|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
883-994 |
9.98e-81 |
|
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: 257.27 E-value: 9.98e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 883 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGI 962
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462558767 963 KPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
883-994 |
3.21e-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: 3.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 883 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGI 962
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 2462558767 963 KPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
877-995 |
5.95e-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: 5.95e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 877 KDPLAALAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEA 956
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462558767 957 AESVGIKPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET 995
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
890-993 |
5.29e-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: 5.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEL 968
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
892-993 |
7.58e-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: 7.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 892 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSE 970
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 2462558767 971 MLY-TDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21200 83 MVRmGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
895-993 |
6.01e-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: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 895 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELSEMLYT 974
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 2462558767 975 DRPDWQSVMQYVAQIYKYF 993
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
890-993 |
1.62e-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: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIkPSLEL 968
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGI-AKLLD 80
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
893-993 |
1.70e-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: 115.85 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 893 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEM 971
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 2462558767 972 LYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
886-993 |
8.24e-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: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 886 EYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAESVGIKP 964
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 2462558767 965 SLELSEMLYTDRPDWQSVMQYVAQIYKYF 993
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 ... |
890-993 |
1.20e-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: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 968
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
890-991 |
1.60e-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: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPS-LEL 968
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQlLDV 80
|
90 100
....*....|....*....|...
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYK 991
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
890-993 |
8.77e-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: 8.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 968
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
892-991 |
4.64e-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: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 892 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVG-IKPSLELSE 970
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 2462558767 971 MLYTDRPDWQSVMQYVAQIYK 991
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
890-993 |
5.48e-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: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 968
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 2462558767 969 SEMLYT-DRPDWQSVMQYVAQIYKYF 993
Cdd:cd21258 81 EDMMIMgKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
895-993 |
4.32e-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: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 895 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELSEMLYT 974
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 2462558767 975 DRPDWQSVMQYVAQIYKYF 993
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
894-994 |
4.54e-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: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 894 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEML 972
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 2462558767 973 YTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
890-994 |
9.44e-27 |
|
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: 9.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELS 969
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
890-993 |
1.22e-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: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 968
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLD- 82
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
890-993 |
9.39e-26 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 102.35 E-value: 9.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESV-GIKPSLEL 968
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 2462558767 969 SEMLYTDR-PDWQSVMQYVAQIYKYF 993
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
891-993 |
1.01e-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: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 891 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLELS 969
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
890-993 |
4.35e-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: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 968
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21189 80 PEDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
889-994 |
6.04e-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: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 889 GSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLE 967
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 2462558767 968 LSEMLyTDRPDWQSVMQYVAQIYKYFE 994
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), ... |
888-994 |
1.00e-23 |
|
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: 96.65 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 888 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSL 966
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 2462558767 967 ELSEMLYTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
890-994 |
1.54e-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: 96.17 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEL 968
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYFE 994
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
892-993 |
1.23e-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: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 892 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSE 970
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 2462558767 971 MLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
891-993 |
2.36e-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: 93.02 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 891 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLELS 969
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
892-995 |
2.37e-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: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 892 RNALLKWCQKKTQGY-ANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKR--NLLLAFEAAE-SVGIKPSLE 967
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83
|
90 100
....*....|....*....|....*...
gi 2462558767 968 LSEMLYTdrPDWQSVMQYVAQIYKYFET 995
Cdd:pfam00307 84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
890-993 |
1.11e-21 |
|
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: 91.27 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 968
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
890-993 |
1.77e-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: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLElS 969
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82
|
90 100
....*....|....*....|....
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
895-991 |
2.80e-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: 89.41 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 895 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-ESVGIKPSLElSEMLY 973
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 2462558767 974 TDRPDWQSVMQYVAQIYK 991
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
890-993 |
5.28e-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: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 968
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
888-993 |
3.63e-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: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 888 GGSKRnALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIkPSL 966
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI-PRL 81
|
90 100
....*....|....*....|....*..
gi 2462558767 967 ELSEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
890-993 |
3.78e-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: 86.69 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 968
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
890-993 |
4.03e-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: 4.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEl 968
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
890-993 |
9.97e-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: 85.90 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 968
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
890-993 |
1.56e-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: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 968
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
890-993 |
1.62e-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: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLEL 968
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
893-989 |
4.10e-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: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 893 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY----QELNSQEKKRNLLLAFEAAESVGIKPSLEL 968
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQI 989
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
894-993 |
3.66e-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: 80.59 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 894 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLELSEmL 972
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 2462558767 973 YTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
890-993 |
5.84e-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: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLElS 969
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
890-995 |
1.10e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 84.61 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYAN-IDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQ--EKKRNLLLAFEAAE-SVGIKPS 965
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 2462558767 966 LELSEMLYTDRPDWQSVMQYVAQIYKYFET 995
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
892-991 |
1.58e-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: 75.84 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 892 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY---QELNSQEKKRNLLLAFEAAESVGIkPSLEL 968
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGL-PELDL 79
|
90 100
....*....|....*....|....*
gi 2462558767 969 --SEMLYtDRPDWQSVMQYVAQIYK 991
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 ... |
890-993 |
1.50e-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: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAESVGIKPSLELS 969
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
|
90 100
....*....|....*....|....
gi 2462558767 970 EMLYTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21244 85 EDVDVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
894-993 |
2.76e-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: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 894 ALLKWCQKKTQGYAnIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-ESVGIKPSLElSEML 972
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 2462558767 973 YTDRPDWQSVMQYVAQIYKYF 993
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
890-988 |
6.32e-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: 71.50 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYAnidITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 967
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|.
gi 2462558767 968 LSEMLYTDrPDWQSVMQYVAQ 988
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLSY 97
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
888-994 |
6.08e-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: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 888 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSL 966
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90 100
....*....|....*....|....*...
gi 2462558767 967 ELSEMLYTDRPdwQSVMQYVAQIYKYFE 994
Cdd:cd21196 81 SAQAVVAGSDP--LGLIAYLSHFHSAFK 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-653 |
2.54e-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: 74.71 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENhhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 368
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 369 RvkNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 448
Cdd:TIGR02168 752 L--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 449 NNMMAKTLEECRVTLEGLKMENGSLK--------SHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNE 519
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSedieslaaEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 520 LRQELLKANGEIKHVSSLLAKVRRD-SSLLVEkdysyLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 598
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRlEGLEVR-----IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558767 599 VEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 653
Cdd:TIGR02168 981 IKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
893-988 |
2.84e-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: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 893 NALLKWCQKKTQgyaNIDITNFSSSWSDGLAFCALLHTyLPAHIP-YQELNSQEKKRNLLLAFEAAESVGIKPSLELSEM 971
Cdd:cd21185 4 KATLRWVRQLLP---DVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 2462558767 972 lyTDrPDWQS--VMQYVAQ 988
Cdd:cd21185 80 --AD-PEVEHlgIMAYAAQ 95
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
895-991 |
3.87e-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: 66.49 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 895 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKK-RNLLLAFEAAE-SVGIKPSLElSEML 972
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 2462558767 973 YTDRPDWQSVMQYVAQIYK 991
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
890-990 |
3.44e-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: 60.80 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAE-SVGIKPSLEl 968
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 2462558767 969 SEMLYTDRPDWQSVMQYVAQIY 990
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
893-987 |
4.17e-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: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 893 NALLKWCQKKTQGYaNIDITNFSSSWSDGLAFCALLHTYLPAHIP----------------------------------- 937
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2462558767 938 -YQELNSQEkKRNLLLAFEAAESVG-IKPSLELSEMLYTdRPDWQSVMQYVA 987
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELGgVPALLRASDMSNT-IPDEKVVILFLS 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
390-694 |
5.55e-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: 67.00 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 390 TGILEQGRfEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRvtlegLKME 469
Cdd:TIGR02168 670 SSILERRR-EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE-----AEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 470 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLV 549
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 550 EKDYSYLKEI--CDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQK 627
Cdd:TIGR02168 824 ERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558767 628 SDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 694
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
895-991 |
6.88e-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: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 895 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAES-VGIKPSLElSEMLY 973
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 2462558767 974 TDRPDWQSVMQYVAQIYK 991
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
286-699 |
1.37e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 355
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 356 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 432
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 433 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 503
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 504 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYsyLKEICDH 562
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERRED--LEELIAE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 563 QAEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSD 629
Cdd:PRK02224 528 RRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 630 LER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 698
Cdd:PRK02224 608 IERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
.
gi 2462558767 699 G 699
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 ... |
285-700 |
4.64e-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: 64.04 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 285 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 362
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 363 -MNLLQERVKNEEPTTQ---------EGKIIELEqkctgileqgrfEREKLLNIQQQLTCSLRKVEEENQGalEMIKRLK 432
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLE------------EDILLLEDQNSKLSKERKLLEERIS--EFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 433 EENEKLNEFLELeRHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAvEQTAESCEVQEMLkvARAEKDL 512
Cdd:pfam01576 170 EEEEKAKSLSKL-KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQL--AKKEEEL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 513 ------LELSCNElRQELLKANGEIK-HVSSLL-------------AKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSL 572
Cdd:pfam01576 246 qaalarLEEETAQ-KNNALKKIRELEaQISELQedleseraarnkaEKQRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 573 KLQE-----KASES-----DAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLT 638
Cdd:pfam01576 325 REQEvtelkKALEEetrshEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558767 639 kQMKEETEEWRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRKLLEEEEKNARLQKELGDVQGH 700
Cdd:pfam01576 398 -QAKQDSEHKRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-692 |
6.48e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 295 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 374
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 375 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKRLK-----------EENEK--LNEF 441
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKAKgkcpvcgreltEEHRKelLEEY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 442 -LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnEL 520
Cdd:PRK03918 458 tAELKR-----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 521 RQELLKANGEIKHVSSLLAKVRrdsslLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE---- 596
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLE-----ELKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyn 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 597 ------DQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLT-----------KQMKEETEEWRRFQADLQTAV 659
Cdd:PRK03918 603 eylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAEL 682
|
410 420 430
....*....|....*....|....*....|...
gi 2462558767 660 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQK 692
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-543 |
6.61e-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: 63.54 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 361
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 362 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 436
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 437 KLNEflELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 516
Cdd:TIGR02168 397 SLNN--EIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260
....*....|....*....|....*..
gi 2462558767 517 CNELRQELLKANGEIKHVSSLLAKVRR 543
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLER 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-693 |
1.87e-09 |
|
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: 61.57 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 283 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 361
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 362 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 441
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 442 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 507
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 508 AEKDLLELSCNELRQELLKANGEIKhvssllakvrrdsSLLVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEI 585
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIE-------------KLKKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 586 KDMKETIFELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTA 658
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
|
410 420 430
....*....|....*....|....*....|....*
gi 2462558767 659 VvvandikceaqQELRTVKRKLLEEEEKNARLQKE 693
Cdd:TIGR04523 495 E-----------KELKKLNEEKKELEEKVKDLTKK 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-694 |
2.31e-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: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 428 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 507
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 508 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEkdysylkeicdhQAEQLSRTSLKLQEKASESDAEIKD 587
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE------------RRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 588 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKc 667
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL- 413
|
250 260
....*....|....*....|....*..
gi 2462558767 668 EAQQELRTVKRKLLEEEEKNARLQKEL 694
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEE 440
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-554 |
4.01e-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: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 446 RhnnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscnELRQELL 525
Cdd:COG1196 407 E--------AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL---LEEAALL 475
|
250 260
....*....|....*....|....*....
gi 2462558767 526 KANGEIKHVSSLLAKVRRDSSLLVEKDYS 554
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
289-694 |
6.14e-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: 60.37 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 361
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 362 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 428
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 429 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 508
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 509 EKDLLELSCNELRQELLKANGEIK-----------HVSSLLAKVRRDSSLLVEKDYSYLKEIcdHQAEQLSRTSLKLQEK 577
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQElqqryaelcaaAITCTAQCEKLEKIHLQESAQSLKERE--QQLQTKEQIHLQETRK 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 578 ASESDAEIKDMKETIFELEDQvEQHRAVKLH-------NNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRR 650
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGS-CIHPNPARQdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2462558767 651 FQADLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 694
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
293-695 |
1.73e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 293 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 369
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 370 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 437
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 438 LNEFLELERHNNNMMAKtLEECRVTLEGLKmengSLKSHLQGEKQKATEASaVEqtaescEVQEMLKVARAEKDLLELSC 517
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRLTGLT-PE------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 518 NELRQELLKANGEIKHVSSLLAKVRRdssllvekdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELED 597
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK------------AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 598 QVEQHRAVKLHNNQLISElESSVIKLE---EQKSDLERQLKTLT-KQMKEETEEWRRFQADLQT----AVVVANDIK--C 667
Cdd:PRK03918 474 KERKLRKELRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklE 552
|
410 420
....*....|....*....|....*...
gi 2462558767 668 EAQQELRTVKRKLLEEEEKNARLQKELG 695
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELE 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-704 |
2.14e-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: 58.53 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 414 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMM---AKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 490
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELeelTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 491 EQtaESCEVQEMLKVARAEkdllelscnELRQELLKANGEIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAEQLSRT 570
Cdd:TIGR02168 296 EI--SRLEQQKQILRERLA---------NLERQLEELEAQLEELESKLDELAEELAEL-EEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 571 SLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ------- 640
Cdd:TIGR02168 364 EAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaele 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558767 641 -MKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 704
Cdd:TIGR02168 444 eLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
270-693 |
2.40e-08 |
|
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: 58.19 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 270 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELT-----------------AENE 332
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 333 KLVDEKTiletsfhQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQ 409
Cdd:pfam05483 419 KLLDEKK-------QFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 410 LTCSLRKVEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEA 487
Cdd:pfam05483 492 AHCDKLLLENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEV 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 488 SAVEQTAESCEVQEMLKVARAEKDL--LELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYlkEICDHQAE 565
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY--EIKVNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 566 -QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQMKE 643
Cdd:pfam05483 643 lELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2462558767 644 ETEEWRRFQADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 693
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
890-988 |
3.79e-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: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTQGyanIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 967
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|.
gi 2462558767 968 LSEMLYTDrPDWQSVMQYVAQ 988
Cdd:cd21230 78 PEEIINPN-VDEMSVMTYLSQ 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-691 |
5.35e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHhstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKLMNL--- 365
Cdd:COG4717 73 LKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELper 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 ---LQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEK 437
Cdd:COG4717 148 leeLEERLEElreleEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 438 LNEflELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEAS 488
Cdd:COG4717 225 LEE--ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 489 AVEQTAESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvekdysYLKEICDHQAEQL 567
Cdd:COG4717 303 EAEELQALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------QLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 568 SR---TSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEE 644
Cdd:COG4717 377 AEagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEEL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462558767 645 TEEWRRFQADLQTAVvvANDIKCEAQQELRTVKRKLLEEEEKNARLQ 691
Cdd:COG4717 452 REELAELEAELEQLE--EDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
319-736 |
1.37e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.51 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 319 DQQQMVQELTAE-NEKLVDEKTILETSFH--QHRERAEQlSQENEKLMNLLQERVKNEepttQEGKIIELEQKCTgiLEQ 395
Cdd:pfam17380 248 DVTTMTPEYTVRyNGQTMTENEFLNQLLHivQHQKAVSE-RQQQEKFEKMEQERLRQE----KEEKAREVERRRK--LEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 396 GRFEREKLLNIQQQLTCSLRKVEEENQGALEmikRLKEENEKLneflELERHNNNMMAKTLEECRvTLEGLKMENGSLKS 475
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQERMAMERERELE---RIRQEERKR----ELERIRQEEIAMEISRMR-ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 476 HLQGEKQKATEASAVEQtaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKhvSSLLAKVRRDssllvEKDYSY 555
Cdd:pfam17380 393 RVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER--AREMERVRLE-----EQERQQ 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 556 LKEICDHQAEQLSRTSLKLqEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELE----SSVIKLEEQKSDLE 631
Cdd:pfam17380 461 QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerQKAIYEEERRREAE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 632 RQLKTltkqmKEETEEWRRFQAdlQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARL------------------QKE 693
Cdd:pfam17380 540 EERRK-----QQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQIVESEKARAEYeattpittikpiyrprisEYQ 612
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2462558767 694 LGDVQGHGRVVTSR----AAPPPVDEEPESSEVDAAGRWPGVCVSRT 736
Cdd:pfam17380 613 PPDVESHMIRFTTQspewATPSPATWNPEWNTVTAEEETPGIPIIHS 659
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
307-700 |
2.03e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 307 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhreRAEQLSQENEKLMNLLQErvkneEPTTQEGKIIELE 386
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL--------QETRKKAVVLARLLELQE-----EPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 387 QKCTGILEQGRFER--EKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKL-NEFLELERHNN------NMMAKTLE 457
Cdd:TIGR00618 515 PARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNrskediPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 458 ECRVTLEGLKMENGSLKSHLQGEKQKATEASA---VEQTAESCEVQEMLKVARAEKDLLELSCNELR--------QELLK 526
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdVRLHLQQCSQELALKLTALHALQLTLTQERVRehalsirvLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 527 ANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASES-DAEIKDMKETIFELEDQVEQHRAV 605
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSlGSDLAAREDALNQSLKELMHQART 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 606 KLHNNQLI----SELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLL 681
Cdd:TIGR00618 755 VLKARTEAhfnnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFL 834
|
410
....*....|....*....
gi 2462558767 682 EEEEKNARLQKELGDVQGH 700
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLK 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-727 |
2.29e-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: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 402 LEELEEAEE--ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 446 RHNNNMMAK------TLEECRVTLEGLkmENGSLKSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNE 519
Cdd:COG1196 480 AELLEELAEaaarllLLLEAEADYEGF--LEGVKAALLLAGLRGLAGAVAVLIGVE--AAYEAALEAALAAALQNIVVED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 520 LRQ-----ELLKANGE----------IKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAE 584
Cdd:COG1196 556 DEVaaaaiEYLKAAKAgratflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 585 IKDMKETIFELEDQVEQHRAVklhnNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVAND 664
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGG----SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558767 665 IKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGR 727
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-728 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 350 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 426
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 427 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 506
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 507 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRdssllvekdysylkeicdhQAEQLSRTSLKLQEKASESDAEIK 586
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-------------------ELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 587 DMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandik 666
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-------- 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558767 667 cEAQQELRTVKRKLLEEEEKNARLQ----KELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRW 728
Cdd:COG1196 483 -LEELAEAAARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
275-693 |
3.02e-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: 54.69 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 275 STAGSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAE 353
Cdd:TIGR02169 661 APRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 354 QLSqenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRL 431
Cdd:TIGR02169 741 ELE---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 432 KEENEKLNEflelerhnnnmmaktleecrvtleglkmengslkshLQGEKQKATEASAVEQtAESCEVQEMLKVARAEKD 511
Cdd:TIGR02169 815 REIEQKLNR------------------------------------LTLEKEYLEKEIQELQ-EQRIDLKEQIKSIEKEIE 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 512 LLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSllvekdysylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKET 591
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERD--------------------------ELEAQLRELERKIEELEAQ 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 592 IFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQkSDLERQLKTLTKQMKEETEEWRRFQadlqtavvvanDIKCEAQQ 671
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQ 979
|
410 420
....*....|....*....|..
gi 2462558767 672 ELRTVKRKLLEEEEKNARLQKE 693
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-610 |
4.84e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 446 RHNnnmmAKTLEECRVTLEGL-KMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDL-LELSCNELRQE 523
Cdd:COG1196 389 LEA----LRAAAELAAQLEELeEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAeLEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 524 LLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHR 603
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
....*..
gi 2462558767 604 AVKLHNN 610
Cdd:COG1196 545 AAALQNI 551
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
307-723 |
6.78e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 6.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 307 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 386
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 387 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 466
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 467 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVRRD 544
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 545 SSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAE--IKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIK 622
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA 1690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 623 LEEQKSDLE--RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN--ARLQKELGDVQ 698
Cdd:PTZ00121 1691 AEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEEKKA 1770
|
410 420
....*....|....*....|....*
gi 2462558767 699 GHGRVVTSRAAPPPVDEEPESSEVD 723
Cdd:PTZ00121 1771 EEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
498-707 |
8.76e-07 |
|
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: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 498 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKVRrdsSLLVEKDYSYLKEICDHQAEQLSRtslkLQEK 577
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALR---LWFAQRRLELLEAELEELRAELAR----LEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 578 ASESDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 656
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462558767 657 TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 707
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
308-703 |
9.48e-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: 53.15 E-value: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 308 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNL--LQERVKNEEPTTQEGKIIEL 385
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 386 EQKctgiLEQGRFEREKLLNIQQQLTcslRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEG 465
Cdd:TIGR02169 236 ERQ----KEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 466 LKMENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRR 543
Cdd:TIGR02169 306 LERSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 544 DSSLLVEKDYSYLKEICDHQAEQ--LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVklhnnqlISELESSVI 621
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 622 KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHG 701
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLG 531
|
..
gi 2462558767 702 RV 703
Cdd:TIGR02169 532 SV 533
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
498-811 |
1.15e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 498 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAEQLSRTSlklqek 577
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARALYRSG------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 578 ASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEwrrfQADLQT 657
Cdd:COG3883 100 GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 658 AVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRWPGVCVSRTS 737
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558767 738 PTPPESATTVKSLIKSFDLGRPGGAGQNISVHKTPRSPLSGIPVRTAPAAAVSPMQRHSTYSSVRPASRGVTQR 811
Cdd:COG3883 256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAG 329
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
428-694 |
1.68e-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: 52.37 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 428 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLqgEKQKATEASAVEQ----TAESCEVQEML 503
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREEL--EELQEELKEAEEEleelTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 504 KVARAEKDLLELSCNELRQELLKANGEIKHVSS--LLAKVRRDSSLLVEKDYSY----LKEICDHQAEQLSRTSLKLQEK 577
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQqkQILRERLANLERQLEELEAqleeLESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 578 ASESD---AEIKDMKETIFELEDQVEQHRA---------------VKLHNNQL------ISELESSVIKLEEQKSDLERQ 633
Cdd:TIGR02168 350 KEELEsleAELEELEAELEELESRLEELEEqletlrskvaqlelqIASLNNEIerlearLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558767 634 LKTLTKQ-MKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 694
Cdd:TIGR02168 430 LEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
895-967 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558767 895 LLKWCQK--KTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIP----YQELNSQEKKRNLLLAFEAAESVGIKPSLE 967
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLT 93
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-672 |
1.93e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHHSTAEELQATLQELS-DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLq 367
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 368 ERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVeeenqgALEMIKRLKEENEKLNEFLELERH 447
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL------ALLFLLLAREKASLGKEAEELQAL 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 448 NNNMMAKTLEECRVtLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD-LLELSCNELRQELLK 526
Cdd:COG4717 311 PALEELEEEELEEL-LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAaLLAEAGVEDEEELRA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 527 ANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravk 606
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE---------- 459
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558767 607 lhnnQLISELESSvikleEQKSDLERQLKTLTKQMKEETEEWRRfqadLQTAVVVANDIKCEAQQE 672
Cdd:COG4717 460 ----AELEQLEED-----GELAELLQELEELKAELRELAEEWAA----LKLALELLEEAREEYREE 512
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
289-698 |
2.64e-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: 51.59 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEEN-HHSTAEELQATLQELSDQQQMVQELTAENEklvdektilETSFHQHRERAEQLSQENEKLMNLLQ 367
Cdd:TIGR00606 593 LAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDE---------ESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 368 ERVKNEEPTTQEgkiielEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERH 447
Cdd:TIGR00606 664 VYSQFITQLTDE------NQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 448 NNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--------EVQEMLK---------VARAEK 510
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKdverkiaqqAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 511 DLLELSCNELRQELLKANGEIKHVSS---LLAKVRRDSSLLVEKDYSYLKEICDH---------QAEQLSRTSLKLQEKA 578
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSkieLNRKLIQDQQEQIQHLKSKTNELKSEklqigtnlqRRQQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 579 SESDAEIKDMKETIFELE-----DQVEQHRAV-KLHNNQLISELESSVIK--------------------LEEQKSDLER 632
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLEtflekDQQEKEELIsSKETSNKKAQDKVNDIKekvknihgymkdienkiqdgKDDYLKQKET 977
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558767 633 QLKTLTKQMKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRKLLEEEEKNARLQKELGDVQ 698
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
426-694 |
2.96e-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: 51.27 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 426 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 504
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 505 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVRRDSSllvekdysylKEIcdHQAEQLSRTSLK-----LQE 576
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG----------KKI--YEHDSMSTMHFRslgsaISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 577 KASESDAEIKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTL 637
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEII 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558767 638 TKQMKEETEEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 694
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
354-694 |
5.54e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 354 QLSQENEKLMNL---LQERVKNEEPTTQEG-KIIELEQKCtgiLEQGRFEREKL-LNIQQQLTCSlRKVEEENQGALEMI 428
Cdd:pfam05483 82 KLYKEAEKIKKWkvsIEAELKQKENKLQENrKIIEAQRKA---IQELQFENEKVsLKLEEEIQEN-KDLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 429 KRLKE----ENEKLNEFlELERH---------NNNM--MAKTLEECRVtleglKMENGSLKSHLQgEKQKATEASAVEQt 493
Cdd:pfam05483 158 NLLKEtcarSAEKTKKY-EYEREetrqvymdlNNNIekMILAFEELRV-----QAENARLEMHFK-LKEDHEKIQHLEE- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 494 aescEVQEMLKVARAEKDLLELSCNElrqellKANgEIKHVSSLLAKVRRDSSLLVEK------DYSYLKEICDHQAEQL 567
Cdd:pfam05483 230 ----EYKKEINDKEKQVSLLLIQITE------KEN-KMKDLTFLLEESRDKANQLEEKtklqdeNLKELIEKKDHLTKEL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 568 SRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ 640
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558767 641 MKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KRKLLEEEEKNARLQKEL 694
Cdd:pfam05483 379 LKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEKKQFEKIAEEL 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
453-666 |
7.74e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 453 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 530
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 531 IKHVSSLLAKVRR-----------------DSSLLVEKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 590
Cdd:COG4942 99 LEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558767 591 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 666
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
308-642 |
8.95e-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: 49.63 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 308 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 386
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 387 QKctgileqgrFEREKLLNiqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 459
Cdd:TIGR04523 398 SK---------IQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 460 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 537
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 538 LAKVRRDSSllvEKDYSYLKEICDHQaeqlsrtslklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELE 617
Cdd:TIGR04523 544 EDELNKDDF---ELKKENLEKEIDEK-----------NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE 609
|
330 340
....*....|....*....|....*
gi 2462558767 618 SSVIKLEEQKSDLERQLKTLTKQMK 642
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIK 634
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
394-700 |
1.36e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 394 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 469
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 470 NGSLKSHLQGEKQKATEASAVE-------------QTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSS 536
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVlkenkeeekekklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 537 LLAKVRRDSSLL--VEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKlhnNQLIS 614
Cdd:pfam02463 329 ELKKEKEEIEELekELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK---SEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 615 ELESSVIKLEEQKSDLERQLKTLTKQMKEETEEwrrfqadlQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKEL 694
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEES--------IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
....*.
gi 2462558767 695 GDVQGH 700
Cdd:pfam02463 478 QLVKLQ 483
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
315-681 |
3.08e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.91 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 315 QELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM-NLLQERvkneeptTQEGKIIELeqkctgiL 393
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRkSLLANR-------FSFGPALDE-------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 394 EqgrferEKLLNIQQQLTcslRKVEEENQG----ALEMIKRLKEENEKLNEFLE----LERHNNNMMAKTLEECRVTLEG 465
Cdd:PRK04778 171 E------KQLENLEEEFS---QFVELTESGdyveAREILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 466 LKMENGSLKsHLQGEKqkateasaveqtaescEVQEML-KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvrrd 544
Cdd:PRK04778 242 LVEEGYHLD-HLDIEK----------------EIQDLKeQIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL------ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 545 ssllvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQLISELESSVIKL 623
Cdd:PRK04778 299 -----EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-YTLnESELESVRQLEKQLESLEKQYDEITERI 371
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558767 624 EEQK---SDLERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDIKCEAQQELRTVKRKLL 681
Cdd:PRK04778 372 AEQEiaySELQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
888-988 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 888 GGSKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAESVGIKPSL 966
Cdd:cd21315 14 GPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDWLDVPQL 90
|
90 100
....*....|....*....|..
gi 2462558767 967 ELSEMLYTDRPDWQSVMQYVAQ 988
Cdd:cd21315 91 IKPEEMVNPKVDELSMMTYLSQ 112
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
414-723 |
4.23e-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: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 414 LRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQT 493
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARE--------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 494 AEscevqemLKVARAEKDLLELSCNELRQELLKANG--------EIKHVSSLLAKVRRDSSLLvEKDYSYLKEICDHQAE 565
Cdd:COG4913 309 AE-------LERLEARLDALREELDELEAQIRGNGGdrleqlerEIERLERELEERERRRARL-EALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 566 QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKlhnNQLISELESsvikLEEQKSDLERQLKTLTKQMKEET 645
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIAS----LERRKSNIPARLLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 646 EEWR---RFQADL----------QTAVVVAndikceaqqeLRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPP 712
Cdd:COG4913 454 GLDEaelPFVGELievrpeeerwRGAIERV----------LGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGL 523
|
330
....*....|.
gi 2462558767 713 VDEEPESSEVD 723
Cdd:COG4913 524 PDPERPRLDPD 534
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-697 |
5.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 399 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 478
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 479 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysy 555
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER---- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 556 LKEicdhqAEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSD 629
Cdd:PRK03918 330 IKE-----LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 630 LERQLKTLTkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN--ARLQKELGDV 697
Cdd:PRK03918 403 IEEEISKIT----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKEllEEYTAELKRI 464
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
291-643 |
5.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 291 SLTEKIQKMEENH---HSTAEELQATLQ----ELSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 359
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEeareAVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 360 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 427
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 428 -----IKRLKEENEKLNEFLElERHNnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAESCEVqem 502
Cdd:PRK02224 506 eaedrIERLEERREDLEELIA-ERRE------TIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAEEARE--- 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 503 lKVARAEKDLLELscNELRQELlkanGEIKHVSSLLAKVRRDSSLLVEKdYSYLKEICDHQAEQLSRTSLKLQEKASESD 582
Cdd:PRK02224 573 -EVAELNSKLAEL--KERIESL----ERIRTLLAAIADAEDEIERLREK-REALAELNDERRERLAEKRERKRELEAEFD 644
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558767 583 aeikdmketifelEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKE 643
Cdd:PRK02224 645 -------------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
290-688 |
5.58e-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: 47.35 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 290 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 369
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 370 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQgalemIKRLKEENEKLNEFLELERHNN 449
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-----VQQVNQEKQEKQHELDTVVSKI 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 450 NMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAE--SCEVQEMLKVARAEKDlLELSCNELRQELLKA 527
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVelSTEVQSLIREIKDAKE-QDSPLETFLEKDQQE 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 528 NGEIKHVSSLLAKVRRDSSLLVEKD-----------YSYLKEICDHQAEQ----LSRTSLKLQEKASESDAEIKDMKETI 592
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKvknihgymkdiENKIQDGKDDYLKQketeLNTVNAQLEECEKHQEKINEDMRLMR 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 593 FELEDQVEQHRAVKlhnNQLiselesSVIKLEEQKSDLERQLKTLTKQMK-----EETEEWRRFQADLQTavVVANDIKC 667
Cdd:TIGR00606 1005 QDIDTQKIQERWLQ---DNL------TLRKRENELKEVEEELKQHLKEMGqmqvlQMKQEHQKLEENIDL--IKRNHVLA 1073
|
410 420
....*....|....*....|....*.
gi 2462558767 668 EAQQ-----ELRTVKRKLLEEEEKNA 688
Cdd:TIGR00606 1074 LGRQkgyekEIKHFKKELREPQFRDA 1099
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
290-594 |
6.57e-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: 46.89 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 290 ASLTEKIQKMEENH-HSTAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKLmnLLQE 368
Cdd:TIGR00618 602 KLSEAEDMLACEQHaLLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPK--ELLA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 369 RVKNEEPTTQEgkiieLEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERH 447
Cdd:TIGR00618 677 SRQLALQKMQS-----EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 448 NNNMMAKTLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELl 525
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE- 830
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 526 kangeikhvSSLLAKVRRDSSLLVEKDYSYLK-EICDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 594
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 ... |
309-660 |
8.37e-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: 46.71 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 309 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIE-LE 386
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 387 QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE----NQGALEMIKRLKEENEKLNEFLELERHNNnmmaKTLEECRVT 462
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNK----ANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 463 LEGlkmENGSLKSHLQGEKQKATEASAVEQTAEScEVQE-MLKVARAEKDLlelscNELRQELLKANGEIKHVSSLLAKV 541
Cdd:pfam01576 382 LES---ENAELQAELRTLQQAKQDSEHKRKKLEG-QLQElQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 542 RRDSSLLvEKDYSYLKEICDHQAEQLS---RTSLKLQEKASESDAEIKDMKEtifELEDQVEQHRAVKLH----NNQL-- 612
Cdd:pfam01576 453 EGKNIKL-SKDVSSLESQLQDTQELLQeetRQKLNLSTRLRQLEDERNSLQE---QLEEEEEAKRNVERQlstlQAQLsd 528
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558767 613 ----ISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW-------RRFQADLQTAVV 660
Cdd:pfam01576 529 mkkkLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLV 587
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
890-991 |
8.47e-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: 42.77 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIKPSLE 967
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCPdWESWDPQKPVDNAREAMQQADDwLGVPQVIT 84
|
90 100
....*....|....*....|....
gi 2462558767 968 LSEMLYTDrPDWQSVMQYVAQIYK 991
Cdd:cd21313 85 PEEIIHPD-VDEHSVMTYLSQFPK 107
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
911-973 |
8.75e-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: 8.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558767 911 ITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE------KKRNLLLAFEAA-ESVGIKPS-LELSEMLY 973
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKEsmsladSLYNIQLLQEFCqRHLGNRCChLTLEDLLY 83
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-729 |
1.01e-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: 45.91 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 472 SLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLvEK 551
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 552 DYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE 631
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 632 RQ---LKTLTKQMKEEteewrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQghgrvvtsRA 708
Cdd:COG4942 171 AEraeLEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE--------AE 235
|
250 260
....*....|....*....|.
gi 2462558767 709 APPPVDEEPESSEVDAAGRWP 729
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
274-515 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 274 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 351
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 352 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 431
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 432 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 511
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 2462558767 512 LLEL 515
Cdd:COG4942 225 LEAL 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
289-699 |
1.66e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 362
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 363 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 413
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 414 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 446
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 447 -------------------------------HNNNMMAKTLEECR--------VTLEGLKMEngslKSHLQGEKQKATEA 487
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGELFE----KSGAMTGGSRAPRG 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 488 SAVEQTAESCEVQEMlkvaRAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLL------VEKDYSYLKEICD 561
Cdd:TIGR02169 665 GILFSRSEPAELQRL----RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIekeieqLEQEEEKLKERLE 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 562 HQAEQLSRTSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLT 638
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIE 818
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558767 639 KQMKEETEEWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 699
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
890-991 |
2.02e-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: 41.98 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 890 SKRNALLKWCQKKTqgyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAES-VGIkPSLE 967
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWESWDPNQPVQNAREAMQQADDwLGV-PQVI 86
|
90 100
....*....|....*....|....
gi 2462558767 968 LSEMLYTDRPDWQSVMQYVAQIYK 991
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPK 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
286-697 |
2.94e-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: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 365
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERvkNEEPTTQEGKIIELEQKctgILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 445
Cdd:COG1196 423 LEEL--EEALAELEEEEEEEEEA---LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 446 RHNNNMMAKTLE-ECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLL---------EL 515
Cdd:COG1196 498 EAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkaakagratFL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 516 SCNELRQELLKANGEIKHVSSLLA------KVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMK 589
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 590 ETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEA 669
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2462558767 670 QQELRTVKRKLLEEEEKN-----------ARLQK------ELGDV 697
Cdd:COG1196 738 LEELLEEEELLEEEALEElpeppdleeleRELERlereieALGPV 782
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
289-647 |
3.24e-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: 44.96 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEEnhhstaeELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 368
Cdd:TIGR00618 551 LTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 369 RVKNEEPTTQEGKIIELEQKctgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 448
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 449 NNMMAKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAVEQTAESCEVQEMLKVARAEKDllelscnelrqELLKAN 528
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQAR-----------TVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 529 GEIKHVSSLLAKVrrdsSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLH 608
Cdd:TIGR00618 760 TEAHFNNNEEVTA----ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFL 834
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462558767 609 NnqLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEE 647
Cdd:TIGR00618 835 S--RLEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQL 874
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
286-683 |
3.39e-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: 44.72 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 362
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 363 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 437
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 438 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLkvaRAEKDLlels 516
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERL---RAVKDI---- 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 517 cNELRQELLKangEIKhvssllaKVRRDSSLLVEkDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 596
Cdd:pfam15921 652 -KQERDQLLN---EVK-------TSRNELNSLSE-DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 597 DQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTV 676
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQ 798
|
....*..
gi 2462558767 677 KRKLLEE 683
Cdd:pfam15921 799 ERRLKEK 805
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-709 |
5.03e-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: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 519 ELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysylkeicdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQ 598
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER-----------------REALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 599 VEQHRAvklhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 678
Cdd:COG4913 677 LERLDA----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190
....*....|....*....|....*....|.
gi 2462558767 679 KLLEEEEKNARLQKELGDVQGHGRVVTSRAA 709
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLN 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
392-692 |
5.08e-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: 44.19 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 392 ILEQGRFEREKLLNIQQ--QLTCSLRKVEEENQGAL---EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTL--- 463
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEkkELLMNLFPLDQYTQLALmefAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLeke 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 464 -----EGLKMENGSLkSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNEL--RQELLKANGEIKHVSS 536
Cdd:TIGR00618 228 lkhlrEALQQTQQSH-AYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 537 LLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHRAVKLHNNQLISEL 616
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI------HIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 617 EsSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRF------QADLQTAVVVANDiKCEAQQELRTVKRKLLEEEEKNARL 690
Cdd:TIGR00618 379 Q-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsaFRDLQGQLAHAKK-QQELQQRYAELCAAAITCTAQCEKL 456
|
..
gi 2462558767 691 QK 692
Cdd:TIGR00618 457 EK 458
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
308-715 |
6.66e-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: 43.81 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 308 EELQATLQELSDQQQMVQELTAENEKLV----DEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEpttqegKII 383
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELklkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ------ELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 384 ELEQKctgileqgrfEREKLLNIQQQLTCSLRKVEEENqgalEMIKRLKEENEKLNEFLELERhnnnmmaKTLEECRVTL 463
Cdd:pfam02463 247 RDEQE----------EIESSKQEIEKEEEKLAQVLKEN----KEEEKEKKLQEEELKLLAKEE-------EELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 464 EGLKMENGSLKSHLQGEKQKateasaveqtAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRR 543
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKK----------AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 544 DSSLLVEKDYSYLKEICDHQAEQLsrtsLKLQEKASESDAEIKDMKETIFELEDQVEqhravKLHNNQLISELESSVIKL 623
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELEL----KSEEEKEAQLLLELARQLEDLLKEEKKEE-----LEILEEEEESIELKQGKL 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 624 EEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQ-QELRTVKRKLLEEEEKNARLQKELGDVQGHGR 702
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQkLEERSQKESKARSGLKVLLALIKDGVGGRIIS 526
|
410
....*....|...
gi 2462558767 703 VVTSRAAPPPVDE 715
Cdd:pfam02463 527 AHGRLGDLGVAVE 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
518-690 |
7.25e-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: 43.47 E-value: 7.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 518 NELRQELLKANGEIKhvssllakVRRDSSLLVEKDYSYLKEICDHQAEQLSRTS---LKLQEKASESDAEIKDMKETIFE 594
Cdd:TIGR04523 99 NKLNSDLSKINSEIK--------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLteiKKKEKELEKLNNKYNDLKKQKEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 595 LEDQVE---------QHRAVKLHNNQLISELESSVIKLEEQK--------SDLERQLKTLTKQMKEETEEWRRFQADLQT 657
Cdd:TIGR04523 171 LENELNllekeklniQKNIDKIKNKLLKLELLLSNLKKKIQKnkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISN 250
|
170 180 190
....*....|....*....|....*....|...
gi 2462558767 658 AVVVANDIKCEAQQELRTVKRKLLEEEEKNARL 690
Cdd:TIGR04523 251 TQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
359-698 |
7.30e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 359 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 437
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 438 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 516
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 517 C---NELRQELLKANGEIKHVSSLLAKvrRDSSLLVEKDYSYLKEIcdhqaeqlsrtsLKLQEkasesdaEIKDMKETIF 593
Cdd:COG5022 913 KslsSDLIENLEFKTELIARLKKLLNN--IDLEEGPSIEYVKLPEL------------NKLHE-------VESKLKETSE 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 594 ELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQEL 673
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILK 1046
|
330 340
....*....|....*....|....*
gi 2462558767 674 RTVKRKLLEEEEKNaRLQKELGDVQ 698
Cdd:COG5022 1047 PLQKLKGLLLLENN-QLQARYKALK 1070
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
453-693 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 453 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 532
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 533 HVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 612
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 613 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 691
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 2462558767 692 KE 693
Cdd:COG4913 841 NE 842
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
911-973 |
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 2462558767 911 ITNFSSSWSDGLAFCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAESV-GIKPSL-----------ELSEMLY 973
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIPMVLspedlssphldELSGMTY 96
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
264-516 |
1.53e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 264 STSNPFKSSKCSTAGSSPNSVSEL--SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAeNEKLVDEKTIL 341
Cdd:pfam10174 485 SALQPELTEKESSLIDLKEHASSLasSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRT-NPEINDRIRLL 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 342 ETSFHQHRERAEQLSQENEKLMNLLQErVKNEEpTTQEGKIIELEQKctgILEQGRFEREKLLNIQqqltcsLRKVEEEN 421
Cdd:pfam10174 564 EQEVARYKEESGKAQAEVERLLGILRE-VENEK-NDKDKKIAELESL---TLRQMKEQNKKVANIK------HGQQEMKK 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 422 QGALEMIKRLKEENEKlneflelerhNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAV---------EQ 492
Cdd:pfam10174 633 KGAQLLEEARRREDNL----------ADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHltnlraerrKQ 702
|
250 260
....*....|....*....|....*....
gi 2462558767 493 TAESCEV-QEMLKVARAEKD----LLELS 516
Cdd:pfam10174 703 LEEILEMkQEALLAAISEKDaniaLLELS 731
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
292-459 |
1.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 292 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 371
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 372 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 449
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 2462558767 450 NMMAKTLEEC 459
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
610-693 |
2.41e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 610 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 685
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 2462558767 686 KNARLQKE 693
Cdd:PRK00409 599 GGYASVKA 606
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
295-628 |
2.59e-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: 41.65 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 295 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDektiletsfhQHRERAEQLSQENEKLMNLlqeRVKNEE 374
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE----------RLDLLKAKASEAEQLRQNL---EKQQSS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 375 PTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTcSLRKVEEEnqgalemIKRLKEENEKLNEFLE----LERHNNN 450
Cdd:pfam05557 165 LAEAEQRIKELEFE----IQSQEQDSEIVKNSKSELA-RIPELEKE-------LERLREHNKHLNENIEnkllLKEEVED 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 451 MMAK--TLEECRVTLEGLKMENGSLKSHLQGEKQKATE-----------ASAVEQ--------TAESCEVQEMLKVARAE 509
Cdd:pfam05557 233 LKRKleREEKYREEAATLELEKEKLEQELQSWVKLAQDtglnlrspedlSRRIEQlqqreivlKEENSSLTSSARQLEKA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 510 KDLLELSCNELRQELLKANGEIKHVSSLLAKVRRdSSLLVEKDYSYLKEICDHQAEQL--SRTSLKLQEKASESDAEIKD 587
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR-RVLLLTKERDGYRAILESYDKELtmSNYSPQLLERIEEAEDMTQK 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462558767 588 MKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKS 628
Cdd:pfam05557 392 MQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQES 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
498-705 |
3.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 498 EVQEMLKVARAEKDllelSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKdysylkeicdHQAEQLSRTSLKLQEK 577
Cdd:COG4717 75 ELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL----------LQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 578 ASESDAEIKDMKETIFELEDQVEQhravklhnnqlISELESSVIKLEEQKSDLERQLKTLT----KQMKEETEEWRRFQA 653
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLA 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462558767 654 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNaRLQKELGDVQGHGRVVT 705
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLA 260
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-658 |
3.34e-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: 41.36 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqMVQELTAENEKLVDEKTILETSFHQHR----ERAEQLSQENEK 361
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE--LNGELSAADAAVAKDRSELEALEDQHGafldADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 362 L------MNLLQERVK---------NEEPTTQEGKIIE-LEQKCTGI---LEQGRFEREKLL----NIQQQLTCSLRKVE 418
Cdd:pfam12128 349 LpswqseLENLEERLKaltgkhqdvTAKYNRRRSKIKEqNNRDIAGIkdkLAKIREARDRQLavaeDDLQALESELREQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 419 EE-----NQGALEMIKRLKEENEKLN------EFLELERHNN---NMMAKTLEECRVTLEGLKMENGSLKSHL--QGEKQ 482
Cdd:pfam12128 429 EAgklefNEEEYRLKSRLGELKLRLNqatatpELLLQLENFDeriERAREEQEAANAEVERLQSELRQARKRRdqASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 483 KATEASAVEQTAESCEVQEML-----------------------KVARAE----------------KDLLELSCNELRQE 523
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLfpqagtllhflrkeapdweqsigKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 524 LLKANGEIKHVSSLlaKVRRDSsllVEKDYSYLKEICDHQAEQLSRTSLKLQE-KASESDAE--IKDMKETIFELEDQve 600
Cdd:pfam12128 589 RIDVPEWAASEEEL--RERLDK---AEEALQSAREKQAAAEEQLVQANGELEKaSREETFARtaLKNARLDLRRLFDE-- 661
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558767 601 qHRAVKLHNNQLISELESSViklEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTA 658
Cdd:pfam12128 662 -KQSEKDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
498-644 |
3.38e-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: 40.29 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 498 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRD-SSLLVEKDY-SYLKEIcDHQAEQLSrtslKLQ 575
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlGNVRNNKEYeALQKEI-ESLKRRIS----DLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558767 576 EKASESDAEIKDMKETIFELEDQVEQHRAvklHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEE 644
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
498-656 |
3.89e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 498 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEI-----------CDHQAEQ 566
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmyekggvcptCTQQISE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 567 LSRTSLKLQEKASESDAEIKDMKETIFELEDQV----EQHRAVKLHNNQlISELESSVIKLEEQKSDLERQLKTLTKQMK 642
Cdd:PHA02562 297 GPDRITKIKDKLKELQHSLEKLDTAIDELEEIMdefnEQSKKLLELKNK-ISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
170
....*....|....
gi 2462558767 643 EETEEWRRFQADLQ 656
Cdd:PHA02562 376 DNAEELAKLQDELD 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
292-469 |
3.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 292 LTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRE---RAEQLSQENEKLMNLLQE 368
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 369 RVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 448
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
170 180
....*....|....*....|.
gi 2462558767 449 NNMMAKTLEECRVTLEGLKME 469
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKE 1776
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
305-470 |
4.03e-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: 39.91 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 305 STAEELQATLQELSDQQQMVQELTaenEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQErvkneepttQEGKIIE 384
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAAQSQKKI---DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVAS---------QEQEIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 385 LEQKCTGIleqgrfERekllnIQQQLTCSLrkveeenqgaLEMIKRLKEENEKLNEFLELERHN-----NNMMA----KT 455
Cdd:pfam11932 81 LERQIEEI------ER-----TERELVPLM----------LKMLDRLEQFVALDLPFLLEERQArlarlRELMDdadvSL 139
|
170
....*....|....*
gi 2462558767 456 LEECRVTLEGLKMEN 470
Cdd:pfam11932 140 AEKYRRILEAYQVEA 154
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
574-698 |
4.11e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.64 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 574 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 653
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462558767 654 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 698
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-653 |
5.98e-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: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM---NL 365
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSL-----RKVEEENQGALEMIKRLKEENEKLNE 440
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 441 FLELERHNNNMMAKTLEECRVTLEG-------------------------------LKMENGSLKSHLQGEKQKA----- 484
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvlgdtllgrtlvaarLEAALRRAVTLAGRLREVTlegeg 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 485 -------TEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLK 557
Cdd:COG1196 656 gsaggslTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 558 EICDHQAEQLSRTSLKLQEKAsESDAEIKDMKETIFELEDQVEQHRAVklhnNQL-ISELESsvIK-----LEEQKSDLE 631
Cdd:COG1196 736 ELLEELLEEEELLEEEALEEL-PEPPDLEELERELERLEREIEALGPV----NLLaIEEYEE--LEerydfLSEQREDLE 808
|
410 420
....*....|....*....|....*
gi 2462558767 632 RQLKTL---TKQMKEETEEwrRFQA 653
Cdd:COG1196 809 EARETLeeaIEEIDRETRE--RFLE 831
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
291-440 |
7.34e-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: 39.62 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 291 SLTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRER------AEQLSQENEKL 362
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQ-LDALQEKLRGLEEENLKLRSEASHLktETDTYEEKEQqlmsdcVEQLSEANQQM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 363 MNLLQERVK--------NEEPTTQEGKIIELEQKCTGILEqgrfEREKLL-------NIQQQLTCSLRKVEEENQGALEM 427
Cdd:pfam04849 220 AELSEELARkmeenlrqQEEITSLLAQIVDLQHKCKELGI----ENEELQqhlqaskEAQRQLTSELQELQDRYAECLGM 295
|
170
....*....|...
gi 2462558767 428 IKRLKEENEKLNE 440
Cdd:pfam04849 296 LHEAQEELKELRK 308
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
286-663 |
7.36e-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: 40.33 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 286 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTILETS-FHQHRERAEQLSQENEKLMN 364
Cdd:COG5185 214 NLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDLRLEkLGENAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 365 LLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE---KLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 441
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 442 LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaesceVQEMLKVARAEKDLLELSCNELR 521
Cdd:COG5185 370 VELSK-----SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT-----------LEDTLKAADRQIEELQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 522 QELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSylkeicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQ 601
Cdd:COG5185 434 SSNEEVSKLLNELISELNKVMREADEESQSRLE----------EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEK 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462558767 602 HRAvklhnnqliselessvikleeqksDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVAN 663
Cdd:COG5185 504 LRA------------------------KLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
289-552 |
7.55e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 289 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL---MNL 365
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 366 LQERVKNEEPTTQEGKIIELEQKCTGILEQ--GRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLE 443
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 444 LERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQE 523
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
250 260
....*....|....*....|....*....
gi 2462558767 524 LLKANGEIKHVSSLLAKVRRDSSLLVEKD 552
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-657 |
7.63e-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: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 567 LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 646
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|.
gi 2462558767 647 EWRRFQADLQT 657
Cdd:COG4942 91 EIAELRAELEA 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
285-565 |
7.64e-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: 40.34 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 285 SELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL 362
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 363 MNLLQErvknEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslrkvEEENQGALEMIKRLKEENEKLNEFL 442
Cdd:pfam02463 815 ELLEEE----QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER-------LEEEITKEELLQELLLKEEELEEQK 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 443 ELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKA----TEASAVEQTAESCEVQEMLKVARAEKDLLELSCN 518
Cdd:pfam02463 884 LKDE-------LESKEEKEKEEKKELEEESQKLNLLEEKENEieerIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2462558767 519 ELRQELLKANGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAE 565
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
393-654 |
7.91e-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: 39.79 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 393 LEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEKLN-EFLELERHNNNMMAKTLEE-CRVTLEGLKMEN 470
Cdd:pfam15905 85 LVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEkQLLELTRVNELLKAKFSEDgTQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 471 GSLKSHLQGeKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQEllkANGEIKHVSSLLAKVRRDSSLL-- 548
Cdd:pfam15905 162 MKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKE---KIEEKSETEKLLEYITELSCVSeq 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 549 VEK---DYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravklhnnqliSELESSVIKLEE 625
Cdd:pfam15905 238 VEKyklDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE-----------------SEKEELLREYEE 300
|
250 260
....*....|....*....|....*....
gi 2462558767 626 QKSDLERQLKTLTKQMKEETEEWRRFQAD 654
Cdd:pfam15905 301 KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
294-647 |
8.88e-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: 40.03 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 294 EKIQKMEENHHSTAEELQatlQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE-RVKN 372
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 373 EEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQqqltcSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHnnnMM 452
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ-----LCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE---IL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 453 AKTLEECRVTLEGLKMENGSLKSHLQGE----KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQ-ELLKA 527
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDqelrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEmEQLNH 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558767 528 NGEIKHVSSLLAKVRRDSSLLVEKDYSYLKEICDHQAEQLSRTSlKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKL 607
Cdd:TIGR00606 530 HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462558767 608 HNNQLISELESSVIKLEEQ------KSDLERQLKTLTKQMKEETEE 647
Cdd:TIGR00606 609 HINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIEKSSKQ 654
|
|
| |
