|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
982-1093 |
4.47e-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: 250.74 E-value: 4.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 982 MLAKNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 1061
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 116007118 1062 GTTLNINDMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
977-1094 |
1.16e-57 |
|
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: 194.14 E-value: 1.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 977 KDPLNMLAKN-GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAA 1055
Cdd:cd21256 1 KDPLSALAREyGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 116007118 1056 AESVGIGTTLNINDMCQIERPDWMQVMSYVTAVYKYFET 1094
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
987-1093 |
1.29e-52 |
|
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: 179.46 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 987 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLN 1066
Cdd:cd21257 6 GGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLE 85
|
90 100
....*....|....*....|....*..
gi 116007118 1067 INDMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21257 86 LSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
991-1092 |
2.28e-38 |
|
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: 138.63 E-value: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 991 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNIND 1069
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 116007118 1070 MCQIE-RPDWMQVMSYVTAVYKYF 1092
Cdd:cd21200 83 MVRMGnRPDWKCVFTYVQSLYRHL 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
994-1092 |
2.65e-34 |
|
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: 126.77 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNINDMCQI 1073
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 116007118 1074 ERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
989-1092 |
2.90e-34 |
|
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: 127.09 E-value: 2.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
989-1092 |
2.09e-32 |
|
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: 121.61 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESV-GIGTTLNI 1067
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 116007118 1068 NDMCQIER-PDWMQVMSYVTAVYKYF 1092
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
989-1090 |
4.76e-32 |
|
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: 120.87 E-value: 4.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKhADCPQLLDV 80
|
90 100
....*....|....*....|...
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYK 1090
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
993-1093 |
2.02e-31 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.60 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 993 ALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNINDMC 1071
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 116007118 1072 QIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
987-1092 |
2.30e-31 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 118.78 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 987 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAF-AAAESVGIGTTL 1065
Cdd:cd21291 8 GLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFdIASKEIGIPQLL 87
|
90 100
....*....|....*....|....*..
gi 116007118 1066 NINDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21291 88 DVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
989-1092 |
4.91e-31 |
|
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: 117.50 E-value: 4.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21248 82 EDV-NVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
991-1090 |
9.07e-31 |
|
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: 117.11 E-value: 9.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 991 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVG-IGTTLNIND 1069
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 116007118 1070 MCQIERPDWMQVMSYVTAVYK 1090
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
989-1092 |
3.50e-30 |
|
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: 115.53 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 116007118 1068 NDMCQI-ERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21258 81 EDMMIMgKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
989-1092 |
4.67e-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: 114.82 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21194 82 EDV-DVARPDEKSIMTYVASYYHYF 105
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
992-1092 |
9.21e-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: 113.92 E-value: 9.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 992 NALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNINDM 1070
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 116007118 1071 CQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
989-1092 |
8.88e-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: 111.64 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLDP 84
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQiERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21319 85 EDVFT-ENPDEKSIITYVVAFYHYF 108
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
990-1092 |
9.48e-29 |
|
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: 111.09 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 990 KRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNIN 1068
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 116007118 1069 DMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
989-1093 |
1.27e-28 |
|
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: 110.65 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNIN 1068
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 116007118 1069 DMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
989-1092 |
1.63e-28 |
|
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: 110.72 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLDP 83
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCqIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21249 84 EDVA-VPHPDERSIMTYVSLYYHYF 107
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
994-1092 |
1.50e-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: 107.63 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNINDMCQI 1073
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 116007118 1074 ERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
991-1092 |
6.13e-26 |
|
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: 103.03 E-value: 6.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 991 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNIND 1069
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 116007118 1070 MCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
985-1092 |
2.18e-23 |
|
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: 96.28 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 985 KNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGT 1063
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTK 80
|
90 100
....*....|....*....|....*....
gi 116007118 1064 TLNINDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21321 81 LLDPEDV-NVDQPDEKSIITYVATYYHYF 108
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
989-1092 |
8.50e-23 |
|
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: 95.12 E-value: 8.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLDP 96
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21322 97 EDV-NMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
989-1092 |
1.54e-22 |
|
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: 93.63 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21320 82 EDI-SVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
989-1093 |
2.13e-22 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 93.09 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
989-1092 |
4.81e-22 |
|
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: 92.07 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21189 81 EDV-DVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
986-1093 |
1.03e-21 |
|
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: 91.26 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 986 NGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTT 1064
Cdd:cd21195 1 SGDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPV 80
|
90 100
....*....|....*....|....*....
gi 116007118 1065 LNINDMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21195 81 TTGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
994-1090 |
1.85e-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: 90.18 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAA-ESVGIGTTLNINDMcQ 1072
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPEDV-N 83
|
90
....*....|....*...
gi 116007118 1073 IERPDWMQVMSYVTAVYK 1090
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
990-1092 |
6.07e-21 |
|
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: 89.17 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 990 KRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNIN 1068
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 116007118 1069 DMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
988-1093 |
8.27e-21 |
|
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: 88.63 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 988 GSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLN 1066
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 116007118 1067 INDMcQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21192 82 VEDV-LVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
989-1092 |
1.91e-20 |
|
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: 88.22 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
989-1092 |
7.22e-20 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 86.32 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
989-1092 |
1.74e-19 |
|
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: 85.51 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
989-1092 |
3.07e-19 |
|
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: 83.94 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNIN 1068
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDAE 83
|
90 100
....*....|....*....|....
gi 116007118 1069 DMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21240 84 DV-DVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
989-1092 |
3.53e-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: 84.37 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMCQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
987-1092 |
8.15e-19 |
|
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: 82.75 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 987 GGSKRnALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTL 1065
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLL 82
|
90 100
....*....|....*....|....*..
gi 116007118 1066 NINDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21243 83 DPEDV-DVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
989-1092 |
1.75e-18 |
|
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: 81.96 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLNIN 1068
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLDPE 80
|
90 100
....*....|....*....|....
gi 116007118 1069 DMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21239 81 DV-DVSSPDEKSVITYVSSLYDVF 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-794 |
1.32e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 501 LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKI 580
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 581 EELEADLSRgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNnakcAVSHLEYRLE 660
Cdd:COG1196 298 ARLEQDIAR-----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 661 QLQRDKDKIAGEWQALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQ 740
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 116007118 741 ADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 794
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
991-1094 |
3.16e-17 |
|
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: 78.48 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 991 RNALLKWCQNKTVGY-RNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPA--NKRRNFSLAF-AAAESVGIgTTLN 1066
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALdVAEKKLGV-PKVL 82
|
90 100 110
....*....|....*....|....*....|
gi 116007118 1067 I--NDmcqIERPDWMQVMSYVTAVYKYFET 1094
Cdd:pfam00307 83 IepED---LVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
991-1090 |
3.58e-17 |
|
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: 78.15 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 991 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYD---QLTPANKRRNFSLAFAAAESVGIGTT--L 1065
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkkPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 116007118 1066 NINDMcqIERPDWMQVMSYVTAVYK 1090
Cdd:cd00014 81 EPEDL--YEKGNLKKVLGTLWALAL 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-713 |
9.87e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.88 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQslcrqteKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLL 486
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------ELEELSRQISALRKDLARLEAE---VEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 487 DLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEI 566
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 567 SRLSTLLENARSKIEELEADLSRG---------DKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGL 637
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLaaeieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 638 TEECKvvknNAKCAVSHLEYRLEQLQRD----KDKIAGEWQALEERVAELQVQCKCHQED-KAQLQSLLAETQRhLGDVQ 712
Cdd:TIGR02168 914 RRELE----ELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALENKIEDDEEEaRRRLKRLENKIKE-LGPVN 988
|
.
gi 116007118 713 L 713
Cdd:TIGR02168 989 L 989
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
494-785 |
2.25e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 84.72 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 494 EEREAVLLKQ----EELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRL 569
Cdd:TIGR02168 666 AKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 570 STLLENARSKIEELEADLS--RGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS-------QAELRRLRDQLSGLTEE 640
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealdelRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 641 CKVVKNNAKCAVSH---LEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGE 717
Cdd:TIGR02168 826 LESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 718 AECRLDQETQLRRKEAEEWQQFQADL-LMTVRVANdfKTEALSAREQLVLDN------------KTQKEKIRLLEQQLEK 784
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLeGLEVRIDN--LQERLSEEYSLTLEEaealenkieddeEEARRRLKRLENKIKE 983
|
.
gi 116007118 785 L 785
Cdd:TIGR02168 984 L 984
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
992-1060 |
2.45e-16 |
|
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: 75.43 E-value: 2.45e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007118 992 NALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPA----NKRRNFSLAFAAAESVG 1060
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLG 73
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
480-833 |
6.20e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 6.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 480 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQ--LELQRQRERIA--LLDSQLDAANAERRQGEAQFSQA 555
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEgyELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 556 MEEISQRAIEISRLSTLLENARSKIEELEAdlsrgdktdlsEVLDVARKEKDALEERVAELQ---DQCSRSQAELRRLRD 632
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNK-----------KIKDLGEEEQLRVKEKIGELEaeiASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 633 QLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQ 712
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 713 LKLGEAECRLDQETQLRRKEAEEwqqfQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQ 792
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 116007118 793 SETPQSV---LSTVQREMEMATRRSKLSFSRQDSRLSVKTLIES 833
Cdd:TIGR02169 475 KEEYDRVekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
989-1094 |
7.59e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 82.30 E-value: 7.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRN-IDITNFSSSWNDGLAFCAILHSYLPDRIPYDQL--TPANKRRNFSLAFAAAE-SVGIGTT 1064
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 116007118 1065 LNINDMCQIERPDWMQVMSYVTAVYKYFET 1094
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
989-1092 |
1.69e-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: 73.04 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRnidITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAES-VGIGTTLN 1066
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|....*.
gi 116007118 1067 INDMCQIErPDWMQVMSYVTavykYF 1092
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLS----YF 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-684 |
1.78e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 408 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLLD 487
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE---EYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 488 LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEIS 567
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 568 RLSTLLENARSKIEELEADLSRGDKTDLSEVLDVAR--KEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvK 645
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----E 458
|
250 260 270
....*....|....*....|....*....|....*....
gi 116007118 646 NNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 684
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
391-856 |
5.34e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 470
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 471 QpapEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 550
Cdd:COG1196 359 E---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 551 QFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDK--TDLSEVLDVARKEKDALEERVAELQDQcsRSQAELR 628
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAalAELLEELAEAAARLLLLLEAEADYEGF--LEGVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 629 RLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRdkDKIAGEWQALEERVAELqvqcKCHQEDKAQLQSLLAETQRHL 708
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ--NIVVEDDEVAAAAIEYL----KAAKAGRATFLPLDKIRARAA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 709 GDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDfkteALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQ 788
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR----LEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116007118 789 QMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADESESHYSSTSSL 856
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-640 |
2.98e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.67 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 385 EISVACLQDKIIQMEEThySTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQEL 464
Cdd:COG1196 226 EAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 465 LLRDTKQpapEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAE 544
Cdd:COG1196 304 IARLEER---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 545 RRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQ 624
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250
....*....|....*.
gi 116007118 625 AELRRLRDQLSGLTEE 640
Cdd:COG1196 456 EEEEALLELLAELLEE 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
479-764 |
3.07e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 479 SEREQKLLDLiktSQEEREAVL----LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQ 554
Cdd:TIGR02168 209 AEKAERYKEL---KAELRELELallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 555 AMEEISQRAIEISRL---------------------STLLENARSKIEELEADLSR---------GDKTDLSEVLDVARK 604
Cdd:TIGR02168 286 LQKELYALANEISRLeqqkqilrerlanlerqleelEAQLEELESKLDELAEELAEleekleelkEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 605 EKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvknnakcaVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 684
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-----------IERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 685 VqcKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQL 764
Cdd:TIGR02168 435 L--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
391-676 |
3.12e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADL-------QTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQE 463
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELrlevselEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 464 LLLRDtkqpapevsaserEQKLLDLiktsQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANA 543
Cdd:TIGR02168 324 QLEEL-------------ESKLDEL----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 544 ERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS 623
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 116007118 624 QAELRRLRDQLSGLTEEckvvknnakcaVSHLEYRLEQLQRDKDKIAGEWQAL 676
Cdd:TIGR02168 467 REELEEAEQALDAAERE-----------LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-735 |
6.46e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.65 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVL--FQSL------CRQTEKLNESRT----------QISTLQELLLRD 468
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAerYQALlkekreYEGYELLKEKEAlerqkeaierQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 469 TKQ-PAPEVSASEREQKLLDL----IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANA 543
Cdd:TIGR02169 257 TEEiSELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 544 ERRQGEaqfsqamEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKT--DLSEVLDVARKEKDALEERVAELQDQCS 621
Cdd:TIGR02169 337 EIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 622 RSQAELRRLRDQLSGLTEECKVvknnakcavshLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLL 701
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAG-----------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350
....*....|....*....|....*....|....*.
gi 116007118 702 AETQRHLGDVQLKLGEAECRLD--QETQLRRKEAEE 735
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEE 514
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
989-1092 |
1.44e-13 |
|
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: 67.94 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNI 1067
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLEP 84
|
90 100
....*....|....*....|....*
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21244 85 EDV-DVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
993-1092 |
2.18e-13 |
|
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: 67.11 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 993 ALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNINDMC 1071
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDVM 83
|
90 100
....*....|....*....|.
gi 116007118 1072 QiERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21226 84 T-GNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
378-646 |
2.72e-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: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 378 DKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLtdtqtenERLAEEKDVLFQSLCRQTEKLNESRTQ 457
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 458 ISTLQELLlrdtkqpapevsaSEREQKLLDLiktsQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ 537
Cdd:TIGR02168 332 LDELAEEL-------------AELEEKLEEL----KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 538 LDAANAERRQGEAQfsqameeISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQ 617
Cdd:TIGR02168 395 IASLNNEIERLEAR-------LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260
....*....|....*....|....*....
gi 116007118 618 DQCSRSQAELRRLRDQLSGLTEECKVVKN 646
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
514-816 |
3.89e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 514 KQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRgdkt 593
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 594 dlsevldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKcavsHLEYRLEQLQRDKDKIAGEW 673
Cdd:COG1196 286 --------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 674 QALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEwQQFQADLLMTVRVANDF 753
Cdd:COG1196 354 EEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEA 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 754 KTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQ-QSETPQSVLSTVQREMEMATRRSKL 816
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAElLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
502-813 |
4.21e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.95 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 502 KQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAAN-------AERRQGEAQFSQAMEEISQRAIEISRLSTLLE 574
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 575 NARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQaeLRRLRDQLSGLTEEckVVKNNAkcAVSH 654
Cdd:TIGR02169 755 NVKSELKELEARIEE------------LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEE--VSRIEA--RLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 655 LEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRL-DQETQLRRKEA 733
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 734 EewqqfqadllmtVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLS--TVQREMEMAT 811
Cdd:TIGR02169 897 Q------------LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVE 964
|
..
gi 116007118 812 RR 813
Cdd:TIGR02169 965 EE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
404-682 |
5.53e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 404 STNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNE-SRTQISTLQELLLRDTKQPAP---EVSAS 479
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASlerSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 480 EREQKLLD-LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQL---DAANAERRQGEAQFSQA 555
Cdd:TIGR02169 314 ERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 556 ME----EISQRAIEISRLSTLLENARSKIEELEADLSR--GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRR 629
Cdd:TIGR02169 394 LEklkrEINELKRELDRLQEELQRLSEELADLNAAIAGieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 116007118 630 LRDQLsglteeckvvknnakcavSHLEYRLEQLQRDKDKIAGEWQALEERVAE 682
Cdd:TIGR02169 474 LKEEY------------------DRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
400-724 |
6.11e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 6.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 400 ETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEkdvlFQSLCRQTEKLNESRT------------------QISTL 461
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDdllaeaglddadaeaveaRREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 462 Q---ELLLRDTKQPAPEVSASERE-QKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ 537
Cdd:PRK02224 320 EdrdEELRDRLEECRVAAQAHNEEaESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 538 LDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRG---------DKTDLSEVLDVARKEKDA 608
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvEGSPHVETIEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 609 LEERVAELQDQCSRSQAELRRLRDqLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGewqaLEERVAELQVQCK 688
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE----LRERAAELEAEAE 554
|
330 340 350
....*....|....*....|....*....|....*.
gi 116007118 689 CHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQ 724
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
992-1090 |
6.21e-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: 65.79 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 992 NALLKWCqNKTVGyrNIDITNFSSSWNDGLAFCAILHSyLPDRIP-YDQLTPANKRRNFSLAFAAAESVGIGTTLNINDM 1070
Cdd:cd21185 4 KATLRWV-RQLLP--DVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90 100
....*....|....*....|
gi 116007118 1071 CQIErPDWMQVMSYVTAVYK 1090
Cdd:cd21185 80 ADPE-VEHLGIMAYAAQLQK 98
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
994-1090 |
6.59e-13 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 65.75 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGIGTTLNINDMCq 1072
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPEDVA- 83
|
90
....*....|....*...
gi 116007118 1073 IERPDWMQVMSYVTAVYK 1090
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
391-785 |
2.38e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 470
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 471 QPAPEVS----ASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERR 546
Cdd:COG1196 394 AAAELAAqleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 547 QGEAQFSQAMEEISQRAIEISRLSTLLENARSKIE----ELEADLSRGDKTDLSEVLDVARKEKDALEER---------- 612
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 613 -----------------------------------------------VAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 645
Cdd:COG1196 554 eddevaaaaieylkaakagratflpldkiraraalaaalargaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 646 NNAKCAVShLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQE 725
Cdd:COG1196 634 AALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116007118 726 TQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDN-------KTQKEKIRLLEQQLEKL 785
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
416-703 |
4.92e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 416 LADLQTQLTDTQTENERlAEEKDVlfqslcrqTEKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLLDLIKTSQEE 495
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-KEEKDL--------HERLNGLESELAELDEEIERYEEQ---REQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 496 REAV-LLKQE--ELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 572
Cdd:PRK02224 250 REELeTLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 573 LENARSKIEEL--EADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECkvvkNNAKC 650
Cdd:PRK02224 330 LEECRVAAQAHneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF----GDAPV 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 116007118 651 AVSHLEYRLEQLQRDKDkiagewqALEERVAELQVQCKCHQEDKAQLQSLLAE 703
Cdd:PRK02224 406 DLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEA 451
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
987-1093 |
2.44e-11 |
|
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: 61.60 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 987 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESvGIGTTLN 1066
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAEN-ELGITPV 79
|
90 100
....*....|....*....|....*..
gi 116007118 1067 INDMCQIERPDWMQVMSYVTAVYKYFE 1093
Cdd:cd21196 80 VSAQAVVAGSDPLGLIAYLSHFHSAFK 106
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
989-1089 |
2.93e-11 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 61.19 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIGTTLNI 1067
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 81
|
90 100
....*....|....*....|..
gi 116007118 1068 NDMcQIERPDWMQVMSYVTAVY 1089
Cdd:cd21238 82 EDV-DVPQPDEKSIITYVSSLY 102
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
993-1092 |
3.47e-11 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 60.96 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 993 ALLKWCQNKTVGYrNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAA-ESVGIGTTLNINDMc 1071
Cdd:cd21245 7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLEPEDV- 84
|
90 100
....*....|....*....|.
gi 116007118 1072 QIERPDWMQVMSYVTAVYKYF 1092
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
994-1090 |
5.90e-11 |
|
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: 60.71 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQ-LTPANKRRNFSLAFAAAE-SVGIGTTLNINDMc 1071
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSvVSQQSATERLDHAFNIARqHLGIEKLLDPEDV- 83
|
90
....*....|....*....
gi 116007118 1072 QIERPDWMQVMSYVTAVYK 1090
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
554-734 |
6.45e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 554 QAMEEISQRA---IEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 630
Cdd:COG4913 242 EALEDAREQIellEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 631 RDQLSGLTEEckvVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQED----KAQLQSLLAETQR 706
Cdd:COG4913 322 REELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEE 398
|
170 180
....*....|....*....|....*....
gi 116007118 707 HLGDVQLKLGEAECRL-DQETQLRRKEAE 734
Cdd:COG4913 399 ELEALEEALAEAEAALrDLRRELRELEAE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
480-679 |
9.85e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 480 EREQKLLDLIKTSQEEREAVLLKQEELGAELAemkqareagQLELQRQRERIALLDSQLDAANAERRQGEAQfsqameei 559
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRA---------ALRLWFAQRRLELLEAELEELRAELARLEAE-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 560 sqraieISRLSTLLENARSKIEELEADLSR---GDKTDLSEVLDVARKEKDALEERVAELQDQCSR-------SQAELRR 629
Cdd:COG4913 311 ------LERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAA 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 116007118 630 LRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEER 679
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
500-672 |
1.58e-10 |
|
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: 62.63 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 500 LLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSk 579
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 580 IEELEAdlsrgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRL 659
Cdd:COG1579 88 NKEYEA---------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 116007118 660 EQLQRDKDKIAGE 672
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
992-1085 |
3.51e-10 |
|
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: 59.24 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 992 NALLKWCQNKTVGYrNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTP----------------------------- 1042
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 116007118 1043 ------ANKRRNFSLAFAAAESVG-IGTTLNINDMCqIERPDWMQVMSYV 1085
Cdd:cd21224 82 lssellANEKRNFKLVQQAVAELGgVPALLRASDMS-NTIPDEKVVILFL 130
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-640 |
5.29e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.78 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 411 ATLQELADLQTQLTDT-QTENERLAEEKDvlFQSLCRQ--------TEKLNESRTQISTLQElllrdtkqpapEVSASER 481
Cdd:COG4913 565 DSPEELRRHPRAITRAgQVKGNGTRHEKD--DRRRIRSryvlgfdnRAKLAALEAELAELEE-----------ELAEAEE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 482 EQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQlELQRQRERI-------ALLDSQLDAANAERRQGEAQFSQ 554
Cdd:COG4913 632 RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLdassddlAALEEQLEELEAELEELEEELDE 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 555 AMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARkeKDALEERVAE-LQDQCSRSQAELRRLRDQ 633
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL--GDAVERELREnLEERIDALRARLNRAEEE 788
|
....*..
gi 116007118 634 LSGLTEE 640
Cdd:COG4913 789 LERAMRA 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-845 |
5.35e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 257 ANNKMQELHKQMERFRSEQMQLETRITELlpyQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESL---RNRLRDVVNS 333
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEEL---EEQLETLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 334 PLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHdgtpcltpdwdkqssssEISVACLQDKIIQMEETHYSTNEELQATL 413
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERL-----------------EEALEELREELEEAEQALDAAERELAQLQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 414 QELADLQTQLTDTQTENERLAEEKDVLF-------------------------------QSLCrqTEKLNESRTQISTLQ 462
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaaieaalggrlQAVV--VENLNAAKKAIAFLK 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 463 E--------LLLRDTKQPAPEVSASEREQK-------LLDLIKTSQEEREAV--LLKQEELGAELAEmkqarEAGQLELQ 525
Cdd:TIGR02168 567 QnelgrvtfLPLDSIKGTEIQGNDREILKNiegflgvAKDLVKFDPKLRKALsyLLGGVLVVDDLDN-----ALELAKKL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 526 RQRERIALLDSQLDAANAERRQGEAQFSQAMEEisqRAIEISRLSTLLENARSKIEELEADLS--RGDKTDLSEVLDVAR 603
Cdd:TIGR02168 642 RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAelRKELEELEEELEQLR 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 604 KEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKvvknNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAEL 683
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT----ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 684 QVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLlmtvrvandfkTEALSAREQ 763
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----------ESLAAEIEE 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 764 LVLDNKTQKEKIRLLEQQLEKLtKQQMQQSETPQSVLSTVQREMEmaTRRSKLSFSRQDSRLSVKTLIESIEnnKAQGKA 843
Cdd:TIGR02168 864 LEELIEELESELEALLNERASL-EEALALLRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLE--GLEVRI 938
|
..
gi 116007118 844 DE 845
Cdd:TIGR02168 939 DN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
487-706 |
7.15e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 487 DLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEI 566
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 567 SRLSTLLEN------ARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQcsrsQAELRRLRDQLSGLTEE 640
Cdd:COG4942 100 EAQKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116007118 641 CKVVKNNakcavshLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQR 706
Cdd:COG4942 176 LEALLAE-------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
394-708 |
1.04e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 394 KIIQMEETHYSTNEELQATLQELADLQTQLtdtQTENERLAeekdvLFQSLCRQTEKLNESRTQISTLQELLlrdtkQPA 473
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDY---QAASDHLN-----LVQTALRQQEKIERYQADLEELEERL-----EEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 474 PEVSASEREQKLldlikTSQEEREAVLLKQEELGAELAEMKQA-----REAGQ-------------------LELQRQRE 529
Cdd:PRK04863 368 NEVVEEADEQQE-----ENEARAEAAEEEVDELKSQLADYQQAldvqqTRAIQyqqavqalerakqlcglpdLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 530 RIALLDSQLDAANAERRQGE----------AQFSQAMEEISQRAIEISRlSTLLENARSKIEELE-----ADLSRGDKTD 594
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEqklsvaqaahSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLReqrhlAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 595 LSEVLDVARKEKDAlEERVAELQDQCSR---SQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD---K 668
Cdd:PRK04863 522 LSELEQRLRQQQRA-ERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQrlaA 600
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 116007118 669 IAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHL 708
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE 640
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
404-635 |
1.36e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 404 STNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQElllrdtkqpapEVSASEREq 483
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----------ELAALEAE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 484 klldlIKTSQEEREAVLLKQEELGAELAEMKQAreagqLELQRQRERIALLDSQLDAANAERR-QGEAQFSQA----MEE 558
Cdd:COG4942 85 -----LAELEKEIAELRAELEAQKEELAELLRA-----LYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLAPArreqAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 559 ISQRAIEISRLSTLLENARSKIEELEADLSR------GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRD 632
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEeraaleALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
...
gi 116007118 633 QLS 635
Cdd:COG4942 235 EAA 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
415-632 |
1.54e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.83 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 415 ELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPApevsasEREQKLLDLiKTSQE 494
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA------ENEALLEEL-RSLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 495 EREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRA----------- 563
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAeadkdriekls 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 564 IEISRLSTLLENARSKIEELEADL-------------SRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 630
Cdd:pfam07888 325 AELQRLEERLQEERMEREKLEVELgrekdcnrvqlseSRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
..
gi 116007118 631 RD 632
Cdd:pfam07888 405 AD 406
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
391-683 |
2.41e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQ-----TEKLNESRTQISTLqELL 465
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRI-EAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 466 LRDTKQpapEVSASEREQKLL-DLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAE 544
Cdd:TIGR02169 814 LREIEQ---KLNRLTLEKEYLeKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 545 RRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKtdlsevlDVARKEKDALEERVAE-LQDQCSRS 623
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-------PKGEDEEIPEEELSLEdVQAELQRV 963
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 624 QAELRRLRDQLSGLTEECKVVknnakcavshlEYRLEQLQRDKDKIAGEWQALEERVAEL 683
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEV-----------LKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
409-806 |
2.57e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.06 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 409 LQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQ----TEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQK 484
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 485 LLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAgqlELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAI 564
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERET---ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 565 E---------------------ISRLSTLLENARSKIEELEAdlSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS 623
Cdd:pfam07888 193 EfqelrnslaqrdtqvlqlqdtITTLTQKLTTAHRKEAENEA--LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 624 QAELRRLRDQLSGLT---EECKVVKNNAKCAVSHLEYRLEQ-LQRDKDKIA---GEWQALEERVaelqvqckchQEDKAQ 696
Cdd:pfam07888 271 QAELHQARLQAAQLTlqlADASLALREGRARWAQERETLQQsAEADKDRIEklsAELQRLEERL----------QEERME 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 697 LQSLLAETQRhlgdvqlklgEAECRLDQETQLRRkeaeEWQQFQADLlmtvRVANDFKtealsarEQLVLDNKTQKEKIR 776
Cdd:pfam07888 341 REKLEVELGR----------EKDCNRVQLSESRR----ELQELKASL----RVAQKEK-------EQLQAEKQELLEYIR 395
|
410 420 430
....*....|....*....|....*....|....*
gi 116007118 777 LLEQQLEKLTKQQ-----MQQSETPQSVLSTVQRE 806
Cdd:pfam07888 396 QLEQRLETVADAKwseaaLTSTERPDSPLSDSEDE 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
528-684 |
3.01e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 528 RERIALLDSQLDAANAERRQGEAQFSQA---MEEISQRAIEISRLSTLLEN------ARSKIEELEADLSRGDKTD---- 594
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALeaeLDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 595 -LSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEeckVVKNNAKCAVSHLEYRLEQL--QRDKDKIAG 671
Cdd:COG4913 689 aLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEERfaAALGDAVER 765
|
170
....*....|....
gi 116007118 672 E-WQALEERVAELQ 684
Cdd:COG4913 766 ElRENLEERIDALR 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-589 |
1.40e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 470
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 471 QPAPEV----SASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERR 546
Cdd:COG4942 119 QPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 116007118 547 QGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSR 589
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
432-821 |
2.05e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 432 RLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPApEVSASER--EQKL------LDLIKTSQEEREAVLLKQ 503
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELE-ELSARESdlEQDYqaasdhLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 504 EELGA---ELAEMKQAREAGQLELQRQRERIALLDSQLDAAnaerRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKI 580
Cdd:COG3096 354 EDLEElteRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----KSQLADYQQALDVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 581 EEleADLSrgdktdlsevldvarkeKDALEERVAELQDQCSRSQAELRRLRDQLSglteeckvvknNAKCAVSHLEYRLE 660
Cdd:COG3096 430 GL--PDLT-----------------PENAEDYLAAFRAKEQQATEEVLELEQKLS-----------VADAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 661 QLQrdkdKIAGE------WQALEERVAElqvqckcHQEDKAQLQSLLAetqrhlgdVQLKLGEAECRLDQETQLRR---- 730
Cdd:COG3096 480 LVC----KIAGEversqaWQTARELLRR-------YRSQQALAQRLQQ--------LRAQLAELEQRLRQQQNAERllee 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 731 ----------------KEAEEWQQFQADLLMTVRVANDFKTEALSAREQLvldnktqKEKIRLLEQQ----------LEK 784
Cdd:COG3096 541 fcqrigqqldaaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL-------RARIKELAARapawlaaqdaLER 613
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 116007118 785 LTKQQMQQSETPQSVLSTVQ----REMEMATRRSKLSFSRQ 821
Cdd:COG3096 614 LREQSGEALADSQEVTAAMQqlleREREATVERDELAARKQ 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-682 |
2.21e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 472 PAPEVSASEREQKLLDL---IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 548
Cdd:COG4942 16 AAQADAAAEAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 549 EAQFSQAMEEISQRAIEISRLS-----TLLENARS-----KIEELEADLSRGDKTDLsEVLDVARKEKDALEERVAELQD 618
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGrqpplALLLSPEDfldavRRLQYLKYLAPARREQA-EELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 619 QCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAE 682
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
399-835 |
2.42e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 58.26 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 399 EETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTL----QELLLRDTKQPAP 474
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaarkQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 475 EVSASEREQKLldliktsQEEREAVLLKQEELGAELAEMKQAREAGQLE-------LQRQRERIALLDSQLDAANAERRQ 547
Cdd:pfam01576 84 LEEEEERSQQL-------QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 548 GEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVldvarKEKDALEERVAELQDQCSRSQAEL 627
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE-----KAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 628 RRLRDQLSGLTEECKVV----------KNNAKCAVSHLEYRLEQLQRD-------KDKIAGEWQALEERVAELQVQCKCH 690
Cdd:pfam01576 232 AELRAQLAKKEEELQAAlarleeetaqKNNALKKIRELEAQISELQEDleseraaRNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 691 QEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQ-LRRKEAEEWQQFQADLLMTVRvandFKTEALSAREQLVLDNK 769
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQeMRQKHTQALEELTEQLEQAKR----NKANLEKAKQALESENA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 770 TQKEKIRLLEQ---QLEKLTKQQMQQSETPQSVLSTVQRE-MEMATRRSKLsfsrQDSRLSVKTLIESIE 835
Cdd:pfam01576 388 ELQAELRTLQQakqDSEHKRKKLEGQLQELQARLSESERQrAELAEKLSKL----QSELESVSSLLNEAE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
483-787 |
2.66e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 483 QKLLDLIKTSQEEREAVLlkQEELGAELAEmKQAREAGQL--ELQRQRERIALLDSQldAANAERRQG--EAQFSQAMEE 558
Cdd:PRK03918 134 QGEIDAILESDESREKVV--RQILGLDDYE-NAYKNLGEVikEIKRRIERLEKFIKR--TENIEELIKekEKELEEVLRE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 559 ISQRAIEISRLSTLLENARSKIEELEAdlSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLT 638
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEE--LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 639 EECKVVKnnakcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSL---LAETQRHLGDVQ--- 712
Cdd:PRK03918 287 ELKEKAE-----EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkkLKELEKRLEELEerh 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116007118 713 LKLGEAECRLDQETQLRRKEAEEwqqfqadllmTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTK 787
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
408-640 |
2.71e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 408 ELQATLQELADLQTQLTDTQTENERLAEEKDVLfQSLCRQTEKLNESRTQISTLQELL-------------LRDTKQPAP 474
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRaalrlwfaqrrleLLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 475 EVSASEREQKLLDL---IKTSQEEREAVLLKQEEL-GAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 550
Cdd:COG4913 301 RAELARLEAELERLearLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 551 QFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLsrgdktdlsevldvaRKEKDALEERVAELQDQCSRSQAELRRL 630
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDL---------------RRELRELEAEIASLERRKSNIPARLLAL 445
|
250
....*....|...
gi 116007118 631 RDQLS---GLTEE 640
Cdd:COG4913 446 RDALAealGLDEA 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
531-743 |
3.06e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 531 IALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALE 610
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 611 ERVAELQDQCSRSQAELRRLRDQLS---------GLTEECKVVKN--NAKCAVSHLEY----------RLEQLQRDKDKI 669
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAellralyrlGRQPPLALLLSpeDFLDAVRRLQYlkylaparreQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 670 AGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAEcrldQETQLRRKEAEEWQQFQADL 743
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA----AELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
461-640 |
5.08e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 461 LQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLD--SQL 538
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 539 DAANAERRQGEAQ---FSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEvldvARKEKDALEERVAE 615
Cdd:COG4717 135 EALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----LAEELEELQQRLAE 210
|
170 180
....*....|....*....|....*
gi 116007118 616 LQDQCSRSQAELRRLRDQLSGLTEE 640
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENE 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
555-735 |
7.70e-08 |
|
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: 54.55 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 555 AMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQL 634
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELA-----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 635 SGLTEECKVVKNNAkcavshlEYrlEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLK 714
Cdd:COG1579 76 KKYEEQLGNVRNNK-------EY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
170 180
....*....|....*....|.
gi 116007118 715 LGEAECRLDQETQLRRKEAEE 735
Cdd:COG1579 147 LDEELAELEAELEELEAEREE 167
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
989-1086 |
9.11e-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: 51.23 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 989 SKRNALLKWCQNKTVGyrnIDITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAES-VGIGTTLN 1066
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|
gi 116007118 1067 INDMCQiERPDWMQVMSYVT 1086
Cdd:cd21230 78 PEEIIN-PNVDEMSVMTYLS 96
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
468-801 |
2.21e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 468 DTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRErialldsQLDAANAERRQ 547
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-------ELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 548 GEAQFSQAMEEISQRAIEISRlstLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDAL--EERVAELQDQCSRSQA 625
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 626 ELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDkiagewqalEERVAELQVQCKCHQEDKA-QLQSLLAET 704
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---------DEKKAAEALKKEAEEAKKAeELKKKEAEE 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 705 QRHLGDVQlklGEAECRLDQETQLRRKEAEE---WQQFQADLLMTVRVANDFKTEALSAREqlvldnkTQKEKIRLLEQQ 781
Cdd:PTZ00121 1715 KKKAEELK---KAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEE-------IRKEKEAVIEEE 1784
|
330 340
....*....|....*....|.
gi 116007118 782 L-EKLTKQQMQQSETPQSVLS 801
Cdd:PTZ00121 1785 LdEEDEKRRMEVDKKIKDIFD 1805
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
260-738 |
2.39e-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: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 260 KMQELHKQMERFRSEQMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNlkyENESLRNRLRDVVNSPLSDAE 339
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITC---TAQCEKLEKIHLQESAQSLKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 340 KHQIIQDSQRLHSSAPASIALPSTH-DAHDGTPCLTpdwdkQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQE-LA 417
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARlLELQEEPCPL-----CGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETsEE 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 418 DLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLlrDTKQPAPEVSASEREQKLLDLIKTSQEERE 497
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT--VRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 498 A-----VLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDS-QLDAANAERRQGEAQFSQA--------MEEISQRA 563
Cdd:TIGR00618 624 EqdlqdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKMQSekeqltywKEMLAQCQ 703
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 564 IEISRLSTLLENARSKIEELEADLS------RGDKTDLSEVLDVARKEKD-ALEERVAELQDQCSRSQAELRRLrDQLSG 636
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSslgsdlAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTG-AELSH 782
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 637 LTEECKVVKNNAKCAVSHLEYRLEQLQrdkdkiagewQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLG 716
Cdd:TIGR00618 783 LAAEIQFFNRLREEDTHLLKTLEAEIG----------QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
490 500
....*....|....*....|..
gi 116007118 717 EAECRLDQETQLRRKEAEEWQQ 738
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQL 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-634 |
3.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVLfqslcrqteklnesrTQISTLQELLLrDTKQPAPEVSASEREQKLL 486
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAL---------------QRLAEYSWDEI-DVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 487 DL----IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG-----EAQFSQAME 557
Cdd:COG4913 681 DAssddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElrallEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 558 EISQRAI------EISRLSTLLENARSKIEEL--------EADLSRGDKT--DLSEVLDVARK-EKDALEERVAELQDQC 620
Cdd:COG4913 761 DAVERELrenleeRIDALRARLNRAEEELERAmrafnrewPAETADLDADleSLPEYLALLDRlEEDGLPEYEERFKELL 840
|
250
....*....|....*
gi 116007118 621 -SRSQAELRRLRDQL 634
Cdd:COG4913 841 nENSIEFVADLLSKL 855
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-683 |
4.21e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKdvlfQSLCRQTEKLNESRTQISTLQ------ELLLRDTKQPAPEVSasE 480
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEgskrklEEKIRELEERIEELK--K 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 481 REQKLLDLIKTSqEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQL-DAANAERRQGEaqFSQAMEEI 559
Cdd:PRK03918 274 EIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkELEEKEERLEE--LKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 560 SQRAIEISRLSTLLENARSKIEELE---ADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLsg 636
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELErlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-- 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 116007118 637 ltEECKVVKnnAKCAV-------SHLEYRLEQLQRDKDKIAGEWQALEERVAEL 683
Cdd:PRK03918 429 --EELKKAK--GKCPVcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
407-636 |
4.97e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELAD----LQTQLTDTQTENERLAEEkdvlFQSLCRQTEKLNESRTQiSTLQELLLRDTKQPAPEVSASERE 482
Cdd:PRK04863 445 EEFQAKEQEATEellsLEQKLSVAQAAHSQFEQA----YQLVRKIAGEVSRSEAW-DVARELLRRLREQRHLAEQLQQLR 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 483 QKLLDLIKTSQEEREAVLLkQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLdaanAERRQGEAQFSQAMEEISQR 562
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERL-LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV----SEARERRMALRQQLEQLQAR 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 563 AIEISRLSTLLENARSKIEEL-----EADLSRGDKT----DLSEVLDVARKEKDALEERVAELQDQCSR-------SQAE 626
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLreqsgEEFEDSQDVTeymqQLLERERELTVERDELAARKQALDEEIERlsqpggsEDPR 674
|
250
....*....|
gi 116007118 627 LRRLRDQLSG 636
Cdd:PRK04863 675 LNALAERFGG 684
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
404-603 |
1.01e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 404 STNEELQATLQELADLQTQLTDTQTEnerlaeekdvlfqslcrqtekLNESRTQISTLQElLLRDTKQPAPEVSASEREQ 483
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAE---------------------LAEAEARLAALRA-QLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 484 KLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERI-ALLDSQLDAANAER---RQGEAQFSQAMEEI 559
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREaslQAQLAQLEARLAEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 116007118 560 SQRAIEISRLSTLLENARSKIEEL-----EADLSRGDKTDLSEVLDVAR 603
Cdd:COG3206 347 PELEAELRRLEREVEVARELYESLlqrleEARLAEALTVGNVRVIDPAV 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
480-795 |
1.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 480 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQR---QRERIALLDSQLDAANAERRQGEAQFSQA- 555
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELe 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 556 -------------------MEEISQRAIEISRLSTLLENARSKIEELEADLSR------------GDKTDLSEVLDVARK 604
Cdd:PRK03918 266 erieelkkeieeleekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRleeeingieeriKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 605 EKDALEERVAELQ------DQCSRSQAELRRLRDQLSGLTEEcKVVKNnakcaVSHLEYRLEQLQRDKDKIAGEWQALEE 678
Cdd:PRK03918 346 KLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPE-KLEKE-----LEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 679 RVAELQ--------VQCKC-------HQEDKAQlqsLLAETQRHLGDVQLKLGEAEcrlDQETQLRRKEAEewqqfqadl 743
Cdd:PRK03918 420 EIKELKkaieelkkAKGKCpvcgrelTEEHRKE---LLEEYTAELKRIEKELKEIE---EKERKLRKELRE--------- 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 116007118 744 lmtvrvandfkTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSET 795
Cdd:PRK03918 485 -----------LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-605 |
1.50e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 258 NNKMQELHKQMERFRSE----QMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVvNS 333
Cdd:TIGR02168 676 RREIEELEEKIEELEEKiaelEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-SK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 334 PLSDAEKhQIIQDSQRLHSSAPASIALPSTHDAhdgtpcLTPDWDKQSSSSEISVACLQDKiiqmEETHYSTNEELQATL 413
Cdd:TIGR02168 755 ELTELEA-EIEELEERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 414 QELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELL-----LRDTKQPAPEVSASERE------ 482
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEelseel 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 483 -------QKLLDLIKTSQEEREAVLLKQEELGAELAEMK-QAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQ 554
Cdd:TIGR02168 904 releskrSELRRELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116007118 555 -------AMEE---ISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKE 605
Cdd:TIGR02168 984 lgpvnlaAIEEyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
391-836 |
1.93e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQatlQELADLQTQLTDTQTENERLAE--------EKDVLFQ----------SLCRQTEKLN 452
Cdd:pfam15921 90 LQRRLNESNELHEKQKFYLR---QSVIDLQTKLQEMQMERDAMADirrresqsQEDLRNQlqntvheleaAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 453 ESRTQISTLQELLLrdtkqpAPEVSASEREQKLLDLIKTSQEE---------------REAVLLKQEELGAELAEMK--- 514
Cdd:pfam15921 167 DSNTQIEQLRKMML------SHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrslGSAISKILRELDTEISYLKgri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 515 ------------QAREAGQLELQRQRERIALLDSQ--------LDAANAERRQGEA--------------QFSQAMEEIS 560
Cdd:pfam15921 241 fpvedqlealksESQNKIELLLQQHQDRIEQLISEheveitglTEKASSARSQANSiqsqleiiqeqarnQNSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 561 QRAIEISRLSTLLENAR----SKIEELEADLSRGDkTDLSEvldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSG 636
Cdd:pfam15921 321 DLESTVSQLRSELREAKrmyeDKIEELEKQLVLAN-SELTE----ARTERDQFSQESGNLDDQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 637 LTEECKVVKNNAkcavSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCkchqedKAQLQSLLAETQRHLGDVQlKLG 716
Cdd:pfam15921 396 EKEQNKRLWDRD----TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC------QGQMERQMAAIQGKNESLE-KVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 717 EAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFkTEALSAREQLVLDNKTQKEKIRlleqQLEKLTKQQMQQSETP 796
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL-TASLQEKERAIEATNAEITKLR----SRVDLKLQELQHLKNE 539
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 116007118 797 QSVLSTVQREMEMAtrrsKLSFSRQDSRLSVktLIESIEN 836
Cdd:pfam15921 540 GDHLRNVQTECEAL----KLQMAEKDKVIEI--LRQQIEN 573
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
407-789 |
2.03e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQ-----------SLCRQTEKLNESRTQISTL---QELLLRDTKQP 472
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRrarLEALLAALGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 473 APEVSAS--EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAA--------- 541
Cdd:COG4913 375 LPASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaealg 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 542 -----------------NAERRQG----------------EAQFSQAMEEISQRaieisRLSTLLENARSKIEELEADLS 588
Cdd:COG4913 455 ldeaelpfvgelievrpEEERWRGaiervlggfaltllvpPEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERP 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 589 RGDKTDLSEVLDVARKE-KDALEERVAELQD-QCSRSQAELRRLRdqlSGLTEECkVVKNNakcavshleYRLEQLQrDK 666
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPfRAWLEAELGRRFDyVCVDSPEELRRHP---RAITRAG-QVKGN---------GTRHEKD-DR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 667 DKIAGEW----------QALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDqeTQLRRKEAEEW 736
Cdd:COG4913 596 RRIRSRYvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAEL 673
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 116007118 737 QQFQADLL---MTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQ 789
Cdd:COG4913 674 EAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
576-845 |
2.39e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 576 ARSKIEELEADLSRgdktdLSEVLDVARKEKDALE------ERVAELQDQCSRSQAELRRLRDQLsgLTEECKVVKNNAK 649
Cdd:COG1196 177 AERKLEATEENLER-----LEDILGELERQLEPLErqaekaERYRELKEELKELEAELLLLKLRE--LEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 650 cavsHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLklgeaecrldqETQLR 729
Cdd:COG1196 250 ----ELEAELEELEAELAELEAELEELRLELEELELE---LEEAQAEEYELLAELARLEQDIAR-----------LEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 730 RKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEM 809
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270
....*....|....*....|....*....|....*.
gi 116007118 810 ATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 845
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-628 |
2.75e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 262 QELHKQMERFRSEQMQLETRITELlpyQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVvNSPLSDAEKH 341
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEEL---REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-PVDLGNAEDF 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 342 --QIIQDSQRLHSS-APASIALPSTHDA-------HDGTPCltPDWDKQSSSSEIsVACLQDKIIQME--ETHYSTNEEL 409
Cdd:PRK02224 414 leELREERDELREReAELEATLRTARERveeaealLEAGKC--PECGQPVEGSPH-VETIEEDRERVEelEAELEDLEEE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 410 QATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTL----QELLLRDTKQPAPEVSASEREQKL 485
Cdd:PRK02224 491 VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEAEEA 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 486 LDLIKTSQEEREAV-------------LLKQEELGAELAEMKQAREA-GQLELQRQ------RERIALLDSQLDAANAER 545
Cdd:PRK02224 571 REEVAELNSKLAELkerieslerirtlLAAIADAEDEIERLREKREAlAELNDERRerlaekRERKRELEAEFDEARIEE 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 546 -RQGEAQFSQAMEEISQRAIEISRLSTLLENA----RSKIEELEadlsrgdktDLSEVLDVARKEKDALE---ERVAELQ 617
Cdd:PRK02224 651 aREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELE---------ELRERREALENRVEALEalyDEAEELE 721
|
410
....*....|.
gi 116007118 618 DQCSRSQAELR 628
Cdd:PRK02224 722 SMYGDLRAELR 732
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
294-840 |
3.15e-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: 51.26 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 294 KLKGDLVKMQSLQEKSQMEIGN-------LKYENESLRNRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHda 366
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDkekqvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH-- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 367 hdgtpcLTPDWDKQSSSSEISVA---CLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQS 443
Cdd:pfam05483 294 ------LTKELEDIKMSLQRSMStqkALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 444 LCRQTEKlNESRTQISTLQelLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELgAELAEMKQAREAGQLE 523
Cdd:pfam05483 368 EQQRLEK-NEDQLKIITME--LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-EKIAEELKGKEQELIF 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 524 LQRQRER-IALLDSQLDAANAERRQGEAQFSQAMEEISQ---RAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVL 599
Cdd:pfam05483 444 LLQAREKeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 600 DVARKEK------DALEERVAELQDQCSRSQAELRRLRDQLsglteECKVVKN--NAKCAVSHLEYRLEQLQRDKDKIAG 671
Cdd:pfam05483 524 NCKKQEErmlkqiENLEEKEMNLRDELESVREEFIQKGDEV-----KCKLDKSeeNARSIEYEVLKKEKQMKILENKCNN 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 672 EWQALEERVAELQvqcKCHQEDKAQLQSLLAETQR------HLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLM 745
Cdd:pfam05483 599 LKKQIENKNKNIE---ELHQENKALKKKGSAENKQlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 746 TVRVANDFKTEALSAREQLvldNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQ-REMEMATRRSKLSFSRQDSR 824
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEI---DKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKnKEQEQSSAKAALEIELSNIK 752
|
570
....*....|....*.
gi 116007118 825 LSVKTLIESIENNKAQ 840
Cdd:pfam05483 753 AELLSLKKQLEIEKEE 768
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
481-822 |
3.20e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 481 REQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQR----ERIALLDSQLDAANAERRQGEAQFSQAM 556
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRreleSRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 557 EEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSG 636
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIK-----TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 637 LTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEE---RVAELQVQCkchqEDKAQLQSLLAETQRH---LGD 710
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALL----EELRSLQERLNASERKvegLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 711 VQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRvandfKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQM 790
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR-----EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEER 333
|
330 340 350
....*....|....*....|....*....|..
gi 116007118 791 QQSETPQSVLSTVQREMEMATRRSKLSFSRQD 822
Cdd:pfam07888 334 LQEERMEREKLEVELGREKDCNRVQLSESRRE 365
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-676 |
3.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 262 QELHKQMERFRSEQMQLETRITELlpyQSEVAKLKGDLVKMQSLQEKSQ--MEIGNLKYENESLRNRLRDVvnsplsdAE 339
Cdd:COG4717 91 AELQEELEELEEELEELEAELEEL---REELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERLEEL-------RE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 340 KHQIIQDSQRLHSSAPASIALPSTHdahdgtpcLTPDWDKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADL 419
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQ--------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 420 QTQLTDTQtENERLAEEKDVL--------FQSLCRQTEKLNESRTQISTLQE-----LLLRDTKQPAPEVSASEREQKLL 486
Cdd:COG4717 233 ENELEAAA-LEERLKEARLLLliaaallaLLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 487 DLIKTSQEEREAVL--------LKQEELGAELAEMKQAREAgQLELQRQRERIALLDSQ------LDAANAErrqGEAQF 552
Cdd:COG4717 312 ALEELEEEELEELLaalglppdLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEqeiaalLAEAGVE---DEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 553 SQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRD 632
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 116007118 633 QLsglteeckvvknnakcAVSHLEYRLEQLQRDKDKIAGEWQAL 676
Cdd:COG4717 468 DG----------------ELAELLQELEELKAELRELAEEWAAL 495
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
379-642 |
3.62e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 379 KQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTdtqtENERLAEEKDVLFQSLCRQTEKLN---ESR 455
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILT----EKEALQGKINILEMRLSETDARIKlaaQEK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 456 TQISTLQELLLRDTKQPAPEvSASEREQKL-----LDLIKTsqeerEAVLLKQ--EELGAELAEMKQAREAgQLELQRQR 528
Cdd:PLN02939 194 IHVEILEEQLEKLRNELLIR-GATEGLCVHslskeLDVLKE-----ENMLLKDdiQFLKAELIEVAETEER-VFKLEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 529 eriALLDSQLdaanaerRQGEAQFSQAMEEISQ---RAIE-----ISRLSTLLENA-----------------RSKIEEL 583
Cdd:PLN02939 267 ---SLLDASL-------RELESKFIVAQEDVSKlspLQYDcwwekVENLQDLLDRAtnqvekaalvldqnqdlRDKVDKL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 584 EADLSRGDKTDLS-EVLDVARKEKDALEERV----AELQDQCSRSQAELRRLRDQLSGLTEECK 642
Cdd:PLN02939 337 EASLKEANVSKFSsYKVELLQQKLKLLEERLqasdHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
472-686 |
3.91e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 472 PAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQ 551
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 552 FSQAMEEISQRAIEISRLSTLLENarskiEELEADLSRGDKTDL-----SEVLDVARKEKDALEERVAELQDQcsrsQAE 626
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGS-----ESFSDFLDRLSALSKiadadADLLEELKADKAELEAKKAELEAK----LAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 627 LRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQ 686
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-787 |
4.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 379 KQSSSSEISVACLQDKIIQMEETHystnEELQATLQELADLQTQLTDTQ---TENERLAEEKDVLFQSLCRQTEKLNESR 455
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERI----EELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 456 TQISTLQELL--LRDTKQPAPEVSASERE-QKLLDLIKTSQEEREAVLLKQ---------------EELGAELAEMKQAR 517
Cdd:PRK03918 321 EEINGIEERIkeLEEKEERLEELKKKLKElEKRLEELEERHELYEEAKAKKeelerlkkrltgltpEKLEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 518 EAGQLELQRQRERIALLDS---QLDAANAERRQGEAQ----------------FSQAMEEISQRAIEISRLSTLLENARS 578
Cdd:PRK03918 401 EEIEEEISKITARIGELKKeikELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 579 KIEELEADLSRGDK-TDLSEVLDVARKEKDALEERVAElqdQCSRSQAELRRLRDQLSGLTEECKVVKNNAKcAVSHLEY 657
Cdd:PRK03918 481 ELRELEKVLKKESElIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 658 RLEQLQRDKDKIAGEWQALEERVAELQVqcKCHQEDKAQLQSL----------------LAETQRHLGDVQLKLGEAECR 721
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGF--ESVEELEERLKELepfyneylelkdaekeLEREEKELKKLEEELDKAFEE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 722 LDQE-----------TQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLV------LDN-KTQKEKIRLLEQQLE 783
Cdd:PRK03918 635 LAETekrleelrkelEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRReeikktLEKlKEELEEREKAKKELE 714
|
....
gi 116007118 784 KLTK 787
Cdd:PRK03918 715 KLEK 718
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
414-808 |
5.63e-06 |
|
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: 50.56 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 414 QELADLQTQLTDTQTENERLAEEK------------DVLFqsLCRQTEKLNESRTQistLQELLLRDTKQPAPEVSASER 481
Cdd:pfam01576 103 QHIQDLEEQLDEEEAARQKLQLEKvtteakikkleeDILL--LEDQNSKLSKERKL---LEERISEFTSNLAEEEEKAKS 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 482 EQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQ-----------RERIALLDSQLDAANAERRQGEA 550
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaelqaqiaelRAQLAKKEEELQAALARLEEETA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 551 QFSQAMEEISQRAIEISRLSTLLEN---ARSKIEELEADLSR---GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQ 624
Cdd:pfam01576 258 QKNNALKKIRELEAQISELQEDLESeraARNKAEKQRRDLGEeleALKTELEDTLDTTAAQQELRSKREQEVTELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 625 AELRRLRDQLSGLTEeckvvKNNAkcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQlqsllAET 704
Cdd:pfam01576 338 EETRSHEAQLQEMRQ-----KHTQ--ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD-----SEH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 705 QRHLGDVQLklgeaecrldQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLdnKTQKEkIRLLEQQLEK 784
Cdd:pfam01576 406 KRKKLEGQL----------QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI--KLSKD-VSSLESQLQD 472
|
410 420
....*....|....*....|....*
gi 116007118 785 LtkQQMQQSETPQSV-LSTVQREME 808
Cdd:pfam01576 473 T--QELLQEETRQKLnLSTRLRQLE 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
399-737 |
7.28e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 399 EETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQT---------EKLNESRTQISTLQELLLRDT 469
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelpERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 470 KQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQ-EELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 548
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 549 EAQ-------------------------------------------FSQAMEEISQRAIEISRLSTLLENARSKIEELEA 585
Cdd:COG4717 247 EARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 586 DLSRGDKTDLSEVLDVARKEKDaLEERVAELQDQcsRSQAELRRLRDQLSGLTEECKVV--------------KNNAKCA 651
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEE-LQELLREAEEL--EEELQLEELEQEIAALLAEAGVEdeeelraaleqaeeYQELKEE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 652 VSHLEYRLEQL---------QRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRhlgdvQLKLGEAECRL 722
Cdd:COG4717 404 LEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQEL 478
|
410
....*....|....*
gi 116007118 723 DQETQLRRKEAEEWQ 737
Cdd:COG4717 479 EELKAELRELAEEWA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
257-663 |
7.32e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 257 ANNKMqELHKQMERFRSEQM--QLETRITELLPYQSEVAKLKGDL-VKMQSLQEKSQ-------MEIGNLKYENESLRNR 326
Cdd:pfam15921 254 SQNKI-ELLLQQHQDRIEQLisEHEVEITGLTEKASSARSQANSIqSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 327 LRD---VVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSssEISVACLQDKIIQMEETHY 403
Cdd:pfam15921 333 LREakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK--ELSLEKEQNKRLWDRDTGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 404 STN-----EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQ-PAPEVS 477
Cdd:pfam15921 411 SITidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEElTAKKMT 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 478 ASEREQKLLDLIKTSQEE--------------REAVLLKQEEL------GAELAEMKQAREAGQLELQRQRERIALLDSQ 537
Cdd:pfam15921 491 LESSERTVSDLTASLQEKeraieatnaeitklRSRVDLKLQELqhlkneGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 538 LD-----AANAERRQGEAQFSQAM--EEISQRAIEISRLSTLLENARSKIEELEADLSrgdKTDLSEVldvarKEKDALE 610
Cdd:pfam15921 571 IEnmtqlVGQHGRTAGAMQVEKAQleKEINDRRLELQEFKILKDKKDAKIRELEARVS---DLELEKV-----KLVNAGS 642
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 116007118 611 ERVAELQD-QCSRSQA--ELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQ 663
Cdd:pfam15921 643 ERLRAVKDiKQERDQLlnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
391-725 |
7.58e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEEL---QATLQELADLQTQLTDTQTENE---RLAEEKDVLFQSLCRQTEKLNESRTQISTLQEL 464
Cdd:COG3096 283 LSERALELRRELFGARRQLaeeQYRLVEMARELEELSARESDLEqdyQAASDHLNLVQTALRQQEKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 465 LlrdtkQPAPEVSASEREQKLldlikTSQEEREAVLLKQEELGAELAEMKQA-----REAGQLELQRQR----------- 528
Cdd:COG3096 363 L-----EEQEEVVEEAAEQLA-----EAEARLEAAEEEVDSLKSQLADYQQAldvqqTRAIQYQQAVQAlekaralcglp 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 529 --------ERIALLDSQLDAANAERRQGE----------AQFSQAMEEISQRAIEISRLST------LLENARS------ 578
Cdd:COG3096 433 dltpenaeDYLAAFRAKEQQATEEVLELEqklsvadaarRQFEKAYELVCKIAGEVERSQAwqtareLLRRYRSqqalaq 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 579 --------------------KIEELEADLSRGDKTDLSEVLDVARkEKDALEERVAELQDQCSRSQA---ELRRLRDQls 635
Cdd:COG3096 513 rlqqlraqlaeleqrlrqqqNAERLLEEFCQRIGQQLDAAEELEE-LLAELEAQLEELEEQAAEAVEqrsELRQQLEQ-- 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 636 glteeckvvknnakcavshleyrLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQL-- 713
Cdd:COG3096 590 -----------------------LRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVer 646
|
410
....*....|...
gi 116007118 714 -KLGEAECRLDQE 725
Cdd:COG3096 647 dELAARKQALESQ 659
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
974-1087 |
7.65e-06 |
|
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: 46.31 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 974 GERKDPLNmlaKNGGSKRNALLKWCQNKTvgyRNIDITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLA 1052
Cdd:cd21315 4 GEDDGPDD---GKGPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEA 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 116007118 1053 FAAAES-VGIGTTLNINDMCQiERPDWMQVMSYVTA 1087
Cdd:cd21315 78 MDLAEDwLDVPQLIKPEEMVN-PKVDELSMMTYLSQ 112
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-795 |
8.21e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 413 LQELADLQTQLTDTQTENERLAEEKDVLFQSlcrqTEKLNESRTQISTLQElllrdtkqpapEVSASEREQKLLDLIKTS 492
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELRE-----------ELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 493 QEEREavllKQEELGAELAEMKQAREagqlELQRQRERIALLDSQLDAANAERRQGEAQFSQAME-EISQRAIEISRLST 571
Cdd:COG4717 135 EALEA----ELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 572 LLENARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQAELRR--------LRDQLSGLTEECKV 643
Cdd:COG4717 207 RLAELEEELEEAQEELEE------------LEEELEQLENELEAAALEERLKEARLLLliaaallaLLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 644 VKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLD 723
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007118 724 QETQLRRK-EAEEWQQFQADLLMTVRVANDfktEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSET 795
Cdd:COG4717 355 EAEELEEElQLEELEQEIAALLAEAGVEDE---EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
405-570 |
8.25e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.03 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 405 TNEELQATLQ-ELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQ 483
Cdd:pfam05667 325 TEEELQQQREeELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIA 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 484 KLLDLIKTSqEEREAVLLKQEE-----LGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEE 558
Cdd:pfam05667 405 KLQALVDAS-AQRLVELAGQWEkhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAE 483
|
170
....*....|..
gi 116007118 559 ISQRAIEISRLS 570
Cdd:pfam05667 484 YERLPKDVSRSA 495
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
391-788 |
1.10e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLlrdtk 470
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 471 qpapevsaSEREQKLLDLIKtsqeEREAVLLKqeELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 550
Cdd:TIGR04523 291 --------NQLKSEISDLNN----QKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 551 QFSQAMEEISQRAIEISRL-------STLLENARSKIEELEADLSRGDKTD--LSEVLDVARKEKDALEERVAELQDQCS 621
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLkkenqsyKQEIKNLESQINDLESKIQNQEKLNqqKDEQIKKLQQEKELLEKEIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 622 RSQAELRRLRDQLSGLteecKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQA---------------------LEERV 680
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVK----ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekelkklneekkeLEEKV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 681 AELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLD-----QETQLRRKEAEEWQQFQADLLmtvrVANDFKT 755
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLK----KKQEEKQ 588
|
410 420 430
....*....|....*....|....*....|...
gi 116007118 756 EALSAREQlvlDNKTQKEKIRLLEQQLEKLTKQ 788
Cdd:TIGR04523 589 ELIDQKEK---EKKDLIKEIEEKEKKISSLEKE 618
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
540-780 |
1.25e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 540 AANAERRQGEAqfSQAMEEISQRaieisrlstlLENARSKIEELEADLS----RGDKTDLSEVLDVARKEKDALEERVAE 615
Cdd:COG3206 163 EQNLELRREEA--RKALEFLEEQ----------LPELRKELEEAEAALEefrqKNGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 616 LQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAkcAVSHLEYRLEQLQRDKDKIAGEW-------QALEERVAELQvqck 688
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALR---- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 689 chQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQlRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDN 768
Cdd:COG3206 305 --AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA-RLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
250
....*....|..
gi 116007118 769 KTQKEKIRLLEQ 780
Cdd:COG3206 382 ALTVGNVRVIDP 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-630 |
1.41e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 262 QELHKQMERFRSEQMQLETRITELL----PYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLSD 337
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEeeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 338 AEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSSSEISVAC-----LQDKIIQMEETHYSTNEELQAT 412
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 413 LQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTS 492
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 493 QEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 572
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 116007118 573 LENARSKIEELEADLSrgdktdlsEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 630
Cdd:COG1196 730 LEAEREELLEELLEEE--------ELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
378-563 |
1.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 378 DKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNE---- 453
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 454 ---SRTQISTLQELLlrDTKQPAPEVS-------ASEREQKLLDLIKTSQEE----REAVLLKQEELGAELAEMKQAREA 519
Cdd:COG3883 95 lyrSGGSVSYLDVLL--GSESFSDFLDrlsalskIADADADLLEELKADKAEleakKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116007118 520 GQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRA 563
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
491-836 |
2.81e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 491 TSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALldsqldAANAERRQG-EAQFSQAMEEISQRAIEISRL 569
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL------VQTALRQQEkIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 570 StllENARSKIEELEADLSRGD------KTDLSEV---LDVARKE-------KDALEervaELQDQCSRSQAELRRLRDQ 633
Cdd:PRK04863 371 V---EEADEQQEENEARAEAAEeevdelKSQLADYqqaLDVQQTRaiqyqqaVQALE----RAKQLCGLPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 634 LSGLTEECKVVKNnakcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQvqckcHQEDKAQLQSLL--AETQRHLGD- 710
Cdd:PRK04863 444 LEEFQAKEQEATE----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS-----RSEAWDVARELLrrLREQRHLAEq 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 711 ---VQLKLGEAECRLDQETQLRR-------------KEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEK 774
Cdd:PRK04863 515 lqqLRMRLSELEQRLRQQQRAERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116007118 775 IRLLEQQ----------LEKLTKQQMQQSETPQSVLSTVQremEMATRRSKLSFSRQDSRLSVKTLIESIEN 836
Cdd:PRK04863 595 IQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQ---QLLERERELTVERDELAARKQALDEEIER 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
397-792 |
2.90e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 397 QMEETHYSTNEELQATLQELADLQTQLTDTQ---TENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQEllLRDTKQPA 473
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 474 PEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ---LDAANAERRQGEA 550
Cdd:TIGR00618 290 RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 551 QFSQAMEE---ISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEvldvarkekDALEERVAELQDQCSRSQAEL 627
Cdd:TIGR00618 370 ISCQQHTLtqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 628 RRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD--KIAGEWQALEERVAELQVQCKC-------HQEDKAQLQ 698
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKKAVVLARLLELQEEPCplcgsciHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 699 SLLAETQRHLG---DVQLKLGEAECRLDQETQLRRKEA----EEWQQFQADLLMTVRVANDFKTEA--LSAREQLVLD-- 767
Cdd:TIGR00618 521 DNPGPLTRRMQrgeQTYAQLETSEEDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIpnLQNITVRLQDlt 600
|
410 420
....*....|....*....|....*
gi 116007118 768 NKTQKEKIRLLEQQLEKLTKQQMQQ 792
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
472-613 |
4.85e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 472 PAPEVSASEREQklldlikTSQEEREAVLLKQ-EELGAELAEMKQareagqlELQRQRERIALLDSQLDAANAERRQGEa 550
Cdd:COG2433 397 AEREKEHEEREL-------TEEEEEIRRLEEQvERLEAEVEELEA-------ELEEKDERIERLERELSEARSEERREI- 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007118 551 qfsQAMEEISQRAIEISRLSTLLENARSKIEELEADLSR----------GDKTDLSEVLDVARKEKDALEERV 613
Cdd:COG2433 462 ---RKDREISRLDREIERLERELEEERERIEELKRKLERlkelwklehsGELVPVKVVEKFTKEAIRRLEEEY 531
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1010-1071 |
6.34e-05 |
|
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: 43.14 E-value: 6.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 1010 ITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAESV-GIGTTLNINDMC 1071
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIPMVLSPEDLS 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
260-684 |
6.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 260 KMQELHKQMERFRSEQMQLET---RITELLPYQSEVAKLKGDLVKMqsLQEKSQMEIGNLKYEN------------ESLR 324
Cdd:PRK03918 260 KIRELEERIEELKKEIEELEEkvkELKELKEKAEEYIKLSEFYEEY--LDELREIEKRLSRLEEeingieerikelEEKE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 325 NRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGtpCLTPDWdkqsssseisvacLQDKIIQMEETHYS 404
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT--GLTPEK-------------LEKELEELEKAKEE 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 405 TNEELQATLQELADLQTQLTDTQTENERLAEEKDVLfqSLCRQ--------------TEKLNESRTQISTLQELL--LRD 468
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKC--PVCGRelteehrkelleeyTAELKRIEKELKEIEEKErkLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 469 TKQPAPEVSASERE----QKLLDLIKTSQEEREAVLLKQEELGAELAEmKQAREAGQLE-----LQRQRERIALLDSQLD 539
Cdd:PRK03918 481 ELRELEKVLKKESEliklKELAEQLKELEEKLKKYNLEELEKKAEEYE-KLKEKLIKLKgeiksLKKELEKLEELKKKLA 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 540 AANAERRQGEAQFSQAMEEISQRAIEI-----SRLSTL---------LENARSKIEELEADLSRgDKTDLSEVLDVARKE 605
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESveeleERLKELepfyneyleLKDAEKELEREEKELKK-LEEELDKAFEELAET 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 606 KDALEERVAELQD-QCSRSQAELRRLRDQLSGLTEEckvvknnakcaVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 684
Cdd:PRK03918 639 EKRLEELRKELEElEKKYSEEEYEELREEYLELSRE-----------LAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
477-835 |
6.65e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 477 SASEREQKLldliKTSQEEREAVLLKQEELGAELA---EMKQAREAGQLELQRQ------RERIAL-LDSQLDAANAERR 546
Cdd:pfam17380 283 AVSERQQQE----KFEKMEQERLRQEKEEKAREVErrrKLEEAEKARQAEMDRQaaiyaeQERMAMeRERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 547 QGEaqfsqaMEEISQR--AIEISRLSTLlenarskiEELEADLSRGDKTDLSEvLDVARKEKDALEERVAELQDQcsrsQ 624
Cdd:pfam17380 359 KRE------LERIRQEeiAMEISRMREL--------ERLQMERQQKNERVRQE-LEAARKVKILEEERQRKIQQQ----K 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 625 AELRRLRDQLSglteeckvvknnakcavshlEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAET 704
Cdd:pfam17380 420 VEMEQIRAEQE--------------------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 705 QRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQAdllmTVRVANDFKTEALSAREQlvlDNKTQKEKIRLLEQQLEK 784
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIYEEER---RREAEEERRKQQEMEERR 552
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 116007118 785 LTKQQMQQSETPQSVLSTVQREMEMAtrRSKLSFSRQDSRLSVKTLIESIE 835
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMEREREMM--RQIVESEKARAEYEATTPITTIK 601
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
407-681 |
9.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQ--SLCRQTEKLN-ESRTQISTLQELLLRDTKQPAPEVSASEREQ 483
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQlkELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 484 KLLDLIKtsqEEREAVLLKQEELGAELAEM-KQAREAGQLELQRQRERIALLDS------QLDAANAERRQGEAQFSQAM 556
Cdd:PRK03918 549 EKLEELK---KKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 557 EEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSG 636
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 116007118 637 LTEECKVVKNnakcavshLEYRLEQLQRDKDKIAgEWQALEERVA 681
Cdd:PRK03918 706 REKAKKELEK--------LEKALERVEELREKVK-KYKALLKERA 741
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
415-735 |
1.46e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 415 ELADLQTQLTDTQTENERLAeekdvlfQSLCRQTEKLnesrtqistlQELLLRDTKQPAPEVSASEREQKLLDLIKTSQE 494
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELR-------AQLAKKEEEL----------QAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 495 E-------REAVLLKQEELGAELAEMKQARE------AGQLELQRQRER-IALLDSQLDAanaERRQGEAQF-------S 553
Cdd:pfam01576 279 DleseraaRNKAEKQRRDLGEELEALKTELEdtldttAAQQELRSKREQeVTELKKALEE---ETRSHEAQLqemrqkhT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 554 QAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDaLEERVAELQDQCSRSQAELRRLRDQ 633
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK-LEGQLQELQARLSESERQRAELAEK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 634 LSGLTEECKVVKNNAKCA----------VSHLEYRL----EQLQ---RDKDKIAGEWQALEERVAELQVQCKCHQEDKAQ 696
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAegkniklskdVSSLESQLqdtqELLQeetRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRN 514
|
330 340 350
....*....|....*....|....*....|....*....
gi 116007118 697 LQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEE 735
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
488-835 |
1.49e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 488 LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEIS 567
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 568 RLSTLLENARSKIEELEAdlsrgDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNN 647
Cdd:COG4372 105 SLQEEAEELQEELEELQK-----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 648 AKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQ 727
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 728 LRRKEAEEW---QQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQ 804
Cdd:COG4372 260 IEELELAILvekDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
330 340 350
....*....|....*....|....*....|.
gi 116007118 805 REMEMATRRSKLSFSRQDSRLSVKTLIESIE 835
Cdd:COG4372 340 ADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
497-639 |
2.31e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 497 EAVL--LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLdaanaerrqgeaqfsQAMEEisqraiEISRLSTLLE 574
Cdd:COG2433 379 EEALeeLIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV---------------ERLEA------EVEELEAELE 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116007118 575 NARSKIEELEADLSRGDKTDLSEVLdvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTE 639
Cdd:COG2433 438 EKDERIERLERELSEARSEERREIR--KDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-616 |
2.72e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 402 HYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLfQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASER 481
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL-AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 482 EQKLLDliktsQEEREAVLLKQEELGAELAEMKQAREAGQLElQRQRERialLDSQLDAANAERRQGEAQFSQAMEEISQ 561
Cdd:COG4913 728 ELDELQ-----DRLEAAEDLARLELRALLEERFAAALGDAVE-RELREN---LEERIDALRARLNRAEEELERAMRAFNR 798
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 562 R-------------AIE--ISRLSTL----LENARSKIEELEADLSRGDKTDLSEVLDVARKEkdaLEERVAEL 616
Cdd:COG4913 799 EwpaetadldadleSLPeyLALLDRLeedgLPEYEERFKELLNENSIEFVADLLSKLRRAIRE---IKERIDPL 869
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
994-1069 |
2.74e-04 |
|
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: 41.52 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 994 LLKWC--QNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIP----YDQLTPANKRRNFSLAFAAAESVGIGTTLNI 1067
Cdd:cd21218 15 LLRWVnyHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
|
..
gi 116007118 1068 ND 1069
Cdd:cd21218 95 ED 96
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
420-805 |
2.78e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 420 QTQLTDTQTENERLAEEKDVLFQSLCRQtEKLNESRTqistlqelllrdTKQPAPEVSAS-EREQKLLDLiktsQEEREA 498
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERR-RKLEEAEK------------ARQAEMDRQAAiYAEQERMAM----EREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 499 VLLKQEELGAELAEMKQAREAGQLELQRQRERIALldsqldaanaERRQGEAQFSQAMEeisqraieisrlstllenARS 578
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELERLQM----------ERQQKNERVRQELE------------------AAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 579 KIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRsqaELRRLRDQLSGLTEECKVVknnakcavshleyR 658
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERL-------------R 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 659 LEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAE------TQRHLGDVQLKLGEAECRLDQETQLRR-K 731
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKqQ 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116007118 732 EAEEWQQFQADLLMTvrvandfkTEALSAREQLvldnktQKEKiRLLEQQLEKLTKQQMQQSETPQSVLSTVQR 805
Cdd:pfam17380 547 EMEERRRIQEQMRKA--------TEERSRLEAM------ERER-EMMRQIVESEKARAEYEATTPITTIKPIYR 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
493-845 |
2.88e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 493 QEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 572
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 573 LENARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvknnakcaV 652
Cdd:COG4372 89 LQAAQAELAQAQEELES------------LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE-----------I 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 653 SHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKE 732
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 733 AEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATR 812
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
330 340 350
....*....|....*....|....*....|...
gi 116007118 813 RSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 845
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
503-794 |
2.90e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 503 QEELGAELAEMKQAreagqleLQRQRERIALLDSQLDAANAerrqgeaqfsqameEISQRAIEISRLSTLLENARSkiee 582
Cdd:pfam12128 599 EEELRERLDKAEEA-------LQSAREKQAAAEEQLVQANG--------------ELEKASREETFARTALKNARL---- 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 583 leadlsrgdktDLSEVLDVARKEKDALEERVAELQDQCSRS----QAELRRLRDQLSGLTEECKVVKNNAKCAvsHLEYR 658
Cdd:pfam12128 654 -----------DLRRLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQAWLEEQKEQKREARTE--KQAYW 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 659 LEQLQRDKDKIAGEWQALEERVAELQVQCK-CHQEDKAQLQSL------LAETQRHLGDVQLKLGEAECRLDQETQLRRK 731
Cdd:pfam12128 721 QVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLgvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFDW 800
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007118 732 EAEEWQQFQADLLMTVRvanDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 794
Cdd:pfam12128 801 YQETWLQRRPRLATQLS---NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-840 |
4.08e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 611 ERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCH 690
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 691 QEDKAQLQSLLAETQRHLGDVQLKLGEaecrLDQETQLRRKEAEEWQQFQADLLMTVRVANDfktealsAREQLVLDNKT 770
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQILRE-------RLANLERQLEE 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 771 QKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQ 840
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
408-845 |
4.24e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 408 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTqistlqelllrdtkqpaPEVSASEREQKLLD 487
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLES-----------------GDDSGTPGGKKYLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 488 L---IKTSQEE-------REAVLLKQEELGAELAEMKQAREagqlELQRQRERIALLDSQLDaanaerrqgeaqfsqAME 557
Cdd:pfam05622 64 LqkqLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNE----ELTSLAEEAQALKDEMD---------------ILR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 558 EISQRAieiSRLSTLLENARSKIEELeADLSRGDKTdLSEVLDVARKEKDALEE---RVAELQDQCSRSQAELRRLRDQL 634
Cdd:pfam05622 125 ESSDKV---KKLEATVETYKKKLEDL-GDLRRQVKL-LEERNAEYMQRTLQLEEelkKANALRGQLETYKRQVQELHGKL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 635 SglTEECKVVKnnAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELqvqcKCHQEDKAQLQSLLAETQRHLGDVQ-- 712
Cdd:pfam05622 200 S--EESKKADK--LEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL----RCAQLQQAELSQADALLSPSSDPGDnl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 713 ------LKLGEAECRLDQETQ-LRRKEAEEWQQFQADLLMTVRVANdfktealSAREQLVLDNKTQKEKIRLLEQQLEKL 785
Cdd:pfam05622 272 aaeimpAEIREKLIRLQHENKmLRLGQEGSYRERLTELQQLLEDAN-------RRKNELETQNRLANQRILELQQQVEEL 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116007118 786 TK-QQMQQSETPQSVLSTVQREMEMATRRsKLSFSRQDSRLSVKTLIESIENNKAQgKADE 845
Cdd:pfam05622 345 QKaLQEQGSKAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQIEELEPKQDSNLAQ-KIDE 403
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
459-662 |
4.24e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 459 STLQELLlrDTKQPAPEVSASEreQKLLDLIKTSQEEREavLLKQEELGAELAEMKQAREagqlelqRQRERIALLDSQL 538
Cdd:pfam09787 4 SAKQELA--DYKQKAARILQSK--EKLIASLKEGSGVEG--LDSSTALTLELEELRQERD-------LLREEIQKLRGQI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 539 DAANAERRQGEAQFSQAMEEISQraiEISRLSTLLENARSKIEELEADLSRgdktdLSEVLDVARKEkdaLEERVAELQD 618
Cdd:pfam09787 71 QQLRTELQELEAQQQEEAESSRE---QLQELEEQLATERSARREAEAELER-----LQEELRYLEEE---LRRSKATLQS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116007118 619 QCSRSQAELRRLRDQLSglteeckvVKNNAKCAVSHLEYRLEQL 662
Cdd:pfam09787 140 RIKDREAEIEKLRNQLT--------SKSQSSSSQSELENRLHQL 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
480-634 |
4.26e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 480 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERrqgeaQFSQAMEEI 559
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116007118 560 SQRAIEISRLSTLLENARSKIEELEADLSRgDKTDLSEVLDVARKEKDALEERVAELQDQcsrsQAELRRLRDQL 634
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAE-LEAELAELEAELEEKKAELDEELAELEAE----LEELEAEREEL 168
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
262-578 |
4.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 262 QELHKQMERFRSEQMQLETRITELL-----PYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLS 336
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLeqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 337 DAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTP-------------------DWDKQSSSSEISVACLQDKIIQ 397
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflllareKASLGKEAEELQALPALEELEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 398 ME-------------------ETHYSTNEELQATLQELADLQTQLT--DTQTENERLAEEKDV----LFQSLCRQTEKLN 452
Cdd:COG4717 319 EEleellaalglppdlspeelLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVedeeELRAALEQAEEYQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 453 ESRTQISTLQELL---LRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGqlELQRQRE 529
Cdd:COG4717 399 ELKEELEELEEQLeelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 116007118 530 RIALLDSQLDAAnAERRQGEAQFSQAMEEISQRAIEiSRLSTLLENARS 578
Cdd:COG4717 477 ELEELKAELREL-AEEWAALKLALELLEEAREEYRE-ERLPPVLERASE 523
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-845 |
5.96e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 427 QTENERLAEEKdvlfqslcRQTEKLNESRTQISTLQELLLR--DTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQE 504
Cdd:PTZ00121 1291 KADEAKKAEEK--------KKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 505 ELGAELAEMKQAREAGQL--------------ELQRQRERIALLDSQLDAANAERRQGE-----AQFSQAMEEISQRAIE 565
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKAdaakkkaeekkkadEAKKKAEEDKKKADELKKAAAAKKKADeakkkAEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 566 ISRLSTL---------LENARSKIEEL--------------EADLSRGDKTDLSEVLDVARK----EKDALEERVAELQD 618
Cdd:PTZ00121 1443 AKKADEAkkkaeeakkAEEAKKKAEEAkkadeakkkaeeakKADEAKKKAEEAKKKADEAKKaaeaKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 619 QCSRS-QAELRRLRDQLSGLTEECKV--VKNNAKCAVSHLEYRLEQLQR-DKDKIAGEWQALEERVAE----LQVQCKCH 690
Cdd:PTZ00121 1523 KADEAkKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEeariEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 691 QEDKAQLQSLLAETQRHLGDVQLKLGEAECRldQETQLRRKEAEEWQqfQADLLMTVRVANDFKTEALSAREQlvlDNKT 770
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAE---EDKK 1675
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116007118 771 QKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAqgKADE 845
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK--KAEE 1748
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
391-631 |
6.51e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 391 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELL--LRD 468
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELdeLRK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 469 TKQPAPEVSASERE-----QKLLDLIKTS----QEEREaVLLKQEELGAELAEMKQAREAgQLELQRQRERIALLDSQLD 539
Cdd:COG1340 100 ELAELNKAGGSIDKlrkeiERLEWRQQTEvlspEEEKE-LVEKIKELEKELEKAKKALEK-NEKLKELRAELKELRKEAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 540 AANaerrqgeaqfsqamEEISQRAIEISRLSTLLENARSKIEEL--EADLSRGDKTDLSEVLDVARKEKDALEERVAELQ 617
Cdd:COG1340 178 EIH--------------KKIKELAEEAQELHEEMIELYKEADELrkEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250
....*....|....
gi 116007118 618 DQCSRSQAELRRLR 631
Cdd:COG1340 244 KELKKLRKKQRALK 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
406-735 |
7.91e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 406 NEELQATLQELADLQTQLTDTQTENER---LAEEK-DVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASER 481
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRariELEKKaSALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 482 EQKLLDLIKTSQEEREAVLLKQEE----LGAELAEMKQAREAGQLELQRQRERIALLDSQLDaanaerrqgeaQFSQAME 557
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREviscLKNELSELRRQIQRAELELQSTNSELEELQERLD-----------LLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 558 EISQRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVLDVARKEkdalEERVAELqdqcsrsQAELRRLRD---QL 634
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS--QEQDSEIVKNSKSE----LARIPEL-------EKELERLREhnkHL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 635 SGLTEECKVVKNNakcaVSHLEYRLEQ----------LQRDKDKIAGEWQ-----------------ALEERVAELQVQC 687
Cdd:pfam05557 217 NENIENKLLLKEE----VEDLKRKLEReekyreeaatLELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQRE 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 116007118 688 KCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLdQETQLRRKEAEE 735
Cdd:pfam05557 293 IVLKEENSSLTSSARQLEKARRELEQELAQYLKKI-EDLNKKLKRHKA 339
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
406-591 |
8.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 406 NEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEV----SASER 481
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeleSLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 482 EQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAE-RRQGEAQFSQAMEEIS 560
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQElQALSEAEAEQALDELL 189
|
170 180 190
....*....|....*....|....*....|.
gi 116007118 561 QRAIEISRLSTLLENARSKIEELEADLSRGD 591
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
407-562 |
8.18e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDvlfqslcRQTEKLNESRTQISTLQELL--LRDTKqpapEVSASEREQK 484
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQLgnVRNNK----EYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116007118 485 LLDLIKTSQEEREAVLLKQ-EELGAELAEMKQAREAGQLELQRQRERialLDSQLDAANAERRQGEAQFSQAMEEISQR 562
Cdd:COG1579 100 SLKRRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
408-588 |
1.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 408 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLqELLLRDTKQpapevsASEREQKLLD 487
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEA------RIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 488 LIKTSQEereavllkQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQraiEIS 567
Cdd:COG1579 84 NVRNNKE--------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELA 152
|
170 180
....*....|....*....|.
gi 116007118 568 RLSTLLENARSKIEELEADLS 588
Cdd:COG1579 153 ELEAELEELEAEREELAAKIP 173
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
487-795 |
1.10e-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: 43.02 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 487 DLIKTSQEEREAVLLKQEELGAELAEMKQAreagQLELQRQRERIALLDSQLDA------ANAERRQgeAQFSQAMEEIS 560
Cdd:COG5185 205 NSIKESETGNLGSESTLLEKAKEIINIEEA----LKGFQDPESELEDLAQTSDKleklveQNTDLRL--EKLGENAESSK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 561 QRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEE 640
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 641 CKVVKNNaKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQC-----------KCHQEDKAQLQSLLAETQRHLG 709
Cdd:COG5185 359 IKEEIEN-IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAqeilatledtlKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 710 DVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLM-TVRVANDFKTEALSAREQLVLDNKTQKEKIRL-LEQQLEKLTK 787
Cdd:COG5185 438 EVSKLLNELISELNKVMREADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAkLERQLEGVRS 517
|
....*...
gi 116007118 788 QQMQQSET 795
Cdd:COG5185 518 KLDQVAES 525
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
465-735 |
1.13e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 465 LLRDTKQPAPEVSASEREQKLLDL---IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAA 541
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLYEKEIEDLrrqLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 542 NAERRQGEAQFSQAMEEIS-QRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVL--------DVARKEKDALEE- 611
Cdd:pfam00038 116 TLARVDLEAKIESLKEELAfLKKNHEEEVRELQAQVSDTQVNVEMDAAR--KLDLTSALaeiraqyeEIAAKNREEAEEw 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 612 ---RVAELQDQCSRSQAELRrlrdqlsglteeckvvknNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ---- 684
Cdd:pfam00038 194 yqsKLEELQQAAARNGDALR------------------SAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEerye 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 116007118 685 VQCKCHQ----EDKAQLQSLLAETQRHLGDVQLKLgEAECRLDQETQLRRK--EAEE 735
Cdd:pfam00038 256 LQLADYQelisELEAELQETRQEMARQLREYQELL-NVKLALDIEIATYRKllEGEE 311
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
477-788 |
1.21e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 477 SASEREQKLLDLIKTSQEEREAVLL---------KQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQ 547
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEfakkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 548 GEAQFSQAMEEISQRaieiSRLSTLLENARSKIEELEADLSRGDKTdlSEVLDVARKEKDALE--ERVAELQDQCSRSQA 625
Cdd:TIGR00618 241 SHAYLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEET--QERINRARKAAPLAAhiKAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 626 ELR-RLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQ-----------ALEERVAELQvQCKCHQED 693
Cdd:TIGR00618 315 ELQsKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsireiscqqhTLTQHIHTLQ-QQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 694 KAQLQSLLAETQRHLGDVQLKLGEAECRLDQetQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTqKE 773
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQG--QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KE 470
|
330
....*....|....*
gi 116007118 774 KIRLLeQQLEKLTKQ 788
Cdd:TIGR00618 471 REQQL-QTKEQIHLQ 484
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
478-622 |
1.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 478 ASEREQKLLDLIKTSQEEREAVLLK-QEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAM 556
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEERE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 557 EEISQRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVLDVARKEK----DALEERVAELQDQCSR 622
Cdd:PRK12705 112 KALSARELELEELEKQLDNELYRVAGLTPEQAR--KLLLKLLDAELEEEKaqrvKKIEEEADLEAERKAQ 179
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
509-719 |
1.59e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 509 ELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLS 588
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 589 R-GDKTDLSEVLDVARKEKDALeervaelqdqcSRSQAeLRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD 667
Cdd:COG3883 97 RsGGSVSYLDVLLGSESFSDFL-----------DRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 116007118 668 KIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAE 719
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
260-845 |
1.92e-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: 42.34 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 260 KMQELHKQMERFRSEQMQ-LETRITELLPY-QSEVAKLKGDLVKMQSlqeksqmEIGNLKYENESLRNRLRDVVNSPLSD 337
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQgTDEQLNDLYHNhQRTVREKERELVDCQR-------ELEKLNKERRLLNQEKTELLVEQGRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 338 AEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPcltpdwdkqssSSEISVACLQDKIIQMEEthystnEELQATLQELA 417
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGP-----------FSERQIKNFHTLVIERQE------DEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 418 DLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQistlqellLRDTKQPAPEVSASEREqklldliktsqeere 497
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE--------LKFVIKELQQLEGSSDR--------------- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 498 aVLLKQEELGAELAEMKQAREAGQLELQRQRErIALLDSQLDAANAERRQgeaqfSQAMEEISQRAIEISRLSTLLENAR 577
Cdd:TIGR00606 473 -ILELDQELRKAERELSKAEKNSLTETLKKEV-KSLQNEKADLDRKLRKL-----DQEMEQLNHHTTTRTQMEMLTKDKM 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 578 SKIEELEADLSRGD------------KTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 645
Cdd:TIGR00606 546 DKDEQIRKIKSRHSdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 646 NN--AKCAVSHLEYRLEQLQRDKDKIAGEW-----------QALEERVAELQVQCK-CHQEDKAQlqsllAETQRHLGDV 711
Cdd:TIGR00606 626 DKlfDVCGSQDEESDLERLKEEIEKSSKQRamlagatavysQFITQLTDENQSCCPvCQRVFQTE-----AELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 712 QLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQL-VLDNKTQKEKIRLLEQqlEKLTKQQM 790
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLKNDIEEQ--ETLLGTIM 778
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 116007118 791 QQSETPQSVLS--TVQREMEMATRRSKLSFSRQDSRLSVKTLIESIE--NNKAQGKADE 845
Cdd:TIGR00606 779 PEEESAKVCLTdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHE 837
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
489-649 |
2.02e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 489 IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAanAERRQGEAQfsQAMEEISQRAIEISR 568
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER--TEERLAEAL--EKLEEAEKAADESER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 569 LSTLLENARSKIEELEADLsrgdKTDLSEVLDVARKEKDALEE---RVAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 645
Cdd:pfam00261 79 GRKVLENRALKDEEKMEIL----EAQLKEAKEIAEEADRKYEEvarKLVVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
....
gi 116007118 646 NNAK 649
Cdd:pfam00261 155 NNLK 158
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
439-636 |
2.23e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 439 VLFQSLCRQTEKLNESRTQISTLQELLlrdtkqpapevsASEREQK--LLDLIKTSQEEREAVLLKQEELGAELAEMKQA 516
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAELADLL------------SLERQGNqdLQDSVANLRASLSAAEAERSRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 517 REAGQlelqrqrERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLS 596
Cdd:PRK09039 111 GAAAE-------GRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIA-----DLG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116007118 597 EVLDVarkekdALEERVAELQdqcsRSQAE-LRRLRDQLSG 636
Cdd:PRK09039 179 RRLNV------ALAQRVQELN----RYRSEfFGRLREILGD 209
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-548 |
2.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 379 KQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEE----------------KDVLF- 441
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyrlgrqppLALLLs 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 442 ------------------QSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQ 503
Cdd:COG4942 128 pedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116007118 504 E-ELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 548
Cdd:COG4942 208 LaELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
407-635 |
2.73e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.60 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 407 EELQATLQELADLQTQLTDTQTENERLAEEKDVLfqslcrqteklnesRTQISTLQELllrdtkQPAP-EVSASEREQKL 485
Cdd:COG0497 158 EEYREAYRAWRALKKELEELRADEAERARELDLL--------------RFQLEELEAA------ALQPgEEEELEEERRR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 486 L----DLIKTSQEEREAvlLKQEELGAeLAEMKQAReagqlelqRQRERIALLDSQLDAAnaerrqgeaqfSQAMEEIsq 561
Cdd:COG0497 218 LsnaeKLREALQEALEA--LSGGEGGA-LDLLGQAL--------RALERLAEYDPSLAEL-----------AERLESA-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 562 rAIEISRLSTLLENARSKIE----ELEA---------DLSRGDKTDLSEVLDVARK------EKDALEERVAELQDQCSR 622
Cdd:COG0497 274 -LIELEEAASELRRYLDSLEfdpeRLEEveerlallrRLARKYGVTVEELLAYAEElraelaELENSDERLEELEAELAE 352
|
250
....*....|...
gi 116007118 623 SQAELRRLRDQLS 635
Cdd:COG0497 353 AEAELLEAAEKLS 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
600-812 |
2.87e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 600 DVARKEKDALEERVAELQDQCSRSQAELRRLRDQ--LSGLTEECKVVKNNakcaVSHLEYRLEQLQRDKDKIAGEWQALE 677
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQ----LSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 678 ERVAELQVQCKCHQEDKA--QLQSLLAETQRHLGDVQLKLGEAECRLdqeTQLRRKEAEEWQQFQAdllMTVRVANDFKT 755
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDV---IALRAQIAALRAQLQQ---EAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116007118 756 EALSAREQLvldnktqkekiRLLEQQLEKLTKQQMQQSETpQSVLSTVQREMEMATR 812
Cdd:COG3206 321 ELEALQARE-----------ASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARE 365
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
404-790 |
3.05e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 404 STNEELQATLQELADL-QTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQIStlqelllrdtkqpapevsasere 482
Cdd:COG5185 250 QTSDKLEKLVEQNTDLrLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID----------------------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 483 qklldlIKTSQEEREAVlLKQEELGAELAEMKQAREAGqleLQRQRERIALLDSQLDAANAERRQGEAQFSqAMEEISQR 562
Cdd:COG5185 307 ------IKKATESLEEQ-LAAAEAEQELEESKRETETG---IQNLTAEIEQGQESLTENLEAIKEEIENIV-GEVELSKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 563 AIEISRLSTLLENARSKIEELEADLSRGDKtdlsEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEC- 641
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQ----EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELn 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 642 KVVKNNAKCAVSHLEYRLEQLQRD----KDKIAGEWQALEERVAELqvqckchqedKAQLQSLLAETQRHLGDVQLKLGE 717
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSvrskKEDLNEELTQIESRVSTL----------KATLEKLRAKLERQLEGVRSKLDQ 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007118 718 AECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQM 790
Cdd:COG5185 522 VAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQA 594
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
559-771 |
4.61e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 559 ISQRAIEISRLSTLLENARSKIEELEadlsrgDKTDLSEVLDVARKEKdALEErvaELQDQCSRSQAELRRLRDQLSGLT 638
Cdd:PRK10361 11 IALVGVAIGWLFASYQHAQQKAEQLA------EREEMVAELSAAKQQI-TQSE---HWRAECELLNNEVRSLQSINTSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 639 EECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAElQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEA 718
Cdd:PRK10361 81 ADLREVTTRMEAAQQHADDKIRQMINSEQRLSEQFENLANRIFE-HSNRRVDEQNRQSLNSLLSPLREQLDGFRRQVQDS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 116007118 719 ecrLDQETQLRRKEAEEWQQFQadllmtvRVANDFKTEALSAREQLVLDNKTQ 771
Cdd:PRK10361 160 ---FGKEAQERHTLAHEIRNLQ-------QLNAQMAQEAINLTRALKGDNKTQ 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
475-774 |
6.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 475 EVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQfsQ 554
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK--K 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 555 AMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELqdqcSRSQAELRRLRDQL 634
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE----AKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 635 SGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERvAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLK 714
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116007118 715 LGEAECRLDQ--ETQLRRKEAEEWQQFQADllmtVRVANDFKTEALSAREQLVLDNKTQKEK 774
Cdd:PTZ00121 1400 AEEDKKKADElkKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADEAKKKAEEAK 1457
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
578-683 |
6.11e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 578 SKIEELEADLsrgdkTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKvvknNAKCAVSHLEY 657
Cdd:COG4026 128 PEYNELREEL-----LELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFD----NIKSEYSDLKS 198
|
90 100
....*....|....*....|....*.
gi 116007118 658 RLEQLqrdKDKIAGEWQALEERVAEL 683
Cdd:COG4026 199 RFEEL---LKKRLLEVFSLEELWKEL 221
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
476-787 |
6.33e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 476 VSASEREQKLLDLIKTSQEEREAvLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERrqgeAQFSQA 555
Cdd:pfam15905 49 TPATARKVKSLELKKKSQKNLKE-SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREK----TSLSAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 556 MEEISQRAIEISRLSTLLenarskieeleadlsrgdKTDLSEvlDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLS 635
Cdd:pfam15905 124 VASLEKQLLELTRVNELL------------------KAKFSE--DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGME 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 636 GLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQV---QCKCHQEDKAQLQSLLAETQRHLGDVQ 712
Cdd:pfam15905 184 GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCvseQVEKYKLDIAQLEELLKEKNDEIESLK 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116007118 713 LKLGEAECRLDQETQLRRKEAEEWQQFQADLLmtvrvandfkTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTK 787
Cdd:pfam15905 264 QSLEEKEQELSKQIKDLNEKCKLLESEKEELL----------REYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
432-635 |
6.89e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 432 RLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEE--REAVLLKQEE---- 505
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekKKAEELKKAEeenk 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 506 -LGAELA-----EMKQAREAGQLELQRQRERIALLDSQLDAANAER-RQGEAQFSQAMEEISQ----RAIEISRLSTLLE 574
Cdd:PTZ00121 1661 iKAAEEAkkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKaeeeNKIKAEEAKKEAE 1740
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116007118 575 NARSKIEELEADLSRGDK-----TDLSEVLDVARKEKDALEERVAELQDQCSRSQAElRRLRDQLS 635
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKiahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIFD 1805
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
570-845 |
8.28e-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: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 570 STLLENARSKIEELEADLSRGDKT-DLSEVLDVARKEKDALE--------------ERVAELQDQCSRSQAELRRLRDQL 634
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPEsELEDLAQTSDKLEKLVEqntdlrleklgenaESSKRLNENANNLIKQFENTKEKI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 635 SGLTEECKVVKnnakcavsHLEYRLEQLQRdkdkiAGEWQALEERVAELQvqckchqEDKAQLQSLLAETQRHLGDVQLK 714
Cdd:COG5185 299 AEYTKSIDIKK--------ATESLEEQLAA-----AEAEQELEESKRETE-------TGIQNLTAEIEQGQESLTENLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 715 LGEAECRLDQETQLRRKEAEewqqfqadllmtvrvANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 794
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEE---------------LDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIE 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 116007118 795 TPQSVLSTVQREMEMAtrrSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 845
Cdd:COG5185 424 ELQRQIEQATSSNEEV---SKLLNELISELNKVMREADEESQSRLEEAYDE 471
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
566-683 |
8.31e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 566 ISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGL-TEECKVV 644
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREI 461
|
90 100 110
....*....|....*....|....*....|....*....
gi 116007118 645 KNNAKcaVSHLEYRLEQLQRDKDKIAGEWQALEERVAEL 683
Cdd:COG2433 462 RKDRE--ISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
483-676 |
9.19e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.06 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 483 QKLLDLIKTSQEEREAvllKQEELGAELAEMKQAR-EAG---QLELQRQR----ERIA-LLDSQLDAANAERRQGEAQFS 553
Cdd:COG0497 171 KKELEELRADEAERAR---ELDLLRFQLEELEAAAlQPGeeeELEEERRRlsnaEKLReALQEALEALSGGEGGALDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007118 554 QAMEEISQRAI---EISRLSTLLENARSKIEELEADLSR-GDKTDLSEvldvarKEKDALEERVAELQDQCSR---SQAE 626
Cdd:COG0497 248 QALRALERLAEydpSLAELAERLESALIELEEAASELRRyLDSLEFDP------ERLEEVEERLALLRRLARKygvTVEE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 116007118 627 L----RRLRDQLSGLTeeckvvknnakcavsHLEYRLEQLQRDKDKIAGEWQAL 676
Cdd:COG0497 322 LlayaEELRAELAELE---------------NSDERLEELEAELAEAEAELLEA 360
|
|
| |
