|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
972-1083 |
1.53e-80 |
|
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: 257.65 E-value: 1.53e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 972 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGI 1051
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462558749 1052 KPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
972-1083 |
7.27e-78 |
|
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: 250.36 E-value: 7.27e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 972 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGI 1051
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462558749 1052 KPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
966-1084 |
9.34e-69 |
|
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: 225.34 E-value: 9.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 966 KDPLAALAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEA 1045
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462558749 1046 AESVGIKPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET 1084
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
979-1082 |
5.79e-35 |
|
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: 129.02 E-value: 5.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEL 1057
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
981-1082 |
8.29e-35 |
|
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: 128.23 E-value: 8.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 981 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSE 1059
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 2462558749 1060 MLY-TDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21200 83 MVRmGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
984-1082 |
6.58e-32 |
|
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: 120.22 E-value: 6.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 984 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELSEMLYT 1063
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 2462558749 1064 DRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
982-1082 |
1.51e-30 |
|
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: 116.23 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 982 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEM 1060
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 2462558749 1061 LYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
979-1082 |
1.77e-30 |
|
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: 115.97 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIkPSLEL 1057
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGI-AKLLD 80
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
975-1082 |
9.02e-30 |
|
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: 114.55 E-value: 9.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 975 EYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAESVGIKP 1053
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 2462558749 1054 SLELSEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
979-1082 |
1.31e-29 |
|
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: 113.64 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 1057
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
979-1080 |
1.76e-29 |
|
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: 113.55 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPS-LEL 1057
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQlLDV 80
|
90 100
....*....|....*....|...
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYK 1080
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
979-1082 |
9.59e-29 |
|
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: 111.25 E-value: 9.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 1057
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
981-1080 |
5.08e-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: 109.40 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 981 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVG-IKPSLELSE 1059
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 2462558749 1060 MLYTDRPDWQSVMQYVAQIYK 1080
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
979-1082 |
6.00e-28 |
|
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: 108.98 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 1057
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 2462558749 1058 SEMLYT-DRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21258 81 EDMMIMgKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
984-1082 |
4.73e-27 |
|
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: 106.47 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 984 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELSEMLYT 1063
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 2462558749 1064 DRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
983-1083 |
4.97e-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: 106.28 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 983 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEML 1061
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 2462558749 1062 YTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
979-1083 |
1.03e-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: 105.25 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELS 1058
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
979-1082 |
1.33e-26 |
|
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: 104.94 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 1057
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLD- 82
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
979-1082 |
1.03e-25 |
|
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: 102.35 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESV-GIKPSLEL 1057
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 2462558749 1058 SEMLYTDR-PDWQSVMQYVAQIYKYF 1082
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
980-1082 |
1.10e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 102.23 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 980 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLELS 1058
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
979-1082 |
5.51e-24 |
|
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: 97.46 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 1057
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21189 80 PEDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
978-1083 |
6.61e-24 |
|
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: 97.49 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 978 GSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLE 1056
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 2462558749 1057 LSEMLyTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
977-1083 |
8.18e-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: 8.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 977 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSL 1055
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 2462558749 1056 ELSEMLYTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
979-1083 |
1.11e-23 |
|
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: 96.94 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEL 1057
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYFE 1083
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
981-1082 |
1.32e-22 |
|
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: 93.78 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 981 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSE 1059
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 2462558749 1060 MLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
980-1082 |
1.72e-22 |
|
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: 93.41 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 980 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLELS 1058
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
981-1084 |
2.60e-22 |
|
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: 92.73 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 981 RNALLKWCQKKTQGY-ANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKR--NLLLAFEAAE-SVGIKPSLE 1056
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83
|
90 100
....*....|....*....|....*...
gi 2462558749 1057 LSEMLYTdrPDWQSVMQYVAQIYKYFET 1084
Cdd:pfam00307 84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
979-1082 |
8.56e-22 |
|
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: 91.66 E-value: 8.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 1057
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
979-1082 |
1.83e-21 |
|
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: 90.49 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLElS 1058
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82
|
90 100
....*....|....*....|....
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
984-1080 |
2.35e-21 |
|
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: 89.79 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 984 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-ESVGIKPSLElSEMLY 1062
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 2462558749 1063 TDRPDWQSVMQYVAQIYK 1080
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
979-1082 |
4.81e-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: 89.76 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 1057
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
979-1082 |
2.89e-20 |
|
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: 87.08 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 1057
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
979-1082 |
3.37e-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: 87.42 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 1057
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
977-1082 |
4.42e-20 |
|
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: 86.60 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 977 GGSKRnALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIkPSL 1055
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI-PRL 81
|
90 100
....*....|....*....|....*..
gi 2462558749 1056 ELSEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
979-1082 |
8.65e-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: 86.28 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 1057
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
979-1082 |
1.40e-19 |
|
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: 85.55 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 1057
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
979-1082 |
1.49e-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: 85.52 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 1057
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
982-1078 |
4.49e-19 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 83.13 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 982 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY----QELNSQEKKRNLLLAFEAAESVGIKPSLEL 1057
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQI 1078
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
983-1082 |
3.50e-18 |
|
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: 80.97 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 983 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEmL 1061
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 2462558749 1062 YTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
979-1082 |
6.39e-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: 77.33 E-value: 6.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLElS 1058
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
979-1084 |
8.55e-17 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 85.38 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYAN-IDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQ--EKKRNLLLAFEAAE-SVGIKPS 1054
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 2462558749 1055 LELSEMLYTDRPDWQSVMQYVAQIYKYFET 1084
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
981-1080 |
1.68e-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: 76.22 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 981 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY---QELNSQEKKRNLLLAFEAAESVGIkPSLEL 1057
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGL-PELDL 79
|
90 100
....*....|....*....|....*
gi 2462558749 1058 --SEMLYtDRPDWQSVMQYVAQIYK 1080
Cdd:cd00014 80 fePEDLY-EKGNLKKVLGTLWALAL 103
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
979-1082 |
1.60e-15 |
|
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: 73.33 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELS 1058
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
|
90 100
....*....|....*....|....
gi 2462558749 1059 EMLYTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21244 85 EDVDVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
983-1082 |
3.21e-15 |
|
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: 72.52 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 983 ALLKWCQKKTQGYAnIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-ESVGIKPSLElSEML 1061
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 2462558749 1062 YTDRPDWQSVMQYVAQIYKYF 1082
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
979-1077 |
5.48e-15 |
|
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: 71.88 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYAnidITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 1056
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|.
gi 2462558749 1057 LSEMLYTDrPDWQSVMQYVAQ 1077
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLSY 97
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
977-1083 |
6.66e-14 |
|
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: 68.92 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 977 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSL 1055
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90 100
....*....|....*....|....*...
gi 2462558749 1056 ELSEMLYTDRPdwQSVMQYVAQIYKYFE 1083
Cdd:cd21196 81 SAQAVVAGSDP--LGLIAYLSHFHSAFK 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-742 |
1.98e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENhhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 457
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 458 RvkNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 537
Cdd:TIGR02168 752 L--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 538 NNMMAKTLEECRVTLEGLKMENGSLK--------SHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNE 608
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSedieslaaEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 609 LRQELLKANGEIKHVSSLLAKVRRD-SSLLVEkdysyLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 687
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRlEGLEVR-----IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558749 688 VEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 742
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
982-1077 |
3.11e-13 |
|
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: 66.56 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 982 NALLKWCQKKTQgyaNIDITNFSSSWSDGLAFCALLHTyLPAHIP-YQELNSQEKKRNLLLAFEAAESVGIKPSLELSEM 1060
Cdd:cd21185 4 KATLRWVRQLLP---DVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 2462558749 1061 lyTDrPDWQS--VMQYVAQ 1077
Cdd:cd21185 80 --AD-PEVEHlgIMAYAAQ 95
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
984-1080 |
3.99e-13 |
|
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: 66.88 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 984 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKK-RNLLLAFEAAE-SVGIKPSLElSEML 1061
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 2462558749 1062 YTDRPDWQSVMQYVAQIYK 1080
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
979-1079 |
3.26e-11 |
|
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: 61.19 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 1057
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 2462558749 1058 SEMLYTDRPDWQSVMQYVAQIY 1079
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
982-1076 |
4.58e-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: 61.55 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 982 NALLKWCQKKTQGYaNIDITNFSSSWSDGLAFCALLHTYLPAHIP----------------------------------- 1026
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462558749 1027 -YQELNSQEkKRNLLLAFEAAESVG-IKPSLELSEMLYTdRPDWQSVMQYVA 1076
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELGgVPALLRASDMSNT-IPDEKVVILFLS 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-783 |
4.67e-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: 67.39 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 479 TGILEQGRfEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEEcrvtlEGLKME 558
Cdd:TIGR02168 670 SSILERRR-EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-----LEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 559 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLV 638
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 639 EKDYSYLKEI--CDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQK 716
Cdd:TIGR02168 824 ERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558749 717 SDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 783
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
984-1080 |
7.17e-11 |
|
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: 59.97 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 984 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLElSEMLY 1062
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 2462558749 1063 TDRPDWQSVMQYVAQIYK 1080
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
375-788 |
1.01e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 444
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 445 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 521
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 522 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 592
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 593 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYsyLKEICDH 651
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED--LEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 652 QAEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSD 718
Cdd:PRK02224 528 RRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 719 LER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 787
Cdd:PRK02224 608 IERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
.
gi 2462558749 788 G 788
Cdd:PRK02224 688 N 688
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
374-789 |
1.40e-10 |
|
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: 65.58 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 374 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 451
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 452 -MNLLQERVKNEEPTTQ---------EGKIIELEqkctgileqgrfEREKLLNIQQQLTCSLRKVEEENQGalEMIKRLK 521
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLE------------EDILLLEDQNSKLSKERKLLEERIS--EFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 522 EENEKLNEFLELeRHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAvEQTAESCEVQEMLkvARAEKDL 601
Cdd:pfam01576 170 EEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQL--AKKEEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 602 ------LELSCNElRQELLKANGEIK-HVSSLL-------------AKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSL 661
Cdd:pfam01576 246 qaalarLEEETAQ-KNNALKKIRELEaQISELQedleseraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 662 KLQE-----KASES-----DAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLT 727
Cdd:pfam01576 325 REQEvtelkKALEEetrshEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558749 728 kQMKEETEEWRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRKLLEEEEKNARLQKELGDVQGH 789
Cdd:pfam01576 398 -QAKQDSEHKRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
372-782 |
1.59e-10 |
|
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: 65.43 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 372 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 450
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 451 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 530
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 531 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 596
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 597 AEKDLLELSCNELRQELLKANGEIKhvssllakvrrdsSLLVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEI 674
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIE-------------KLKKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 675 KDMKETIFELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTA 747
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
410 420 430
....*....|....*....|....*....|....*
gi 2462558749 748 VvvandikceaqQELRTVKRKLLEEEEKNARLQKE 782
Cdd:TIGR04523 495 E-----------KELKKLNEEKKELEEKVKDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-781 |
2.28e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 384 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 463
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 464 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKRLK-----------EENEK--LNEF 530
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKAKgkcpvcgreltEEHRKelLEEY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 531 -LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnEL 609
Cdd:PRK03918 458 tAELKR-----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 610 RQELLKANGEIKHVSSLLAKVRrdsslLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE---- 685
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLE-----ELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyn 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 686 ------DQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLER---QLKTLTK--------QMKEETEEWRRFQADLQTAV 748
Cdd:PRK03918 603 eylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKkyseeeyeELREEYLELSRELAGLRAEL 682
|
410 420 430
....*....|....*....|....*....|...
gi 2462558749 749 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQK 781
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-654 |
5.56e-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: 63.92 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 450
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 451 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 525
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 526 KLNEflELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 605
Cdd:TIGR02168 397 SLNN--EIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462558749 606 CNELRQELLKANGEIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAE 654
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENL-EGFSEGVKALLKNQSG 517
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
378-783 |
2.02e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.91 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 450
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 451 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 517
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 518 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 597
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 598 EKDLLELSCNELRQELLKANGEIK-----------HVSSLLAKVRRDSSLLVEKDYSYLKEIcdHQAEQLSRTSLKLQEK 666
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQElqqryaelcaaAITCTAQCEKLEKIHLQESAQSLKERE--QQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 667 ASESDAEIKDMKETIFELEDQvEQHRAVKLH-------NNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRR 739
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGS-CIHPNPARQdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462558749 740 FQADLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 783
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-783 |
2.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 517 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 596
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 597 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEkdysylkeicdhQAEQLSRTSLKLQEKASESDAEIKD 676
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE------------RRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 677 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKc 756
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL- 413
|
250 260
....*....|....*....|....*..
gi 2462558749 757 EAQQELRTVKRKLLEEEEKNARLQKEL 783
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEE 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-643 |
4.49e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 535 RhnnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscnELRQELL 614
Cdd:COG1196 407 E--------AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL---LEEAALL 475
|
250 260
....*....|....*....|....*....
gi 2462558749 615 KANGEIKHVSSLLAKVRRDSSLLVEKDYS 643
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
359-782 |
4.62e-09 |
|
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: 60.51 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 359 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELT-----------------AENE 421
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 422 KLVDEKTiletsfhQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQ 498
Cdd:pfam05483 419 KLLDEKK-------QFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 499 LTCSLRKVEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEA 576
Cdd:pfam05483 492 AHCDKLLLENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEV 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 577 SAVEQTAESCEVQEMLKVARAEKDL--LELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYlkEICDHQAE 654
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY--EIKVNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 655 -QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQMKE 732
Cdd:pfam05483 643 lELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462558749 733 ETEEWRRFQADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 782
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-784 |
6.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 382 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 458
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 459 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 526
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 527 LNEFLELERHNNNMMAKtLEECRVTLEGLKmengSLKSHLQGEKQKATEASaVEqtaescEVQEMLKVARAEKDLLELSC 606
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRLTGLT-PE------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 607 NELRQELLKANGEIKHVSSLLAKVRRdssllvekdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELED 686
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK------------AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 687 QVEQHRAVKLHNNQLISElESSVIKLE---EQKSDLERQLKTLT-KQMKEETEEWRRFQADLQT----AVVVANDIK--C 756
Cdd:PRK03918 474 KERKLRKELRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklE 552
|
410 420
....*....|....*....|....*...
gi 2462558749 757 EAQQELRTVKRKLLEEEEKNARLQKELG 784
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELE 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
503-793 |
1.66e-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: 58.91 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 503 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMM---AKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 579
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELeelTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 580 EQtaESCEVQEMLKVARAEkdllelscnELRQELLKANGEIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAEQLSRT 659
Cdd:TIGR02168 296 EI--SRLEQQKQILRERLA---------NLERQLEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 660 SLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ------- 729
Cdd:TIGR02168 364 EAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaele 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558749 730 -MKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 793
Cdd:TIGR02168 444 eLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-780 |
3.33e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHhstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKLMNL--- 454
Cdd:COG4717 73 LKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELper 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 ---LQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEK 526
Cdd:COG4717 148 leeLEERLEElreleEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 527 LNEflELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEAS 577
Cdd:COG4717 225 LEE--ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 578 AVEQTAESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvekdysYLKEICDHQAEQL 656
Cdd:COG4717 303 EAEELQALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------QLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 657 SR---TSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEE 733
Cdd:COG4717 377 AEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462558749 734 TEEWRRFQADLQTAVvvANDIKCEAQQELRTVKRKLLEEEEKNARLQ 780
Cdd:COG4717 452 REELAELEAELEQLE--EDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
979-1077 |
4.14e-08 |
|
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: 52.00 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTQGyanIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 1056
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|.
gi 2462558749 1057 LSEMLYTDrPDWQSVMQYVAQ 1077
Cdd:cd21230 78 PEEIINPN-VDEMSVMTYLSQ 97
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
408-825 |
5.39e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 408 DQQQMVQELTAE-NEKLVDEKTILETSFH--QHRERAEQlSQENEKLMNLLQERVKNEepttQEGKIIELEQKCTgiLEQ 484
Cdd:pfam17380 248 DVTTMTPEYTVRyNGQTMTENEFLNQLLHivQHQKAVSE-RQQQEKFEKMEQERLRQE----KEEKAREVERRRK--LEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 485 GRFEREKLLNIQQQLTCSLRKVEEENQGALEmikRLKEENEKLneflELERHNNNMMAKTLEECRvTLEGLKMENGSLKS 564
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQERMAMERERELE---RIRQEERKR----ELERIRQEEIAMEISRMR-ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 565 HLQGEKQKATEASAVEQtaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKhvSSLLAKVRRDssllvEKDYSY 644
Cdd:pfam17380 393 RVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLE-----EQERQQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 645 LKEICDHQAEQLSRTSLKLqEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELE----SSVIKLEEQKSDLE 720
Cdd:pfam17380 461 QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerQKAIYEEERRREAE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 721 RQLKTltkqmKEETEEWRRFQAdlQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARL------------------QKE 782
Cdd:pfam17380 540 EERRK-----QQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQIVESEKARAEYeattpittikpiyrprisEYQ 612
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462558749 783 LGDVQGHGRVVTSR----AAPPPVDEEPESSEVDAAGRWPGVCVSRT 825
Cdd:pfam17380 613 PPDVESHMIRFTTQspewATPSPATWNPEWNTVTAEEETPGIPIIHS 659
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
396-789 |
8.46e-08 |
|
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: 56.52 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 396 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhreRAEQLSQENEKLMNLLQErvkneEPTTQEGKIIELE 475
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL--------QETRKKAVVLARLLELQE-----EPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 476 QKCTGILEQGRFER--EKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKL-NEFLELERHNN------NMMAKTLE 546
Cdd:TIGR00618 515 PARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNrskediPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 547 ECRVTLEGLKMENGSLKSHLQGEKQKATEASA---VEQTAESCEVQEMLKVARAEKDLLELSCNELR--------QELLK 615
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdVRLHLQQCSQELALKLTALHALQLTLTQERVRehalsirvLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 616 ANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASES-DAEIKDMKETIFELEDQVEQHRAV 694
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSlGSDLAAREDALNQSLKELMHQART 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 695 KLHNNQLI----SELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLL 770
Cdd:TIGR00618 755 VLKARTEAhfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
410
....*....|....*....
gi 2462558749 771 EEEEKNARLQKELGDVQGH 789
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLK 853
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-782 |
2.06e-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: 55.46 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 367 GSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLS 445
Cdd:TIGR02169 664 GGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 446 qenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRLKEE 523
Cdd:TIGR02169 744 ---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 524 NEKLNEflelerhnnnmmaktleecrvtleglkmengslkshLQGEKQKATEASAVEQtAESCEVQEMLKVARAEKDLLE 603
Cdd:TIGR02169 818 EQKLNR------------------------------------LTLEKEYLEKEIQELQ-EQRIDLKEQIKSIEKEIENLN 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 604 LSCNELRQELLKANGEIKHVSSLLAKVRRDSSllvekdysylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFE 683
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERD--------------------------ELEAQLRELERKIEELEAQIEK 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 684 LEDQVEQHRAVKLHNNQLISELESSVIKLEEQkSDLERQLKTLTKQMKEETEEWRRFQadlqtavvvanDIKCEAQQELR 763
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYE 982
|
410
....*....|....*....
gi 2462558749 764 TVKRKLLEEEEKNARLQKE 782
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-816 |
2.55e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 402 LEELEEAEE--ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 535 RHNNNMMAK------TLEECRVTLEGLkmENGSLKSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNE 608
Cdd:COG1196 480 AELLEELAEaaarllLLLEAEADYEGF--LEGVKAALLLAGLRGLAGAVAVLIGVE--AAYEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 609 LRQ-----ELLKANGE----------IKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAE 673
Cdd:COG1196 556 DEVaaaaiEYLKAAKAgratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 674 IKDMKETIFELEDQVEQHRAVklhnNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVAND 753
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGG----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558749 754 IKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGR 816
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
439-817 |
2.78e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 439 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 515
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 516 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 595
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 596 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRdssllvekdysylkeicdhQAEQLSRTSLKLQEKASESDAEIK 675
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-------------------ELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 676 DMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandik 755
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-------- 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558749 756 cEAQQELRTVKRKLLEEEEKNARLQ----KELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRW 817
Cdd:COG1196 483 -LEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
396-812 |
4.36e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 396 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 475
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 476 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 555
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 556 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVRRD 633
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 634 SSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAE--IKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIK 711
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 712 LEEQKSDLE--RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN--ARLQKELGDVQ 787
Cdd:PTZ00121 1691 AEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEEKKA 1770
|
410 420
....*....|....*....|....*
gi 2462558749 788 GHGRVVTSRAAPPPVDEEPESSEVD 812
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-699 |
5.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 535 RHNnnmmAKTLEECRVTLEGL-KMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDL-LELSCNELRQE 612
Cdd:COG1196 389 LEA----LRAAAELAAQLEELeEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAeLEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 613 LLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHR 692
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
....*..
gi 2462558749 693 AVKLHNN 699
Cdd:COG1196 545 AAALQNI 551
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-792 |
6.46e-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: 53.92 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 397 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNL--LQERVKNEEPTTQEGKIIEL 474
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 475 EQKctgiLEQGRFEREKLLNIQQQLTcslRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEG 554
Cdd:TIGR02169 236 ERQ----KEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 555 LKMENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRR 632
Cdd:TIGR02169 306 LERSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 633 DSSLLVEKDYSYLKEICDHQAEQ--LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVklhnnqlISELESSVI 710
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 711 KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHG 790
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLG 531
|
..
gi 2462558749 791 RV 792
Cdd:TIGR02169 532 SV 533
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
443-783 |
7.86e-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: 53.19 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 443 QLSQENEKLMNL---LQERVKNEEPTTQEG-KIIELEQKCtgiLEQGRFEREKL-LNIQQQLTCSlRKVEEENQGALEMI 517
Cdd:pfam05483 82 KLYKEAEKIKKWkvsIEAELKQKENKLQENrKIIEAQRKA---IQELQFENEKVsLKLEEEIQEN-KDLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 518 KRLKE----ENEKLNEFlELERH---------NNNM--MAKTLEECRVtleglKMENGSLKSHLQgEKQKATEASAVEQt 582
Cdd:pfam05483 158 NLLKEtcarSAEKTKKY-EYEREetrqvymdlNNNIekMILAFEELRV-----QAENARLEMHFK-LKEDHEKIQHLEE- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 583 aescEVQEMLKVARAEKDLLELSCNElrqellKANgEIKHVSSLLAKVRRDSSLLVEK------DYSYLKEICDHQAEQL 656
Cdd:pfam05483 230 ----EYKKEINDKEKQVSLLLIQITE------KEN-KMKDLTFLLEESRDKANQLEEKtklqdeNLKELIEKKDHLTKEL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 657 SRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ 729
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558749 730 MKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KRKLLEEEEKNARLQKEL 783
Cdd:pfam05483 379 LKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEKKQFEKIAEEL 434
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
378-787 |
1.01e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEEN-HHSTAEELQATLQELSDQQQMVQELTAENEklvdektilETSFHQHRERAEQLSQENEKLMNLLQ 456
Cdd:TIGR00606 593 LAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDE---------ESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 457 ERVKNEEPTTQEgkiielEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERH 536
Cdd:TIGR00606 664 VYSQFITQLTDE------NQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 537 NNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--------EVQEMLK---------VARAEK 599
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKdverkiaqqAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 600 DLLELSCNELRQELLKANGEIKHVSS---LLAKVRRDSSLLVEKDYSYLKEICDH---------QAEQLSRTSLKLQEKA 667
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSkieLNRKLIQDQQEQIQHLKSKTNELKSEklqigtnlqRRQQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 668 SESDAEIKDMKETIFELE-----DQVEQHRAV-KLHNNQLISELESSVIK--------------------LEEQKSDLER 721
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLEtflekDQQEKEELIsSKETSNKKAQDKVNDIKekvknihgymkdienkiqdgKDDYLKQKET 977
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558749 722 QLKTLTKQMKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRKLLEEEEKNARLQKELGDVQ 787
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
587-796 |
1.04e-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: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 587 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKVRrdsSLLVEKDYSYLKEICDHQAEQLSRtslkLQEK 666
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALR---LWFAQRRLELLEAELEELRAELAR----LEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 667 ASESDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 745
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462558749 746 TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 796
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
517-783 |
1.22e-06 |
|
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: 52.75 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 517 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLqgEKQKATEASAVEQ----TAESCEVQEML 592
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREEL--EELQEELKEAEEEleelTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 593 KVARAEKDLLELSCNELRQELLKANGEIKHVSS--LLAKVRRDSSLLVEKDYSY----LKEICDHQAEQLSRTSLKLQEK 666
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQqkQILRERLANLERQLEELEAqleeLESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 667 ASESD---AEIKDMKETIFELEDQVEQHRA---------------VKLHNNQL------ISELESSVIKLEEQKSDLERQ 722
Cdd:TIGR02168 350 KEELEsleAELEELEAELEELESRLEELEEqletlrskvaqlelqIASLNNEIerlearLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558749 723 LKTLTKQ-MKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 783
Cdd:TIGR02168 430 LEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
397-731 |
1.49e-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: 52.33 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 397 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 475
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 476 QKctgileqgrFEREKLLNiqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 548
Cdd:TIGR04523 398 SK---------IQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 549 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 626
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 627 LAKVRRDSSllvEKDYSYLKEICDHQaeqlsrtslklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELE 706
Cdd:TIGR04523 544 EDELNKDDF---ELKKENLEKEIDEK-----------NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE 609
|
330 340
....*....|....*....|....*
gi 2462558749 707 SSVIKLEEQKSDLERQLKTLTKQMK 731
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIK 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
378-761 |
1.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHHSTAEELQATLQELS-DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLq 456
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 457 ERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVeeenqgALEMIKRLKEENEKLNEFLELERH 536
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL------ALLFLLLAREKASLGKEAEELQAL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 537 NNNMMAKTLEECRVtLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD-LLELSCNELRQELLK 615
Cdd:COG4717 311 PALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 616 ANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravk 695
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE---------- 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558749 696 lhnnQLISELESSvikleEQKSDLERQLKTLTKQMKEETEEWRRfqadLQTAVVVANDIKCEAQQE 761
Cdd:COG4717 460 ----AELEQLEED-----GELAELLQELEELKAELRELAEEWAA----LKLALELLEEAREEYREE 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
515-783 |
1.74e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 515 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 593
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 594 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVRRDSSllvekdysylKEIcdHQAEQLSRTSLK-----LQE 665
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG----------KKI--YEHDSMSTMHFRslgsaISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 666 KASESDAEIKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTL 726
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEII 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558749 727 TKQMKEETEEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 783
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
587-900 |
1.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 587 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAEQLSRTSlklqek 666
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARALYRSG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 667 ASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEwrrfQADLQT 746
Cdd:COG3883 100 GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 747 AVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRWPGVCVSRTS 826
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558749 827 PTPPESATTVKSLIKSFDLGRPGGAGQNISVHKTPRSPLSGIPVRTAPAAAVSPMQRHSTYSSVRPASRGVTQR 900
Cdd:COG3883 256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAG 329
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
984-1056 |
1.90e-06 |
|
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: 47.68 E-value: 1.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558749 984 LLKWCQK--KTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIP----YQELNSQEKKRNLLLAFEAAESVGIKPSLE 1056
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLT 93
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
483-789 |
5.81e-06 |
|
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: 50.74 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 483 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 558
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 559 NGSLKSHLQGEKQKATEASAVE-------------QTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSS 625
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVlkenkeeekekklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 626 LLAKVRRDSSLL--VEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQhravklhNNQLIS 703
Cdd:pfam02463 329 ELKKEKEEIEELekELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE-------ELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 704 ELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVvandIKCEAQQELRTVKRKLLEEEEKNARLQKEL 783
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT----EEKEELEKQELKLLKDELELKKSEDLLKET 477
|
....*.
gi 2462558749 784 GDVQGH 789
Cdd:pfam02463 478 QLVKLQ 483
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
404-770 |
9.07e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 404 QELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM-NLLQERvkneeptTQEGKIIELeqkctgiL 482
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRkSLLANR-------FSFGPALDE-------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 483 EqgrferEKLLNIQQQLTcslRKVEEENQG----ALEMIKRLKEENEKLNEFLE----LERHNNNMMAKTLEECRVTLEG 554
Cdd:PRK04778 171 E------KQLENLEEEFS---QFVELTESGdyveAREILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 555 LKMENGSLKsHLQGEKqkateasaveqtaescEVQEML-KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvrrd 633
Cdd:PRK04778 242 LVEEGYHLD-HLDIEK----------------EIQDLKeQIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 634 ssllvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQLISELESSVIKL 712
Cdd:PRK04778 299 -----EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-YTLnESELESVRQLEKQLESLEKQYDEITERI 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558749 713 EEQK---SDLERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDIKCEAQQELRTVKRKLL 770
Cdd:PRK04778 372 AEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
542-755 |
1.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 542 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 619
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 620 IKHVSSLLAKVRR-----------------DSSLLVEKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 679
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558749 680 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 755
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
488-786 |
2.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 488 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 567
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 568 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysy 644
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 645 LKEicdhqAEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSD 718
Cdd:PRK03918 330 IKE-----LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 719 LERQLKTLTkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN--ARLQKELGDV 786
Cdd:PRK03918 403 IEEEISKIT----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKEllEEYTAELKRI 464
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
379-777 |
2.77e-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: 48.50 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 379 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 458
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 459 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQgalemIKRLKEENEKLNEFLELERHNN 538
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-----VQQVNQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 539 NMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAE--SCEVQEMLKVARAEKDlLELSCNELRQELLKA 616
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVelSTEVQSLIREIKDAKE-QDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 617 NGEIKHVSSLLAKVRRDSSLLVEKD-----------YSYLKEICDHQAEQ----LSRTSLKLQEKASESDAEIKDMKETI 681
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvknihgymkdiENKIQDGKDDYLKQketeLNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 682 FELEDQVEQHRAVKlhnNQLiselesSVIKLEEQKSDLERQLKTLTKQMK-----EETEEWRRFQADLQTavVVANDIKC 756
Cdd:TIGR00606 1005 QDIDTQKIQERWLQ---DNL------TLRKRENELKEVEEELKQHLKEMGqmqvlQMKQEHQKLEENIDL--IKRNHVLA 1073
|
410 420
....*....|....*....|....*.
gi 2462558749 757 EAQQ-----ELRTVKRKLLEEEEKNA 777
Cdd:TIGR00606 1074 LGRQkgyekEIKHFKKELREPQFRDA 1099
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-683 |
3.05e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 379 ASLTEKIQKMEENH-HSTAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKLmnLLQE 457
Cdd:TIGR00618 602 KLSEAEDMLACEQHaLLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPK--ELLA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 458 RVKNEEPTTQEgkiieLEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERH 536
Cdd:TIGR00618 677 SRQLALQKMQS-----EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 537 NNNMMAKTLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELl 614
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE- 830
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 615 kangeikhvSSLLAKVRRDSSLLVEKDYSYLK-EICDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 683
Cdd:TIGR00618 831 ---------EQFLSRLEEKSATLGEITHQLLKyEECSKQLAQLTQEQAKIIQL--SDKLNGINQIKIQFD 889
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
398-749 |
3.25e-05 |
|
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: 48.25 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 398 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIE-LE 475
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 476 QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE----NQGALEMIKRLKEENEKLNEFLELERHNNnmmaKTLEECRVT 551
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNK----ANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 552 LEGlkmENGSLKSHLQGEKQKATEASAVEQTAEScEVQE-MLKVARAEKDLlelscNELRQELLKANGEIKHVSSLLAKV 630
Cdd:pfam01576 382 LES---ENAELQAELRTLQQAKQDSEHKRKKLEG-QLQElQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 631 RRDSSLLvEKDYSYLKEICDHQAEQLS---RTSLKLQEKASESDAEIKDMKEtifELEDQVEQHRAVKLH----NNQL-- 701
Cdd:pfam01576 453 EGKNIKL-SKDVSSLESQLQDTQELLQeetRQKLNLSTRLRQLEDERNSLQE---QLEEEEEAKRNVERQlstlQAQLsd 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558749 702 ----ISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW-------RRFQADLQTAVV 749
Cdd:pfam01576 529 mkkkLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLV 587
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
977-1077 |
3.27e-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: 44.39 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 977 GGSKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAESVGIKPSL 1055
Cdd:cd21315 14 GPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDWLDVPQL 90
|
90 100
....*....|....*....|..
gi 2462558749 1056 ELSEMLYTDRPDWQSVMQYVAQ 1077
Cdd:cd21315 91 IKPEEMVNPKVDELSMMTYLSQ 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
380-783 |
4.61e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 380 SLTEKIQKMEENH---HSTAEELQATLQE----LSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 448
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEEareaVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 449 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 516
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 517 -----IKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAESCEVqem 591
Cdd:PRK02224 506 eaedrIERLEERREDLEELIAERR-------ETIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAEEARE--- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 592 lKVARAEKDLLELscNELRQELlkanGEIKHVSSLLAKVRRDSSLLVEKdYSYLKEICDHQAEQLSRTSLKLQEKASESD 671
Cdd:PRK02224 573 -EVAELNSKLAEL--KERIESL----ERIRTLLAAIADAEDEIERLREK-REALAELNDERRERLAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 672 aeikdmketifelEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMkEETEEWRRFQADLQtavvva 751
Cdd:PRK02224 645 -------------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALE------ 704
|
410 420 430
....*....|....*....|....*....|..
gi 2462558749 752 ndikcEAQQELRTVKRKLLEEEEKNARLQKEL 783
Cdd:PRK02224 705 -----NRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
503-812 |
5.37e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 503 LRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQT 582
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARE--------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 583 AEscevqemLKVARAEKDLLELSCNELRQELLKANG--------EIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAE 654
Cdd:COG4913 309 AE-------LERLEARLDALREELDELEAQIRGNGGdrleqlerEIERLERELEERERRRARL-EALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 655 QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKlhnNQLISELESsvikLEEQKSDLERQLKTLTKQMKEET 734
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIAS----LERRKSNIPARLLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 735 EEWR---RFQADL----------QTAVVVAndikceaqqeLRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPP 801
Cdd:COG4913 454 GLDEaelPFVGELievrpeeerwRGAIERV----------LGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGL 523
|
330
....*....|.
gi 2462558749 802 VDEEPESSEVD 812
Cdd:COG4913 524 PDPERPRLDPD 534
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
979-1080 |
7.21e-05 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 43.16 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 1056
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCPdWESWDPQKPVDNAREAMQQADDwLGVPQVIT 84
|
90 100
....*....|....*....|....
gi 2462558749 1057 LSEMLYTDrPDWQSVMQYVAQIYK 1080
Cdd:cd21313 85 PEEIIHPD-VDEHSVMTYLSQFPK 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-788 |
8.64e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 451
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 452 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 502
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 503 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 535
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 536 -------------------------------HNNNMMAKTLEECR--------VTLEGLKMEngslKSHLQGEKQKATEA 576
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGELFE----KSGAMTGGSRAPRG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 577 SAVEQTAESCEVQEMlkvaRAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLL------VEKDYSYLKEICD 650
Cdd:TIGR02169 665 GILFSRSEPAELQRL----RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqLEQEEEKLKERLE 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 651 HQAEQLSRTSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLT 727
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558749 728 KQMKEETEEWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 788
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
1000-1062 |
9.56e-05 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 41.90 E-value: 9.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558749 1000 ITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE------KKRNLLLAFEAA-ESVGIKPS-LELSEMLY 1062
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKEsmsladSLYNIQLLQEFCqRHLGNRCChLTLEDLLY 83
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
561-818 |
1.33e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 561 SLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvEK 640
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 641 DYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE 720
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 721 RQ---LKTLTKQMKEEteewrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQghgrvvtsRA 797
Cdd:COG4942 171 AEraeLEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE--------AE 235
|
250 260
....*....|....*....|.
gi 2462558749 798 APPPVDEEPESSEVDAAGRWP 818
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKLP 256
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
979-1080 |
1.61e-04 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 42.37 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 979 SKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIkPSLE 1056
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWESWDPNQPVQNAREAMQQADDwLGV-PQVI 86
|
90 100
....*....|....*....|....
gi 2462558749 1057 LSEMLYTDRPDWQSVMQYVAQIYK 1080
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPK 110
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
378-736 |
1.62e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEEnhhstaeELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 457
Cdd:TIGR00618 551 LTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 458 RVKNEEPTTQEGKIIELEQKctgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 537
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 538 NNMMAKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAVEQTAESCEVQEMLKVARAEKDllelscnelrqELLKAN 617
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQAR-----------TVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 618 GEIKHVSSLLAKVrrdsSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLH 697
Cdd:TIGR00618 760 TEAHFNNNEEVTA----ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFL 834
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462558749 698 NnqLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEE 736
Cdd:TIGR00618 835 S--RLEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQL 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-604 |
1.81e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 363 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 440
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 441 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 520
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 521 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 600
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 2462558749 601 LLEL 604
Cdd:COG4942 225 LEAL 228
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
375-772 |
1.94e-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: 45.49 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 451
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 452 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 526
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 527 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLkvaRAEKDLlels 605
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERL---RAVKDI---- 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 606 cNELRQELLKangEIKhvssllaKVRRDSSLLVEkDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 685
Cdd:pfam15921 652 -KQERDQLLN---EVK-------TSRNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 686 DQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTV 765
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQ 798
|
....*..
gi 2462558749 766 KRKLLEE 772
Cdd:pfam15921 799 ERRLKEK 805
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
397-804 |
2.09e-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: 45.73 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 397 EELQATLQELSDQQQMVQELTAENEKLV----DEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEpttqegKII 472
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELklkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ------ELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 473 ELEQKctgileqgrfEREKLLNIQQQLTCSLRKVEEENqgalEMIKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTL 552
Cdd:pfam02463 247 RDEQE----------EIESSKQEIEKEEEKLAQVLKEN----KEEEKEKKLQEEELKLLAKEE-------EELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 553 EGLKMENGSLKSHLQGEKQKateasaveqtAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRR 632
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKK----------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 633 DSSLLVEKDYSYLKEICDHQAEQLsrtsLKLQEKASESDAEIKDMKETIFELEDQVEqhravKLHNNQLISELESSVIKL 712
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELEL----KSEEEKEAQLLLELARQLEDLLKEEKKEE-----LEILEEEEESIELKQGKL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 713 EEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQ-QELRTVKRKLLEEEEKNARLQKELGDVQGHGR 791
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQkLEERSQKESKARSGLKVLLALIKDGVGGRIIS 526
|
410
....*....|...
gi 2462558749 792 VVTSRAAPPPVDE 804
Cdd:pfam02463 527 AHGRLGDLGVAVE 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
607-779 |
2.24e-04 |
|
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: 45.40 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 607 NELRQELLKANGEIKhvssllakVRRDSSLLVEKDYSYLKEICDHQAEQLSRTS---LKLQEKASESDAEIKDMKETIFE 683
Cdd:TIGR04523 99 NKLNSDLSKINSEIK--------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLteiKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 684 LEDQVE---------QHRAVKLHNNQLISELESSVIKLEEQK--------SDLERQLKTLTKQMKEETEEWRRFQADLQT 746
Cdd:TIGR04523 171 LENELNllekeklniQKNIDKIKNKLLKLELLLSNLKKKIQKnkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190
....*....|....*....|....*....|...
gi 2462558749 747 AVVVANDIKCEAQQELRTVKRKLLEEEEKNARL 779
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
481-781 |
2.31e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 481 ILEQGRFEREKLLNIQQ--QLTCSLRKVEEENQGAL---EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTL--- 552
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEkkELLMNLFPLDQYTQLALmefAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLeke 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 553 -----EGLKMENGSLkSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNEL--RQELLKANGEIKHVSS 625
Cdd:TIGR00618 228 lkhlrEALQQTQQSH-AYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 626 LLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHRAVKLHNNQLISEL 705
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI------HIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 706 EsSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRF------QADLQTAVVVANDiKCEAQQELRTVKRKLLEEEEKNARL 779
Cdd:TIGR00618 379 Q-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsaFRDLQGQLAHAKK-QQELQQRYAELCAAAITCTAQCEKL 456
|
..
gi 2462558749 780 QK 781
Cdd:TIGR00618 457 EK 458
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
375-786 |
3.26e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 454
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERvkNEEPTTQEGKIIELEQKctgILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 534
Cdd:COG1196 423 LEEL--EEALAELEEEEEEEEEA---LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 535 RHNNNMMAKTLE-ECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLL---------EL 604
Cdd:COG1196 498 EAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkaakagratFL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 605 SCNELRQELLKANGEIKHVSSLLA------KVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMK 678
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 679 ETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEA 758
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462558749 759 QQELRTVKRKLLEEEEKN-----------ARLQK------ELGDV 786
Cdd:COG1196 738 LEELLEEEELLEEEALEElpeppdleeleRELERlereieALGPV 782
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
448-787 |
4.44e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 448 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 526
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 527 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 605
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 606 C---NELRQELLKANGEIKHVSSLLAKvrRDSSLLVEKDYSYLKEIcdhqaeqlsrtsLKLQEkasesdaEIKDMKETIF 682
Cdd:COG5022 913 KslsSDLIENLEFKTELIARLKKLLNN--IDLEEGPSIEYVKLPEL------------NKLHE-------VESKLKETSE 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 683 ELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQEL 762
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILK 1046
|
330 340
....*....|....*....|....*
gi 2462558749 763 RTVKRKLLEEEEKNaRLQKELGDVQ 787
Cdd:COG5022 1047 PLQKLKGLLLLENN-QLQARYKALK 1070
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
608-798 |
5.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 608 ELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysylkeicdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQ 687
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER-----------------REALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 688 VEQHRAvklhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 767
Cdd:COG4913 677 LERLDA----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190
....*....|....*....|....*....|.
gi 2462558749 768 KLLEEEEKNARLQKELGDVQGHGRVVTSRAA 798
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLN 783
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
353-605 |
8.08e-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: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 353 STSNPFKSSKCSTAGSSPNSVSEL--SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAeNEKLVDEKTIL 430
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRIRLL 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 431 ETSFHQHRERAEQLSQENEKLMNLLQErVKNEEpTTQEGKIIELEQKctgILEQGRFEREKLLNIQqqltcsLRKVEEEN 510
Cdd:pfam10174 564 EQEVARYKEESGKAQAEVERLLGILRE-VENEK-NDKDKKIAELESL---TLRQMKEQNKKVANIK------HGQQEMKK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 511 QGALEMIKRLKEENEKlneflelerhNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAV---------EQ 581
Cdd:pfam10174 633 KGAQLLEEARRREDNL----------ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHltnlraerrKQ 702
|
250 260
....*....|....*....|....*....
gi 2462558749 582 TAESCEV-QEMLKVARAEKD----LLELS 605
Cdd:pfam10174 703 LEEILEMkQEALLAAISEKDaniaLLELS 731
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
384-717 |
1.15e-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: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 384 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDektiletsfhQHRERAEQLSQENEKLMNLlqeRVKNEE 463
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE----------RLDLLKAKASEAEQLRQNL---EKQQSS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 464 PTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTcSLRKVEEEnqgalemIKRLKEENEKLNEFLE----LERHNNN 539
Cdd:pfam05557 165 LAEAEQRIKELEFE----IQSQEQDSEIVKNSKSELA-RIPELEKE-------LERLREHNKHLNENIEnkllLKEEVED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 540 MMAK--TLEECRVTLEGLKMENGSLKSHLQGEKQKATE-----------ASAVEQ--------TAESCEVQEMLKVARAE 598
Cdd:pfam05557 233 LKRKleREEKYREEAATLELEKEKLEQELQSWVKLAQDtglnlrspedlSRRIEQlqqreivlKEENSSLTSSARQLEKA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 599 KDLLELSCNELRQELLKANGEIKHVSSLLAKVRRdSSLLVEKDYSYLKEICDHQAEQL--SRTSLKLQEKASESDAEIKD 676
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-RVLLLTKERDGYRAILESYDKELtmSNYSPQLLERIEEAEDMTQK 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462558749 677 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKS 717
Cdd:pfam05557 392 MQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQES 432
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1000-1062 |
1.41e-03 |
|
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: 39.29 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558749 1000 ITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAESV-GIKPSL-----------ELSEMLY 1062
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIPMVLspedlssphldELSGMTY 96
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
381-548 |
1.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.39 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 381 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 460
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 461 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 538
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 2462558749 539 NMMAKTLEEC 548
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
542-782 |
1.73e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 542 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 621
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 622 HVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 701
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 702 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 780
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 2462558749 781 KE 782
Cdd:COG4913 841 NE 842
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
699-782 |
2.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 699 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 774
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 2462558749 775 KNARLQKE 782
Cdd:PRK00409 599 GGYASVKA 606
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
587-794 |
2.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 587 EVQEMLKVARAEKDllelSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysylkeicdHQAEQLSRTSLKLQEK 666
Cdd:COG4717 75 ELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL----------LQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 667 ASESDAEIKDMKETIFELEDQVEQhravklhnnqlISELESSVIKLEEQKSDLERQLKTLT----KQMKEETEEWRRFQA 742
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLA 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462558749 743 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNaRLQKELGDVQGHGRVVT 794
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLA 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
375-747 |
2.68e-03 |
|
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: 42.13 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqMVQELTAENEKLVDEKTILETSFHQHR----ERAEQLSQENEK 450
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE--LNGELSAADAAVAKDRSELEALEDQHGafldADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 451 L------MNLLQERVK---------NEEPTTQEGKIIE-LEQKCTGI---LEQGRFEREKLL----NIQQQLTCSLRKVE 507
Cdd:pfam12128 349 LpswqseLENLEERLKaltgkhqdvTAKYNRRRSKIKEqNNRDIAGIkdkLAKIREARDRQLavaeDDLQALESELREQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 508 EE-----NQGALEMIKRLKEENEKLN------EFLELERHNN---NMMAKTLEECRVTLEGLKMENGSLKSHL--QGEKQ 571
Cdd:pfam12128 429 EAgklefNEEEYRLKSRLGELKLRLNqatatpELLLQLENFDeriERAREEQEAANAEVERLQSELRQARKRRdqASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 572 KATEASAVEQTAESCEVQEML-----------------------KVARAE----------------KDLLELSCNELRQE 612
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLfpqagtllhflrkeapdweqsigKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 613 LLKANGEIKHVSSLlaKVRRDSsllVEKDYSYLKEICDHQAEQLSRTSLKLQE-KASESDAE--IKDMKETIFELEDQve 689
Cdd:pfam12128 589 RIDVPEWAASEEEL--RERLDK---AEEALQSAREKQAAAEEQLVQANGELEKaSREETFARtaLKNARLDLRRLFDE-- 661
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558749 690 qHRAVKLHNNQLISELESSViklEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTA 747
Cdd:pfam12128 662 -KQSEKDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
587-733 |
2.84e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 587 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRD-SSLLVEKDY-SYLKEIcDHQAEQLSrtslKLQ 664
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYeALQKEI-ESLKRRIS----DLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558749 665 EKASESDAEIKDMKETIFELEDQVEQHRAvklHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEE 733
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
375-752 |
3.02e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 375 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTILETS-FHQHRERAEQLSQENEKLMN 453
Cdd:COG5185 214 NLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDLRLEkLGENAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 454 LLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE---KLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 530
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 531 LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAteASAVEQTaescevqemLKVARAEKDLLELSCNELR 610
Cdd:COG5185 370 VELSK-----SSEELDSFKDTIESTKESLDEIPQNQRGYAQEI--LATLEDT---------LKAADRQIEELQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 611 QELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSylkeicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQ 690
Cdd:COG5185 434 SSNEEVSKLLNELISELNKVMREADEESQSRLE----------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558749 691 HRAvklhnnqliselessvikleeqksDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVAN 752
Cdd:COG5185 504 LRA------------------------KLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
587-745 |
3.21e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 587 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEI-----------CDHQAEQ 655
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 656 LSRTSLKLQEKASESDAEIKDMKETIFELEDQV----EQHRAVKLHNNQlISELESSVIKLEEQKSDLERQLKTLTKQMK 731
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefnEQSKKLLELKNK-ISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
170
....*....|....
gi 2462558749 732 EETEEWRRFQADLQ 745
Cdd:PHA02562 376 DNAEELAKLQDELD 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
381-558 |
3.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 381 LTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRE---RAEQLSQENEKLMNLLQE 457
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 458 RVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 537
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
170 180
....*....|....*....|.
gi 2462558749 538 NNMMAKTLEECRVTLEGLKME 558
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKE 1776
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
374-654 |
3.84e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 374 SELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL 451
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 452 MNLLQErvknEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslrkvEEENQGALEMIKRLKEENEKLNEFL 531
Cdd:pfam02463 815 ELLEEE----QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER-------LEEEITKEELLQELLLKEEELEEQK 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 532 ELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKA----TEASAVEQTAESCEVQEMLKVARAEKDLLELSCN 607
Cdd:pfam02463 884 LKDE-------LESKEEKEKEEKKELEEESQKLNLLEEKENEieerIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462558749 608 ELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAE 654
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
482-743 |
3.98e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 482 LEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLN-EFLELERHNNNMMAKTLEE-CRVTLEGLKMEN 559
Cdd:pfam15905 85 LVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEkQLLELTRVNELLKAKFSEDgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 560 GSLKSHLQGeKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQEllkANGEIKHVSSLLAKVRRDSSLL-- 637
Cdd:pfam15905 162 MKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKE---KIEEKSETEKLLEYITELSCVSeq 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 638 VEK---DYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravklhnnqliSELESSVIKLEE 714
Cdd:pfam15905 238 VEKyklDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE-----------------SEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 2462558749 715 QKSDLERQLKTLTKQMKEETEEWRRFQAD 743
Cdd:pfam15905 301 KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
394-559 |
3.98e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 394 STAEELQATLQELSDQQQMVQELTaenEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQErvkneepttQEGKIIE 473
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAAQSQKKI---DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVAS---------QEQEIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 474 LEQKCTGIleqgrfERekllnIQQQLTCSLrkveeenqgaLEMIKRLKEENEKLNEFLELERHN-----NNMMA----KT 544
Cdd:pfam11932 81 LERQIEEI------ER-----TERELVPLM----------LKMLDRLEQFVALDLPFLLEERQArlarlRELMDdadvSL 139
|
170
....*....|....*
gi 2462558749 545 LEECRVTLEGLKMEN 559
Cdd:pfam11932 140 AEKYRRILEAYQVEA 154
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
380-529 |
4.16e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.39 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 380 SLTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRER------AEQLSQENEKL 451
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQ-LDALQEKLRGLEEENLKLRSEASHLktETDTYEEKEQqlmsdcVEQLSEANQQM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 452 MNLLQERVK--------NEEPTTQEGKIIELEQKCTGILEqgrfEREKLL-------NIQQQLTCSLRKVEEENQGALEM 516
Cdd:pfam04849 220 AELSEELARkmeenlrqQEEITSLLAQIVDLQHKCKELGI----ENEELQqhlqaskEAQRQLTSELQELQDRYAECLGM 295
|
170
....*....|...
gi 2462558749 517 IKRLKEENEKLNE 529
Cdd:pfam04849 296 LHEAQEELKELRK 308
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
378-641 |
4.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL---MNL 454
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERVKNEEPTTQEGKIIELEQKCTGILEQ--GRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLE 532
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 533 LERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQE 612
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
250 260
....*....|....*....|....*....
gi 2462558749 613 LLKANGEIKHVSSLLAKVRRDSSLLVEKD 641
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
663-787 |
4.52e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.64 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 663 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 742
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462558749 743 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 787
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-736 |
4.91e-03 |
|
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: 41.19 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 383 EKIQKMEENHHSTAEELQatlQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE-RVKN 461
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 462 EEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQqqltcSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHnnnMM 541
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ-----LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE---IL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 542 AKTLEECRVTLEGLKMENGSLKSHLQGE----KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQ-ELLKA 616
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDqelrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEmEQLNH 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 617 NGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSlKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKL 696
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462558749 697 HNNQLISELESSVIKLEEQ------KSDLERQLKTLTKQMKEETEE 736
Cdd:TIGR00606 609 HINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQ 654
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
378-742 |
6.62e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 378 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM---NL 454
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 455 LQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSL-----RKVEEENQGALEMIKRLKEENEKLNE 529
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 530 FLELERHNNNMMAKTLEECRVTLEG-------------------------------LKMENGSLKSHLQGEKQKA----- 573
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvlgdtllgrtlvaarLEAALRRAVTLAGRLREVTlegeg 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 574 -------TEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLK 646
Cdd:COG1196 656 gsaggslTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 647 EICDHQAEQLSRTSLKLQEKAsESDAEIKDMKETIFELEDQVEQHRAVklhnNQL-ISELESsvIK-----LEEQKSDLE 720
Cdd:COG1196 736 ELLEELLEEEELLEEEALEEL-PEPPDLEELERELERLEREIEALGPV----NLLaIEEYEE--LEerydfLSEQREDLE 808
|
410 420
....*....|....*....|....*
gi 2462558749 721 RQLKTL---TKQMKEETEEwrRFQA 742
Cdd:COG1196 809 EARETLeeaIEEIDRETRE--RFLE 831
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
561-732 |
7.77e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 39.74 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 561 SLKSHLQGEKQKAT--------------EASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHV-SS 625
Cdd:pfam09787 4 SAKQELADYKQKAArilqskekliaslkEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 626 LLAKVR----------------RDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIfeledqve 689
Cdd:pfam09787 84 QQEEAEssreqlqeleeqlateRSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQL-------- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558749 690 qhrAVKLHNNQLISELESSVIKLEE--------------QKSDLERQLKTLTKQMKE 732
Cdd:pfam09787 156 ---TSKSQSSSSQSELENRLHQLTEtliqkqtmlealstEKNSLVLQLERMEQQIKE 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
656-746 |
9.02e-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: 39.75 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558749 656 LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 735
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|.
gi 2462558749 736 EWRRFQADLQT 746
Cdd:COG4942 91 EIAELRAELEA 101
|
|
| |
