEENSSWEKEEKRDS----RLGRY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 616 DKEKAETLASSLQEDLAHTrnDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKETERS--DMKETIFE 693
Cdd:pfam02029 129 KEEETEIREKEYQENKWST--EVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 694 LEDEV--EQHRAVKLHDNLIISDLENTVKKLQDQKHDLERENK--TLHRRLRE-ESAEWRQFQADLQTAVVIANDIKSEA 768
Cdd:pfam02029 207 VKSQNgeEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKleELRRRRQEkESEEFEKLRQKQQEAELELEELKKKR 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 564397587 769 QEeigdlKRRLHEA------QEKNEKLTKELEEIKSRKQEEERGRvynyMNAVER 817
Cdd:pfam02029 287 EE-----RRKLLEEeeqrrkQEEAERKLREEEEKRRMKEEIERRR----AEAAEK 332
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
655-822 |
6.72e-03 |
|
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: 40.82 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 655 FQEEAKKQIEDLNMTLEKLRSELEEKETERSDMKETIFELEDEveqhravklhdnliISDLENTVKKLQDQKHDLEREnk 734
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQLEQE-- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 735 tlHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL-----EEI--KSRKQEEERGR 807
Cdd:TIGR02169 732 --EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIqaELSKLEEEVSR 809
|
170
....*....|....*
gi 564397587 808 VYNYMNAVERDLAAL 822
Cdd:TIGR02169 810 IEARLREIEQKLNRL 824
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
728-785 |
9.28e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 38.87 E-value: 9.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 564397587 728 DLERENKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 785
Cdd:PRK10884 97 DLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNQLIVAQKK 154
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
656-819 |
9.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 656 QEEAKKQIEDLNMTLEKLRselEEKETErsdMKETIFELEDEVEQHRAVKlhdNLIISDLEntvKKLQDQKHDLERENKT 735
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIK---KEALLE---AKEEIHKLRNEFEKELRER---RNELQKLE---KRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 736 LHRRLREesaewrqfqadlqtavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVynyMNAV 815
Cdd:PRK12704 105 LEKREEE------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL---LEKV 163
|
....
gi 564397587 816 ERDL 819
Cdd:PRK12704 164 EEEA 167
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
550-802 |
9.82e-03 |
|
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: 40.16 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 550 ESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEKEK-------QKVAELYS------IHNSGDKSDIQDLLESVRLD 616
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKnalqeqlQAETELCAeaeemrARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 617 KEKAETLASSLQEDlahTRNDANRLQDTIAKVEDEYRAFQE--------EAK-KQIEDLNMTLE----KLRSELEEKETE 683
Cdd:pfam01576 84 LEEEEERSQQLQNE---KKKMQQHIQDLEEQLDEEEAARQKlqlekvttEAKiKKLEEDILLLEdqnsKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397587 684 RSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDLERenktLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEK----AKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 564397587 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE 275
|
|
| |
