|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1006-1117 |
3.87e-81 |
|
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: 259.60 E-value: 3.87e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1006 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGI 1085
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 1720362509 1086 KSTLDINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
1000-1118 |
1.05e-78 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 253.07 E-value: 1.05e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1000 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQA 1079
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1720362509 1080 AESVGIKSTLDINEMARTERPDWQNVMLYVTAIYKYFET 1118
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1006-1117 |
1.52e-72 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 235.69 E-value: 1.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1006 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGI 1085
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 1720362509 1086 KSTLDINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1015-1116 |
2.00e-35 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 130.16 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINE 1093
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 1720362509 1094 MARTE-RPDWQNVMLYVTAIYKYF 1116
Cdd:cd21200 83 MVRMGnRPDWKCVFTYVQSLYRHL 106
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1013-1116 |
5.90e-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: 126.32 E-value: 5.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1013-1114 |
2.37e-31 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 118.94 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKhADCPQLLDV 80
|
90 100
....*....|....*....|...
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYK 1114
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1018-1116 |
1.74e-30 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 115.99 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDINEMART 1097
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 1720362509 1098 ERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1009-1116 |
2.37e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 116.09 E-value: 2.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1009 EYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQ-AAESVGIKS 1087
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 1720362509 1088 TLDINEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1013-1116 |
7.32e-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: 114.43 E-value: 7.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLDA 81
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21194 82 EDVD-VARPDEKSIMTYVASYYHYF 105
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1016-1116 |
1.70e-29 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 113.15 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1016 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINEM 1094
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 1720362509 1095 ARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1015-1114 |
1.54e-28 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 110.94 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVG-IKSTLDINE 1093
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 1720362509 1094 MARTERPDWQNVMLYVTAIYK 1114
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1013-1116 |
3.97e-28 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 109.71 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1013-1116 |
9.60e-28 |
|
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: 108.25 E-value: 9.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21248 82 EDVN-VEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1013-1116 |
1.43e-27 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 107.83 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 1720362509 1092 NEMA-RTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21258 81 EDMMiMGKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1017-1117 |
1.47e-27 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 107.82 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1017 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINEMA 1095
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 1720362509 1096 RTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1013-1116 |
3.39e-27 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 106.87 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLDP 83
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21249 84 EDVA-VPHPDERSIMTYVSLYYHYF 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1013-1117 |
1.20e-26 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 105.25 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDIN 1092
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 1720362509 1093 EMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1014-1116 |
1.77e-26 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 104.54 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1014 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDIN 1092
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 1720362509 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1013-1116 |
3.00e-26 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 103.89 E-value: 3.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESV-GIKSTLDI 1091
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 1720362509 1092 NEMARTER-PDWQNVMLYVTAIYKYF 1116
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1018-1116 |
2.52e-25 |
|
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: 101.47 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDINEMART 1097
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 1720362509 1098 ERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1011-1117 |
2.39e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 98.57 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1011 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTL 1089
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 1720362509 1090 DINEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1014-1116 |
3.75e-24 |
|
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: 98.03 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1014 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDIN 1092
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 1720362509 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1013-1116 |
2.59e-23 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 95.54 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTErPDWQNVMLYVTAIYKYF 1116
Cdd:cd21189 81 EDVDVPE-PDEKSIITYVSSLYDVF 104
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1015-1116 |
3.17e-23 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 95.32 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINE 1093
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 1720362509 1094 MARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1013-1117 |
4.70e-23 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 95.01 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDI 1091
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1018-1114 |
7.64e-23 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 94.03 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAA-ESVGIKSTLDINEMAr 1096
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLDPEDVN- 83
|
90
....*....|....*...
gi 1720362509 1097 TERPDWQNVMLYVTAIYK 1114
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1013-1116 |
3.13e-22 |
|
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: 93.23 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1013-1116 |
6.08e-21 |
|
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: 89.36 E-value: 6.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1013-1116 |
9.82e-21 |
|
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: 89.01 E-value: 9.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1013-1116 |
1.09e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 88.58 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1013-1116 |
1.65e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 88.57 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDi 1091
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1013-1116 |
2.90e-20 |
|
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: 87.83 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1012-1117 |
5.91e-20 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 85.94 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1012 GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 1720362509 1091 INEMArTERPDWQNVMLYVTAIYKYFE 1117
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1013-1116 |
7.16e-20 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 85.86 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDIn 1092
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDA- 82
|
90 100
....*....|....*....|....
gi 1720362509 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1013-1116 |
1.95e-19 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 84.77 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLDP 81
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMArTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21320 82 EDIS-VDHPDEKSIITYVVTYYHYF 105
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1015-1118 |
2.43e-19 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 84.26 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1015 RNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKKRNFTLAFQAAE-SVGIKSTL- 1089
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPKVLi 83
|
90 100 110
....*....|....*....|....*....|..
gi 1720362509 1090 ---DINEmarterPDWQNVMLYVTAIYKYFET 1118
Cdd:pfam00307 84 epeDLVE------GDNKSVLTYLASLFRRFQA 109
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1017-1116 |
4.88e-18 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 80.59 E-value: 4.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1017 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINEMa 1095
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAEDV- 82
|
90 100
....*....|....*....|.
gi 1720362509 1096 RTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1013-1116 |
3.61e-17 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 78.10 E-value: 3.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTLDiN 1092
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 1720362509 1093 EMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1016-1109 |
5.18e-17 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 77.36 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1016 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY----QELNSQDKKRNFTLAFQAAESVGIKSTL-- 1089
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLfe 80
|
90 100
....*....|....*....|..
gi 1720362509 1090 --DINEMarteRPDWQNVMLYV 1109
Cdd:smart00033 81 peDLVEG----PKLILGVIWTL 98
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1013-1116 |
3.37e-16 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 75.35 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQnidITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|....*.
gi 1720362509 1091 INEMARTErPDWQNVMLYVTaiykYF 1116
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLS----YF 98
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1015-1114 |
5.05e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 74.68 E-value: 5.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1015 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY---QELNSQDKKRNFTLAFQAAESVGIKST--L 1089
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 1720362509 1090 DINEMarTERPDWQNVMLYVTAIYK 1114
Cdd:cd00014 81 EPEDL--YEKGNLKKVLGTLWALAL 103
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1018-1114 |
4.28e-15 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 72.27 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKK-RNFTLAFQAAE-SVGIKSTLDINEMA 1095
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLDPEDVA 84
|
90
....*....|....*....
gi 1720362509 1096 rTERPDWQNVMLYVTAIYK 1114
Cdd:cd21233 85 -TAHPDKKSILMYVTSLFQ 102
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1011-1116 |
5.56e-15 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 71.97 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1011 GGSKRnALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTL 1089
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLL 82
|
90 100
....*....|....*....|....*..
gi 1720362509 1090 DiNEMARTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21243 83 D-PEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1013-1118 |
1.63e-14 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 78.06 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQN-IDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKKRNFTLAFQAAE-SVGIKST 1088
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 1720362509 1089 LDINEMARTERPDWQNVMLYVTAIYKYFET 1118
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-824 |
1.84e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 558 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS--DIQDLLESVRLDKEKAETLASSLQEDLAHTR 635
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEieELQKELYALANEISRLEQQKQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 636 NDANRLQDTIAKVE---DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliI 712
Cdd:TIGR02168 316 RQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK-------V 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 713 SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKE 792
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 1720362509 793 LEEIKSRKQEEERGRVynymnAVERDLAALRQ 824
Cdd:TIGR02168 463 LEELREELEEAEQALD-----AAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
500-816 |
2.06e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 500 AENARFEREQLLGVQQH----LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQI 575
Cdd:TIGR02169 700 IENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKA--------QLENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAK 647
Cdd:TIGR02169 780 ALNDLEArlshsripEIQAELSKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 648 VEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRavklhdnLIISDLENTVKKLQD 724
Cdd:TIGR02169 859 LNGKKEELEEELEEleaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-------KRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 725 QkhdmEREIKTLHRRLREESAEW---RQFQADLQ---TAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKS 798
Cdd:TIGR02169 932 E----LSEIEDPKGEDEEIPEEElslEDVQAELQrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
330
....*....|....*...
gi 1720362509 799 RKQEEERGRVYNYMNAVE 816
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEAFE 1025
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-802 |
7.66e-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: 76.63 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 501 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 580
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 581 KAQLENEKQKVAELySIHNSGDKSDIQDLLESVRLDKEKAETL----------ASSLQEDLAHTRNDANRLQDTIAKVED 650
Cdd:TIGR02168 760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALrealdelraeLTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 651 EYRAFQEEAKK----------QIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVK 720
Cdd:TIGR02168 839 RLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 721 KLQDQKHDMER-------EIKTLHRRLREEsaewrqFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLT 790
Cdd:TIGR02168 919 ELREKLAQLELrleglevRIDNLQERLSEE------YSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAI 992
|
330
....*....|..
gi 1720362509 791 KELEEIKSRKQE 802
Cdd:TIGR02168 993 EEYEELKERYDF 1004
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1013-1113 |
7.88e-13 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 65.81 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAE-SVGIKSTLDi 1091
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 1720362509 1092 NEMARTERPDWQNVMLYVTAIY 1113
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1011-1089 |
8.21e-13 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.84 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1011 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTL 1089
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
549-805 |
1.01e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 549 IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdiQDLLESVRLDKEKAETLASSLQ 628
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL------------ELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 629 EDLAHTRNDANRLQDTIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHD 708
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 709 NLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 785
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAeeaLLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260
....*....|....*....|
gi 1720362509 786 NEKLTKELEEIKSRKQEEER 805
Cdd:COG1196 458 EEALLELLAELLEEAALLEA 477
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1018-1114 |
1.28e-12 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 64.98 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDINEMAr 1096
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLDPEDVA- 83
|
90
....*....|....*...
gi 1720362509 1097 TERPDWQNVMLYVTAIYK 1114
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
605-800 |
1.88e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 605 DIQDLLESVRLDKEKAETLA--SSLQEDLAHTRNDANRLQDTIAKVEDeYRAFQ--EEAKKQIEDLNMTLEKLRSELEEK 680
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRL-WFAQRrlELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 681 DTERSDMKETIFELEDEVEQHravklhDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLR-------EESAEWRQFQAD 753
Cdd:COG4913 315 EARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1720362509 754 LQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRK 800
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1016-1111 |
5.41e-12 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 63.09 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1016 NALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTyLPAHIP-YQELNSQDKKRNFTLAFQAAESVGIKSTLDINEM 1094
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 1720362509 1095 ArteRPDWQN--VMLYVTA 1111
Cdd:cd21185 80 A---DPEVEHlgIMAYAAQ 95
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
568-822 |
7.51e-12 |
|
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: 70.10 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 568 ATVASDQIEMNRLKAQLENEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQD 643
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIID--EKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 644 TIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDM--------KETIFELEDEVEQHRAVKLHDNLIISDL 715
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 716 ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKE 792
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720362509 793 LEEIK---------SRKQEEERGRVYNYMNAVERDLAAL 822
Cdd:TIGR02169 401 INELKreldrlqeeLQRLSEELADLNAAIAGIEAKINEL 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
529-804 |
9.00e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 9.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 529 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQD 608
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--------EQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 609 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMK 688
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 689 ETIFELEDEVEQHRAvklhdnliisDLENTVKKLQDQKHDMEREIKTLHRRLREESAEwRQFQADLQTAVVIANDIKSEA 768
Cdd:COG1196 386 EELLEALRAAAELAA----------QLEELEEAEEALLERLERLEEELEELEEALAEL-EEEEEEEEEALEEAAEEEAEL 454
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720362509 769 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1013-1116 |
9.64e-12 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 62.93 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAES-VGIKSTLDI 1091
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLEP 84
|
90 100
....*....|....*....|....*
gi 1720362509 1092 NEMARTErPDWQNVMLYVTAIYKYF 1116
Cdd:cd21244 85 EDVDVVN-PDEKSIMTYVAQFLQYS 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-826 |
4.04e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 202 LRNELRDMRAQLGISEDHCEGEDRSEVKETIIA--HQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGfSL 279
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEaeEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-NE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 280 EQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSApgsvEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTS 359
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 360 SDDALDAPSSSESEGVPSIER---------SRKGSSGNASEVSVACLTERIHQMEENQHSTseELQATLQELADLQQITQ 430
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELqiaslnneiERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 431 ELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhhisyvidedvksgrYMELEQRYMDLAENARF---ER 507
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS---------------LERLQENLEGFSEGVKAllkNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 508 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGA-----LKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKA 582
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 583 QLENEKQKVAELYSIHNSGDKSdIQDLLESVR-----------LDKEKAETLASSLQEDLAH------------------ 633
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKA-LSYLLGGVLvvddldnalelAKKLRPGYRIVTLDGDLVRpggvitggsaktnssile 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 634 TRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNL 710
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 711 IISDLEN---------------------TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI---KS 766
Cdd:TIGR02168 755 ELTELEAeieeleerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLerrIA 834
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362509 767 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGM 826
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEEliEELESELEALLNERASLEEALALLRSEL 896
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1016-1109 |
6.38e-11 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 61.16 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1016 NALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQ--------------------------------E 1063
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDairqpttqtvdraqdeaedfwvaefspstgdsG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720362509 1064 LNSQDK---KRNFTLAFQAAESVGikstlDINEMARTE-----RPDWQNVMLYV 1109
Cdd:cd21224 82 LSSELLaneKRNFKLVQQAVAELG-----GVPALLRASdmsntIPDEKVVILFL 130
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
530-805 |
1.20e-10 |
|
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: 65.86 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 530 EAQEMIGALK-ERSHHMERIIESEQKGKAALAAtLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSihnsgDKSDIQD 608
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-----DLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 609 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIA-----KVEDEYRAFQEEAKKQ----------IEDLNMTLEKL 673
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 674 RSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQAD 753
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1720362509 754 LQTAVVIANDIK---SEAQEEIGDLKRRLHEAQEKNEKlTKELEEIKSRKQEEER 805
Cdd:TIGR02169 912 IEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1017-1116 |
1.38e-10 |
|
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: 59.42 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1017 ALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAA-ESVGIKSTLDINEMA 1095
Cdd:cd21245 7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLEPEDVM 85
|
90 100
....*....|....*....|.
gi 1720362509 1096 rTERPDWQNVMLYVTAIYKYF 1116
Cdd:cd21245 86 -VDSPDEQSIMTYVAQFLEHF 105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
388-798 |
2.79e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 64.66 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 388 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVIL---MESLCQQSDKLEHFGRQI 464
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 465 EYFRSLLDehhiSYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHH 544
Cdd:TIGR04523 200 ELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 545 MERI---IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYS-IHNSGDK-SDIQDLLESVRLDKEK 619
Cdd:TIGR04523 276 LEQNnkkIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNqISQNNKIiSQLNEQISQLKKELTN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 620 AETLASSLQEDLahtrNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVE 699
Cdd:TIGR04523 354 SESENSEKQREL----EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIE 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 700 QHRAVKLHDNLIISDLEN-------TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQ--- 769
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKele 509
|
410 420
....*....|....*....|....*....
gi 1720362509 770 EEIGDLKRRLHEAQEKNEKLTKELEEIKS 798
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
610-805 |
3.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 610 LESVRLDKEKAE---TLASSLQE-DLAHTRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSELEEKDT 682
Cdd:COG1196 202 LEPLERQAEKAEryrELKEELKElEAELLLLKLRELEAELEELEAELEELEaelEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 683 ERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAN 762
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720362509 763 DIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
397-749 |
4.02e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmesLCQQSDKLEHFGRQIEYFRSLLDEHHI 476
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ-------ISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 SYVIDEDVKSGRYMELEQRYMDLAENARfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK 556
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEA-EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 557 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYS--IHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 634
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESelEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 635 RNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLN----MTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLhdnL 710
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSeeysLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL---A 990
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720362509 711 IISDLENTVKKLQD---QKHDMEREIKTLHRRLREESAEWRQ 749
Cdd:TIGR02168 991 AIEEYEELKERYDFltaQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-826 |
5.42e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 399 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFGRQIEYFRSLLDEHhiSY 478
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 479 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 554
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 555 GKAALAATLEEYKatvasdqiEMNRLKAQLENEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 634
Cdd:PRK03918 353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 635 RNDANRLQDTIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERS------- 685
Cdd:PRK03918 418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 686 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDMEREIKTLHR 738
Cdd:PRK03918 498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 739 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 800
Cdd:PRK03918 578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
|
490 500
....*....|....*....|....*.
gi 1720362509 801 QEEERGRVYNYMNAVERDLAALRQGM 826
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAEL 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
413-825 |
5.44e-10 |
|
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: 63.93 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQATLQELADLQQITQELNSENERLGEEKvilmeslcqqsdklehfgRQIEYFRSLLDEHhisyvidEDVksgRYMEL 492
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRER------------------EKAERYQALLKEK-------REY---EGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 493 EQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQkgkAALAATLEEYKATVAS 572
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 573 --DQIEMNRLKAQ-LENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVE 649
Cdd:TIGR02169 306 leRSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 650 DEYRAFQEEakkqiedlnmtLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDM 729
Cdd:TIGR02169 385 DELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 730 EREIKTLHRRLREESAewrqfqadlqtavviandIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVY 809
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAA------------------DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410
....*....|....*.
gi 1720362509 810 NYmnAVERDLAALRQG 825
Cdd:TIGR02169 509 GR--AVEEVLKASIQG 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
397-823 |
7.75e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 7.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDehhi 476
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 syviDEDVKSGrymELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALK--------ERSHHMERI 548
Cdd:PRK02224 402 ----DAPVDLG---NAEDFLEELRE----ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 549 IESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaelysihnsgdksdiqdlLESVRLDKEKAETLASSLQ 628
Cdd:PRK02224 471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------------------IERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 629 EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLnmtlEKLRSELEEKDTERSDMKETIFELEDEVEQHRAvklhd 708
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA----- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 709 nliISDLENTVKKLQDQKHDMErEIKTLHR-RLREESAEWRQFQADLQTAvviandikseaqeeigdlkrRLHEAQEKNE 787
Cdd:PRK02224 601 ---IADAEDEIERLREKREALA-ELNDERReRLAEKRERKRELEAEFDEA--------------------RIEEAREDKE 656
|
410 420 430
....*....|....*....|....*....|....*...
gi 1720362509 788 KLTKELEEI--KSRKQEEERGRVYNYMNAVERDLAALR 823
Cdd:PRK02224 657 RAEEYLEQVeeKLDELREERDDLQAEIGAVENELEELE 694
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
406-757 |
4.35e-09 |
|
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: 60.84 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 406 ENQHSTSEELQATLQELADLQQITQELNSEnerlgeekvilMESLCQQSDKLEHFgrqIEYfRSLLDEHHISYVIDedvk 485
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERY---KEL-KAELRELELALLVL---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 486 sgRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEE 565
Cdd:TIGR02168 233 --RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 566 YKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdiQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTI 645
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDEL------------AEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 646 AKVEDEYRAFQE---EAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENTVKKL 722
Cdd:TIGR02168 375 EELEEQLETLRSkvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEEL 452
|
330 340 350
....*....|....*....|....*....|....*
gi 1720362509 723 QDQKHDMEREIKTLHRRLREESAEWRQFQADLQTA 757
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
670-807 |
7.19e-09 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 59.87 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 670 LEKLRSELEEKDTERSDMKETIFELEDEVEQHRavklhdnliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQ 749
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEE---------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362509 750 FQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:COG2433 453 ARSEERREIRKDREISRL-DREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1013-1110 |
1.78e-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: 53.16 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1013 SKRNALLKWCQKKTEGyqnIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKKRNFTLAFQAAES-VGIKSTLD 1090
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|
gi 1720362509 1091 INEMArTERPDWQNVMLYVT 1110
Cdd:cd21230 78 PEEII-NPNVDEMSVMTYLS 96
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
631-830 |
2.00e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 631 LAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---------------------QIEDLNMTLEKLRSELEEKDTERSDMKE 689
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 690 TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTA---VVIANDIKS 766
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELA 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720362509 767 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGrvynyMNAVERDLAALRQGMGLSR 830
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLN 399
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
413-809 |
2.48e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDEdvKSGRYMEL 492
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE--LPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 493 EQRYMDLAEnARFEREQLLGVQQHLSNTLKMAEQDNKEA--QEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATV 570
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEE-LEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 571 asDQIEMNRLKAQLENEKQKVAELYSIHN-----SGDKSDIQDLLESV----------------RLDKEKAETLASSLQE 629
Cdd:COG4717 230 --EQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIagvlflvlgllallflLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 630 DLAHTRNDANRLQdtIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKEtifeleDEVEQHRAVKLHDN 709
Cdd:COG4717 308 QALPALEELEEEE--LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------EELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 710 LIIS--DLENTVKKLQdQKHDMEREIKTLHRRLREESAEWRQFQADLQtavviandiKSEAQEEIGDLKRRLHEAQEKNE 787
Cdd:COG4717 380 GVEDeeELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELE 449
|
410 420
....*....|....*....|..
gi 1720362509 788 KLTKELEEIKSRKQEEERGRVY 809
Cdd:COG4717 450 ELREELAELEAELEQLEEDGEL 471
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
388-823 |
3.44e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 388 NASEVSVACLTERIHQMEENQhstsEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYF 467
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 468 RSLLDEHhisyvidEDVKSGRYMELEQRYMDlAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERShhmeR 547
Cdd:PRK02224 285 RERLEEL-------EEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA----D 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 548 IIESEQKGKAALAATLEEykatvasdqiEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVR---LDKEKAETLA 624
Cdd:PRK02224 353 DLEERAEELREEAAELES----------ELEEAREAVEDRREEIEEL--------EEEIEELRERFGdapVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 625 SSLQEDLAHTRNDANRLQDTIAKVED---EYRAFQEEAK--------------KQIEDLNMTLEKLRSELEEKDTERSDM 687
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARErveEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 688 KETIFELEDEVEQHRAV-KLHDNL-----IISDLENTVKK-------LQDQKHDMEREIKTLHR----------RLREES 744
Cdd:PRK02224 495 EERLERAEDLVEAEDRIeRLEERRedleeLIAERRETIEEkreraeeLRERAAELEAEAEEKREaaaeaeeeaeEAREEV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 745 AEWRQFQADLQTAVVIANDIKS------EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE--------------EE 804
Cdd:PRK02224 575 AELNSKLAELKERIESLERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKREleaefdearieearED 654
|
490
....*....|....*....
gi 1720362509 805 RGRVYNYMNAVERDLAALR 823
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELR 673
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
650-804 |
4.49e-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: 55.32 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 650 DEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQK--H 727
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVRNNKeyE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362509 728 DMEREIKTLHRRlreesaewrqfQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG1579 93 ALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
400-779 |
1.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 400 RIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmeslcqqsdkLEHFGRQIEyfrslldehhisyv 479
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE--------------LEELELELE-------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 480 idedVKSGRYMELEQRYMDLAENARFEREQLlgvqQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAAL 559
Cdd:COG1196 285 ----EAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 560 AATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN 639
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 640 RLQDTIA--KVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE- 716
Cdd:COG1196 426 LEEALAEleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEg 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720362509 717 -NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVV-IANDIKSEAQEEIGDLKRRL 779
Cdd:COG1196 506 fLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnIVVEDDEVAAAAIEYLKAAK 570
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
360-792 |
1.70e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 360 SDDALDAPSSSESEGVPSIERSRKgssgnASEVSVACLTERIHQMEENQHSTSEEL----QATLQELADLQQITQELNSE 435
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKK-----AEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 436 NERLGEEKVILMESLcqqsDKLEHFGRQIEYFRSLLDEHHISYvidEDVKSgrymELEQRYMDLAENARFEREQllgvqQ 515
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKA---EELKK----AEEENKIKAAEEAKKAEED-----K 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 516 HLSNTLKMAEQDNKEAQEMIGALKERSHHMERI--IESEQKGKAalaatlEEYKATVASDQIEMNRLKAQLENEKQKVAE 593
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkKEAEEKKKA------EELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 594 LYSihNSGDKSDIQDLLE-----SVRLDKEKAETLASSLQEDLAHTRNDANRlqdTIAKVEDEYRAFQEEAKKQIEDLNM 668
Cdd:PTZ00121 1749 AKK--DEEEKKKIAHLKKeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIND 1823
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 669 TLEKLRSELEEKdterSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIktlhrrlrEESAEWR 748
Cdd:PTZ00121 1824 SKEMEDSAIKEV----ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI--------EEADEIE 1891
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1720362509 749 QFQADLQTAVVIANDIKSEAQEEIGD-------LKRRLHEAQEKNEKLTKE 792
Cdd:PTZ00121 1892 KIDKDDIEREIPNNNMAGKNNDIIDDkldkdeyIKRDAEETREEIIKISKK 1942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
344-697 |
2.58e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 344 DNLDSECSEVYQPLTSSDDALDAPSSSESEGVPSIERSRKgssgnasevsvaclteRIHQMEENQHSTSEE-------LQ 416
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK----------------EIEQLEQEEEKLKERleeleedLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 417 ATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL-EHFGRQIEYFRSLLDEHHISYvidedvkSGRYMELEQR 495
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRI-------EARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 496 ymdlaENARFEREQLLgvqqhlsntlkmaEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATV----- 570
Cdd:TIGR02169 821 -----LNRLTLEKEYL-------------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdles 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 571 --ASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRND---------AN 639
Cdd:TIGR02169 883 rlGDLKKERDELEAQLRELERKIEEL--------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDeeipeeelsLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362509 640 RLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLrSELEEK----DTERSDMKETIFELEDE 697
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKraklEEERKAILERIEEYEKK 1015
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
500-746 |
2.77e-07 |
|
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: 54.00 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 500 AENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKErshhMERIIESEQKGKAALAATLEEYKATVASDQIEMNR 579
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 580 LKAQLENEKQKVAE-LYSIHNSGDKSDIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyRAFQEE 658
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 659 AKKQIEDLNMTLEKLRSELEEKDTERsdmKETIFELEDEveqhravklhdnliISDLENTVKKLQDQKHDMEREIKTLHR 738
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAER---QKLLARLEKE--------------LAELAAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1720362509 739 RLREESAE 746
Cdd:COG4942 235 EAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
398-803 |
3.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 398 TERIHQMEENQHSTSEELQATLQELADLQQITQELN--SENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhh 475
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 476 iSYVIDEDVKSGRYmELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKG 555
Cdd:COG4717 165 -LEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 556 K-----------AALAATLEEYKATVASDQIE------------------MNRLKAQLENEKQKVAELYSIHNsGDKSDI 606
Cdd:COG4717 243 ErlkearlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEE-LEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 607 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEyrAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSD 686
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 687 MKETIFELEDEVEQHR--AVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADlqtavvianDI 764
Cdd:COG4717 400 LKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED---------GE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1720362509 765 KSEAQEEIGDLKRRLHEAQEKN-------EKLTKELEEIKSRKQEE 803
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPP 516
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
621-824 |
3.87e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 621 ETLASSLQEDLAH---TRNDANRLQDTIAKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFEL 694
Cdd:PRK02224 212 ESELAELDEEIERyeeQREQARETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 695 EDEVEQHRAVKLHDNLIISDLEntvkklqDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---- 770
Cdd:PRK02224 292 EEERDDLLAEAGLDDADAEAVE-------ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElree 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362509 771 ------EIGDLKRRLHEAQEKNEKLTKELEEIKSR--KQEEERGRVYNYMNAVERDLAALRQ 824
Cdd:PRK02224 365 aaelesELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRE 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
603-804 |
4.10e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 603 KSDIQDLLESVRLDK--EKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEeAKKQIEDLNMTLEKLRSELEEK 680
Cdd:COG4717 36 KSTLLAFIRAMLLERleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 681 DTERSDMKETI--FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 758
Cdd:COG4717 115 REELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720362509 759 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
416-793 |
7.91e-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: 53.43 E-value: 7.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 416 QATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDE---------DVKS 486
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 487 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHM---ERIIESEQKGKAALAATL 563
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkEQIHLQETRKKAVVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 564 EEYK---------------ATVASDQIEMN-RLKAQLENEKQKVAElysihnSGDKSD--IQDLLESVRLDKEKAETLAS 625
Cdd:TIGR00618 497 LELQeepcplcgscihpnpARQDIDNPGPLtRRMQRGEQTYAQLET------SEEDVYhqLTSERKQRASLKEQMQEIQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 626 SLQ----------EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKE------ 689
Cdd:TIGR00618 571 SFSiltqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalha 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 690 TIFEL--EDEVEQHRAVKLHDNLIISDLENTVKKLQDQK-----------------HDMEREIKTLHRRLREESAEWRQF 750
Cdd:TIGR00618 651 LQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtllRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1720362509 751 QADLQTAVVIANDIKSEAQEEIGD-LKRRLHEAQEKNEKLTKEL 793
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAAL 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
618-823 |
9.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 618 EKAETLASSLQEDLAHTRNDANRLQDTIAKVED------EYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETI 691
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENieelikEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 692 FELEDEVEQHRAVKLHdnliISDLENTVKKLQDQKHDMEREIKTLHRR------LREESAEWRQFQADLQTAVVIANDIK 765
Cdd:PRK03918 238 EEIEELEKELESLEGS----KRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720362509 766 SEA---QEEIGDLKRRLHEAQEKN---EKLTKELEEIKSRKQE-EERGRVYNYMNAVERDLAALR 823
Cdd:PRK03918 314 KRLsrlEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEElEERHELYEEAKAKKEELERLK 378
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
576-810 |
1.00e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.71 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKaqleneKQKVAELYSihnsgdksDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQ---DTIAKVEDEY 652
Cdd:PHA02562 167 EMDKLN------KDKIRELNQ--------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQnkyDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 653 RAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHravklHDNLI-------ISDLENTVKKLQDQ 725
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY-----EKGGVcptctqqISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 726 KHDMER-----------------EIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSE---AQEEIGDLKRRLHEAQEK 785
Cdd:PHA02562 308 LKELQHslekldtaideleeimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDE 387
|
250 260
....*....|....*....|....*
gi 1720362509 786 NEKLTKELEEIKsrKQEEERGRVYN 810
Cdd:PHA02562 388 LDKIVKTKSELV--KEKYHRGIVTD 410
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
399-823 |
1.10e-06 |
|
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: 52.92 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 399 ERIHQMEENQHS--------TSEELQA-TLQELAD--LQQITQELNSENERLGEekviLMESLCQQSDKLEHFGRQieyf 467
Cdd:pfam12128 471 ERIERAREEQEAanaeverlQSELRQArKRRDQASeaLRQASRRLEERQSALDE----LELQLFPQAGTLLHFLRK---- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 468 RSLLDEHHISYVIDEdvksgrymELEQRyMDLaeNARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 547
Cdd:pfam12128 543 EAPDWEQSIGKVISP--------ELLHR-TDL--DPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 548 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSgdksdiqdllESVRLDKEKAETLASSL 627
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS----------EKDKKNKALAERKDSAN 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 628 QE--DLAHTRNdanrlqdtiaKVEDEYRAFQEEAKKQIEDLNMT-LEKLRSELEEKDTERSDMKETIFELEdevEQHRAv 704
Cdd:pfam12128 682 ERlnSLEAQLK----------QLDKKHQAWLEEQKEQKREARTEkQAYWQVVEGALDAQLALLKAAIAARR---SGAKA- 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 705 klHDNLIISDLENTVKKL---QDQKHDMEREIKTLHRRL------REESAEWRQFQADL-----QTAVVIANDIKSEAQE 770
Cdd:pfam12128 748 --ELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIeriavrRQEVLRYFDWYQETwlqrrPRLATQLSNIERAISE 825
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 771 EIGDLKRRLHEAQEKNEKLTKELEeiKSRKQEEERGRVYNYMNAVERDLAALR 823
Cdd:pfam12128 826 LQQQLARLIADTKLRRAKLEMERK--ASEKQQVRLSENLRGLRCEMSKLATLK 876
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-703 |
1.24e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 465 EYFRSL-LDEHHISYVIDEDVKS-GRYMELEQRymdlAENARFEREQLLGVQQHLSntlkmAEQDNKEAQEMIGALKERS 542
Cdd:COG4913 211 DFVREYmLEEPDTFEAADALVEHfDDLERAHEA----LEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 543 HHMERiieseQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIH--NSGD-----KSDIQDL---LES 612
Cdd:COG4913 282 RLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgNGGDrleqlEREIERLereLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 613 VRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIF 692
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250
....*....|.
gi 1720362509 693 ELEDEVEQHRA 703
Cdd:COG4913 437 NIPARLLALRD 447
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
620-882 |
1.25e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 620 AETLASSLQEDLAHTRNDANR------------LQDTIAKVEDEYRAFQEeaKKQIEDLNMTLEKLRSELEEKDTERSDM 687
Cdd:COG3206 154 ANALAEAYLEQNLELRREEARkalefleeqlpeLRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 688 KETIFELEDEVEQHRAVKLHDNLIISDLEN--TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavvIANDIK 765
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA---LRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 766 SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSR-KQEEERGRVYNymnAVERDLAALRQGMG--LSRRSSTSSEptptv 842
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARlAELPELEAELR---RLEREVEVARELYEslLQRLEEARLA----- 380
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720362509 843 ktliksfdSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVS 882
Cdd:COG3206 381 --------EALTVGNVRVIDPAVVPLKPVSPKKLLILALG 412
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
522-805 |
1.34e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 522 KMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATvASDQIEMNRLKAQLENEKQKVAELYSIHNSG 601
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 602 DKSDIQDLLESVRLDKE--KAETLASSLQEDLAHTRNDANRLQ--DTIAKVEDEYRAfqEEAKKQIEDLNMTLEKlRSEL 677
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKkaEELKKAEEKKKA--EEAKKAEEDKNMALRK-AEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 678 EEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISD---LENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADL 754
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1720362509 755 QTAVVIANDIKSEAQEEIGDlKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
620-896 |
1.72e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 620 AETLASSLQEDLAHTRNDANRLQDTIAKVEDEYrafqEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVE 699
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 700 QH-RAVKLHDNLI-----------ISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI 764
Cdd:COG3883 90 ERaRALYRSGGSVsyldvllgsesFSDFldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 765 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynymNAVERDLAALRQGMGLSRRSSTSSEPTPTVKT 844
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA-------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720362509 845 LIKSFDSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 896
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
571-799 |
2.01e-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: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 571 ASDQIEmnRLKAQLENEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLahtrnDANRLQDTIAKVED 650
Cdd:COG4913 608 NRAKLA--ALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 651 EYRAFQ------EEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAV-----------------KLH 707
Cdd:COG4913 676 ELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelralleERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 708 DNLIISDLENTVKK-LQDQKHDMEREIKTLHRRLREE----SAEWRQFQADLQTAV-----------VIANDIKSEAQEE 771
Cdd:COG4913 756 AAALGDAVERELREnLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLeslpeylalldRLEEDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 1720362509 772 igdLKRRLHEAQEK-----NEKLTKELEEIKSR 799
Cdd:COG4913 836 ---FKELLNENSIEfvadlLSKLRRAIREIKER 865
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-824 |
2.23e-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: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILmESLCQQSDKLEHFGRQIEYFRSLLDEHHI 476
Cdd:COG1196 293 LLAELARLEQDIARLEERRR---ELEERLEELEEELAELEEELEELEEEL-EELEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 SYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLK---MAEQDNKEAQEMIGALKERSHHMERIIESEQ 553
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 554 KGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAH 633
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 634 TRNDANRLQDTIAKVEDEYRAFQ-----EEAKKQIEDLN-----------MTLEKLRSELEEKDTERSDMKETIFELEDE 697
Cdd:COG1196 529 LIGVEAAYEAALEAALAAALQNIvveddEVAAAAIEYLKaakagratflpLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 698 VEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKR 777
Cdd:COG1196 609 READARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1720362509 778 RLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQ 824
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
379-823 |
2.47e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 379 ERSRKGSSGNASEVSVACLTERIHQM-EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL 457
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 458 EHFGRQIEYFRSLLDEHHISYVIDEDVksgrYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGA 537
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 538 LKERSHHMERI---IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaELYSIHNsgDKSDIQDLLESVR 614
Cdd:TIGR02169 415 LQRLSEELADLnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE--EYDRVEKELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTI----------AKVEDEYRAFQE----------------EAKKQIEDLN- 667
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKr 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 668 -----MT---LEKLRSEleEKDTERSDMKETIFELEDEVE---QHRAV---KLHDNLIISDLENT--------------- 718
Cdd:TIGR02169 570 rkagrATflpLNKMRDE--RRDLSILSEDGVIGFAVDLVEfdpKYEPAfkyVFGDTLVVEDIEAArrlmgkyrmvtlege 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 719 ----------------------------VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLqtavviandikSEAQE 770
Cdd:TIGR02169 648 lfeksgamtggsraprggilfsrsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-----------SDASR 716
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 771 EIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALR 823
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-----ENVKSELKELE 764
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
397-802 |
2.78e-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: 51.65 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 458
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 459 HFGRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 525
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 526 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLENEKQKVAELYSIHNsgdksd 605
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 606 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELeekDTE 683
Cdd:pfam05483 496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL---DKS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 684 RSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
410 420 430
....*....|....*....|....*....|....*....
gi 1720362509 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-824 |
2.81e-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: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHI 476
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 SY------VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 550
Cdd:COG1196 387 ELlealraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 551 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAET-----LAS 625
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 626 SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKE---------------T 690
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREadaryyvlgdtllgrT 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 691 IFELEDEVEQHRAVKLHDNLIISDLENTV----KKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKS 766
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGgsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362509 767 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNY----------MNAVERDLAALRQ 824
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdLEELERELERLER 774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
522-807 |
4.58e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 522 KMAEQDNKEAQEM--IGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEN---EKQKVAELYS 596
Cdd:PTZ00121 1398 KKAEEDKKKADELkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaeEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 597 IHNSGDKSDiqDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQDTI----AKVEDEYRAFQEEAK----KQIE 664
Cdd:PTZ00121 1478 KAEEAKKAD--EAKKKAEEAKKKADEAKKAAEAkkkaDEAKKAEEAKKADEAKkaeeAKKADEAKKAEEKKKadelKKAE 1555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 665 DLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREES 744
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR---IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362509 745 AEWRQFQADLQTAVVIANDIKSEAQEEI---GDLKRRLHEAQEKNEKLTKELEEikSRKQEEERGR 807
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAEED--EKKAAEALKK 1696
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
379-691 |
5.58e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.51 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 379 ERSRKGSSGNASEVsvacltERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLG-EEKVILMESLCQQSDKL 457
Cdd:pfam17380 299 ERLRQEKEEKAREV------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 458 EhFGRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaENARFEREQLLGVQQhlsntlKMAEQDNKEAQEMIGA 537
Cdd:pfam17380 373 E-ISRMRELERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQ------IRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 538 LKERSHHMERIIESEQKGKAALaatleeykATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDK 617
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720362509 618 EKAETLASSLQEdlahtRNDANRLQDTIAKVEDEYRAFQE-EAKKQIEDLNMTLEKLRSELEEKDTERSDMKETI 691
Cdd:pfam17380 513 RKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
576-805 |
5.64e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKAQLENEKQKVAElysihnsgDKSDIQDLLESVRLDKEKAETLASSLQE----------DLAHTRNDANRLQDTI 645
Cdd:TIGR04523 163 DLKKQKEELENELNLLEK--------EKLNIQKNIDKIKNKLLKLELLLSNLKKkiqknkslesQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 646 AKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliISDLENtvKKL 722
Cdd:TIGR04523 235 EKKQQEINEKTTEisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-------ISDLNN--QKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 723 QDQKHDMEREIKTLHRRLREesaewrqfqadLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEE-----------IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
...
gi 1720362509 803 EER 805
Cdd:TIGR04523 375 LKK 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
616-805 |
5.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 616 DKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQE---EAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIF 692
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 693 ELEDEVEQhRAVKLHDN-------LIIS--DLENTVKKLQDQKHdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 763
Cdd:COG4942 101 AQKEELAE-LLRALYRLgrqpplaLLLSpeDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1720362509 764 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1018-1091 |
5.98e-06 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 46.52 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1018 LLKWCQK--KTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIP----YQELNSQDKKRNFTLAFQAAESVGIKSTL-- 1089
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLtp 94
|
...
gi 1720362509 1090 -DI 1091
Cdd:cd21218 95 eDI 97
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
657-826 |
6.22e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.53 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 657 EEAKKQIEDLNMTLEKLRSELEEKdtersdmKETIFELEDEVEQHRAvklhdnliisDLENTVKKLQDQKHDMEREIKTL 736
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERE-------RRELEEEREEAERLRE----------ELEKLREELEEKLEELEEEKEEI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 737 HRRLREEsaewrqfqadlqtavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE-EERGRVYNYMNAV 815
Cdd:COG1193 566 LEKAREE-----------------AEEILREARKEAEELIRELREAQAEEEELKEARKKLEELKQElEEKLEKPKKKAKP 628
|
170
....*....|.
gi 1720362509 816 ERDLAALRQGM 826
Cdd:COG1193 629 AKPPEELKVGD 639
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
492-969 |
8.44e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 492 LEQRYMDLAENARFEReQLLGVQQHLSNTLKmAEQDNKEAQEMIGALKERSHHmERIIESEQKGKAALaatLEEYKATVA 571
Cdd:COG5022 798 KLQPLLSLLGSRKEYR-SYLACIIKLQKTIK-REKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFS---LLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 572 SDQIEMNRLKAQLENEKQKVAELYSIHNSGDKsdiqdlLESVRLdkEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDE 651
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKSISSLKLVNLE------LESEII--ELKKSLSSDLIENLEFKTELIARLKKLLNNIDLE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 652 yrafqeeakkqiEDLNMTLEKLrSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQ---DQKHD 728
Cdd:COG5022 944 ------------EGPSIEYVKL-PELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYGA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 729 MEREIKTLHRRLREesaewrqfQADLQTAVVIANDIKSEAQ--EEIGDLKRRL------HEAQEKNEKLTKELEEIKSrK 800
Cdd:COG5022 1011 LQESTKQLKELPVE--------VAELQSASKIISSESTELSilKPLQKLKGLLllennqLQARYKALKLRRENSLLDD-K 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 801 QEEERGRVYNYMNAVERD--LAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNAaaaaiprtpLSPSPMKTPPA 878
Cdd:COG5022 1082 QLYQLESTENLLKTINVKdlEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNT---------LEPVFQKLSVL 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 879 -AAVSPMQRHSISGPISTSKPLTALSDKRsnygelPVQEHLLRTSSTSRPASLPrvpaMESAKTISVSRRSSEEMKRDIS 957
Cdd:COG5022 1153 qLELDGLFWEANLEALPSPPPFAALSEKR------LYQSALYDEKSKLSSSEVN----DLKNELIALFSKIFSGWPRGDK 1222
|
490
....*....|..
gi 1720362509 958 ASEGASPASLMA 969
Cdd:COG5022 1223 LKKLISEGWVPT 1234
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
539-679 |
9.02e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 539 KERSHHMERIIESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE----LYSIHNSGDKSDIQDLLESVR 614
Cdd:COG1579 24 HRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqLGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720362509 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEE 679
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
615-824 |
1.14e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 49.33 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYR--AFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIF 692
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRqnAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 693 ELEDEVEqhravklhdnliiSDLENTVKKLQDQKHDMEREIK-TLHRRLREESAEWRQFqadlqtavviandiKSEAQEE 771
Cdd:pfam03528 93 EAIDEVK-------------SQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQY--------------RESAERE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 772 IGDLKRRLHEAQEKnEKLTKELeeiksRKQEEERGRVYNYMNAVERDLAALRQ 824
Cdd:pfam03528 146 IADLRRRLSEGQEE-ENLEDEM-----KKAQEDAEKLRSVVMPMEKEIAALKA 192
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1011-1111 |
1.16e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 45.54 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 1011 GGSKRNALLKWCQKKTEgyqNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKKRNFTLAFQAAES-VGIKST 1088
Cdd:cd21315 14 GPTPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDwLDVPQL 90
|
90 100
....*....|....*....|...
gi 1720362509 1089 LDINEMArTERPDWQNVMLYVTA 1111
Cdd:cd21315 91 IKPEEMV-NPKVDELSMMTYLSQ 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
397-732 |
1.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILmeSLCQQSDKLEHFGRQIEYFRSLLDEhhi 476
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC--PVCGRELTEEHRKELLEEYTAELKR--- 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 syvIDEDVKsgrymELEQRYMDLAENARfEREQLLGVQQHLSNTLKMAEQ--------------DNKEAQEMIGALKERS 542
Cdd:PRK03918 464 ---IEKELK-----EIEEKERKLRKELR-ELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 543 HHME---RIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENE--------KQKVAELYSIHN-----SGDKSDI 606
Cdd:PRK03918 535 IKLKgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveelEERLKELEPFYNeylelKDAEKEL 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 607 QDLLEsvRLDKEKAETLASSlqEDLAHTRNDANRLQdtiAKVEDEYRAFQEEAKKQIEDLNMTLEK----LRSELEEKDT 682
Cdd:PRK03918 615 EREEK--ELKKLEEELDKAF--EELAETEKRLEELR---KELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEK 687
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 683 ERSDMKETIFELEDEVEQHRAVKLHDNLI---ISDLENTVKKLQDQKHDMERE 732
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKELEKLekaLERVEELREKVKKYKALLKER 740
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
576-820 |
1.84e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKAQLENEKQKVAELYS--------IHNSGDKSDIQDLLESVRLDKEKAE-TLASSLQEDLAHTRNDANRLQDTIA 646
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKnlnkdeekINNSNNKIKILEQQIKDLNDKLKKNkDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 647 KVEDEYRAFQEEAK---KQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDE--------------VEQHRAVKLHDN 709
Cdd:TIGR04523 121 KLEVELNKLEKQKKenkKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnllekeklniqknIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 710 LIISDLENTVKK---LQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKN 786
Cdd:TIGR04523 201 LLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720362509 787 EK---LTKELEEIKSRKQEEERGRVYNYMNAVERDLA 820
Cdd:TIGR04523 281 KKikeLEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
399-805 |
2.37e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 399 ERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHHISY 478
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 479 VIDE-------DVKSGRYMELEQRYM------------DLAENARFEREQL-------LGVQQHLSNTLKMAEQDNKEAQ 532
Cdd:TIGR00606 378 ELDGfergpfsERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQAdeirdekKGLGRTIELKKEILEKKQEELK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 533 EMIGALKERSHHMERIIESEQKGKAALA--------ATLEEYKATVASDQIEMNRLKAQLENEKQKVAEL---------- 594
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERelskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqm 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 595 --------------YSIHNSGD------------KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKV 648
Cdd:TIGR00606 538 emltkdkmdkdeqiRKIKSRHSdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 649 EDEYRAFQEEAKK--QIEDLNMTLEKLRSELEEKDTERSDM-------KETIFELEDE-------VEQHRAVKLHDNLII 712
Cdd:TIGR00606 618 EEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLagatavySQFITQLTDEnqsccpvCQRVFQTEAELQEFI 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 713 SDLENTVKKLQDQKHDMEREIKTLHRRlREESAewrqfqadlqtavviandIKSEAQEEIGDLK-RRLHEAQEKNEKLTK 791
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKR-RDEML------------------GLAPGRQSIIDLKeKEIPELRNKLQKVNR 758
|
490
....*....|....
gi 1720362509 792 ELEEIKSRKQEEER 805
Cdd:TIGR00606 759 DIQRLKNDIEEQET 772
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-802 |
3.60e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 652 YRAFQEEAKKQIEDLNMTLEKL---RSELE----------EKDTERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENT 718
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLediLNELErqlkslerqaEKAERYKELKAELRELELALLVLRLEELREEL--EELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 719 VKKLQDQKHDMEREIKTLH---RRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 795
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
....*..
gi 1720362509 796 IKSRKQE 802
Cdd:TIGR02168 328 LESKLDE 334
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
583-896 |
3.70e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 583 QLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQ 662
Cdd:COG3883 17 QIQAKQKELSEL-----QAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 663 IEDLNM---TLEKLRSELEEKDTErsdmketifELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLhrr 739
Cdd:COG3883 92 ARALYRsggSVSYLDVLLGSESFS---------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 740 lreesaewRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDL 819
Cdd:COG3883 160 --------EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA-----AAAAAAA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362509 820 AALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNAAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 896
Cdd:COG3883 227 AAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
413-682 |
4.32e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQAtlqELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFGRQIEYFRSLLDEHHISyvIDEDvkSGRYMEL 492
Cdd:PRK02224 478 EELEA---ELEDLEEEVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRET--IEEK--RERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 493 EQRYMDLAENARFEREQLlgvqqhlsntlKMAEQDNKEAQEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATVAS 572
Cdd:PRK02224 543 RERAAELEAEAEEKREAA-----------AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIER 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 573 ------DQIEMNRL-KAQLENEKQKVAELYSIHNsgdksdiQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTI 645
Cdd:PRK02224 611 lrekreALAELNDErRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720362509 646 AKVEDEYRAFqEEAKKQIEDLNMTLEKLRSELEEKDT 682
Cdd:PRK02224 684 GAVENELEEL-EELRERREALENRVEALEALYDEAEE 719
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
161-801 |
4.97e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 161 EGDIRMSKSKSDNQIsdKAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGISEDHCEG-EDRSEVKETIIAHQPTD 239
Cdd:pfam15921 244 EDQLEALKSESQNKI--ELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 240 VESTLLQLqeqntaiREELNQLKnenRMLKDRLNALGFSLEqrLDNSEklfgyqsLSPEITPGNQ-SDGGGTLTSSVEGS 318
Cdd:pfam15921 322 LESTVSQL-------RSELREAK---RMYEDKIEELEKQLV--LANSE-------LTEARTERDQfSQESGNLDDQLQKL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 319 APG----SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGvpSIERSRKGSSG-NAS 390
Cdd:pfam15921 383 LADlhkrEKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNES 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 391 EVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFGRQIEYFRSL 470
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 471 ldehhisyvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIE 550
Cdd:pfam15921 526 ---------VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVG 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 551 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---- 625
Cdd:pfam15921 580 QHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdi 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 626 -----SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMketifeledEVEQ 700
Cdd:pfam15921 652 kqerdQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM---------EGSD 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 701 HRAVKLhdnliisdlentVKKLQDQKHDMEREIKTLHRRLreesaewrQFqadLQTAVVIANDIKSEAQEEIGDLKRRLH 780
Cdd:pfam15921 723 GHAMKV------------AMGMQKQITAKRGQIDALQSKI--------QF---LEEAMTNANKEKHFLKEEKNKLSQELS 779
|
650 660
....*....|....*....|.
gi 1720362509 781 EAQEKNEKLTKELEEIKSRKQ 801
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQER 800
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
605-808 |
6.43e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 605 DIQDLLESVRLDKEKAETLASSLQedlahtrndanRLQDTIAKVEDEYRAFQEEAKKqiedlnmtLEKLRSELEEKDTER 684
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQ-----------QHGNALAQLEPIVSVLQSDPEQ--------FEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 685 SDMKETIFELEDEVEQHRAVKLHDNLII----SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVI 760
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDAAEMlaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 761 ANDIKSEAQEEIGDLKRRLHE-----AQEKNEKLTKELEEIKSRKQEEERGRV 808
Cdd:PRK04863 1032 KRQMLQELKQELQDLGVPADSgaeerARARRDELHARLSANRSRRNQLEKQLT 1084
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
636-803 |
6.63e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 636 NDANRLQDTIAKVEDEYRAfQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIF-ELEDEVEQH-RAVKLHDNLIIS 713
Cdd:PRK00409 513 EDKEKLNELIASLEELERE-LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAiKEAKKEADEIIK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 714 DLENTVKKLQ-DQKhdmEREIKTLHRRLRE-----------ESAEWRQFQA--------DLQTAVVIANDIKSEAQEEIG 773
Cdd:PRK00409 592 ELRQLQKGGYaSVK---AHELIEARKRLNKanekkekkkkkQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAG 668
|
170 180 190
....*....|....*....|....*....|
gi 1720362509 774 DLKRRLHEAQEknEKLTKELEEIKSRKQEE 803
Cdd:PRK00409 669 IMKMKVPLSDL--EKIQKPKKKKKKKPKTV 696
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
605-738 |
6.88e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.21 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 605 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSElEEKD 681
Cdd:cd22656 99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362509 682 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDMEREIKTLHR 738
Cdd:cd22656 176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
397-839 |
8.69e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 8.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSE--ELQATL-----QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRS 469
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNEsnELHEKQkfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 470 LldehhisyviDEDVKSGRYMELEQ-RYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEaqemigalkerSHHMERI 548
Cdd:pfam15921 160 L----------KEDMLEDSNTQIEQlRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMS-----------TMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 549 IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENekqKVAELYSIHnsgdksdiQDLLESVRLDKEKAETlasSLQ 628
Cdd:pfam15921 219 GSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQN---KIELLLQQH--------QDRIEQLISEHEVEIT---GLT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 629 EDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKE-----------TIFELEDE 697
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEelekqlvlansELTEARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 698 VEQ--HRAVKLHDNL--IISDLENTVKKLQDQKHDMER----------EIKTLHRRLREESAEWRQFQADLQTavviand 763
Cdd:pfam15921 365 RDQfsQESGNLDDQLqkLLADLHKREKELSLEKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKA------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 764 IKSEAQeeiGDLKRRLHEAQEKNE------KLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGMGLSRRS--S 833
Cdd:pfam15921 438 MKSECQ---GQMERQMAAIQGKNEslekvsSLTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAieA 514
|
....*.
gi 1720362509 834 TSSEPT 839
Cdd:pfam15921 515 TNAEIT 520
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
576-826 |
9.90e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKA-QLENEKQKVAElySIHNSGdKSDIQDLLESVRLDK-EKAETLASSLQEDLAHTRNDANrLQDTIAKVEDEYR 653
Cdd:PRK05771 5 RMKKVLIvTLKSYKDEVLE--ALHELG-VVHIEDLKEELSNERlRKLRSLLTKLSEALDKLRSYLP-KLNPLREEKKKVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 654 AFQEEakKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQhraVKlhdnlIISDLENTVKKLQDQKHdMEREI 733
Cdd:PRK05771 81 VKSLE--ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER---LE-----PWGNFDLDLSLLLGFKY-VSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 734 KTLHRRLREES-AEWRQFQADLQT--------AVVIANDIKSEAQEEI-------------GDLKRRLHEAQEKNEKLTK 791
Cdd:PRK05771 150 GTVPEDKLEELkLESDVENVEYIStdkgyvyvVVVVLKELSDEVEEELkklgferleleeeGTPSELIREIKEELEEIEK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720362509 792 ELEEIKSR------KQEEERGRVYNYM-NAVERDLAALRQGM 826
Cdd:PRK05771 230 ERESLLEElkelakKYLEELLALYEYLeIELERAEALSKFLK 271
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
659-805 |
1.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 659 AKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLII--SDLENTVKKLQDQKHDMEREIKTL 736
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362509 737 hRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:COG4913 688 -AALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
506-826 |
1.07e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 506 EREQLlgvqQHLSNTL-------KMAEQDNKEAQEMIGALKERSHHMERIIESeqkgkaALAATLEEYKATVASDQIEMN 578
Cdd:pfam00038 2 EKEQL----QELNDRLasyidkvRFLEQQNKLLETKISELRQKKGAEPSRLYS------LYEKEIEDLRRQLDTLTVERA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 579 RLKAQLENekqkvaelysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLqdTIAKVEDEyrafqee 658
Cdd:pfam00038 72 RLQLELDN-------------------LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA--TLARVDLE------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 659 akKQIEDLNMTLEKLRSELEEkdtERSDMKETIfeledeVEQHRAVKLHDNLIIsDLENTVKKLQDQKHDMEReiktlhr 738
Cdd:pfam00038 124 --AKIESLKEELAFLKKNHEE---EVRELQAQV------SDTQVNVEMDAARKL-DLTSALAEIRAQYEEIAA------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 739 RLREESAEWRQFQ-ADLQTAVVIANDIKSEAQEEIGDLKRRLH------EAQEK-NEKLTKELEEIKSRkQEEERGRVYN 810
Cdd:pfam00038 185 KNREEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQsleielQSLKKqKASLERQLAETEER-YELQLADYQE 263
|
330
....*....|....*.
gi 1720362509 811 YMNAVERDLAALRQGM 826
Cdd:pfam00038 264 LISELEAELQETRQEM 279
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
399-805 |
1.28e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 399 ERIHQMEENQHSTSEELQATLQE----LADLQQITQELNSENERLG---EEKVILMESLCQQSDKLEHFGRQIEYFRSLL 471
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKVSlklEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 472 DEHHISYVIDEDVKSGRYMELEQRYMDL----------AENARFEREQLLGVQ----QHLSNTLKmAEQDNKEaqemiga 537
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqAENARLEMHFKLKEDhekiQHLEEEYK-KEINDKE------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 538 lKERSHHMERIIESEQKGKAaLAATLEEYKATV----ASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS--------- 604
Cdd:pfam05483 240 -KQVSLLLIQITEKENKMKD-LTFLLEESRDKAnqleEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 605 DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEE-- 679
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEmt 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 680 -----KDTERSDMKETIFELEDEVEQHRAV-KLHDNLIISDLENT--VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQ 751
Cdd:pfam05483 398 kfknnKEVELEELKKILAEDEKLLDEKKQFeKIAEELKGKEQELIflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1720362509 752 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
576-960 |
1.38e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.19 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKAQLENEKQKVAELYS----IHNSGDKSDIQDL--LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVE 649
Cdd:PTZ00108 1003 KLERELARLSNKVRFIKHVINgelvITNAKKKDLVKELkkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 650 DEYRAFQEEAKKQIEDLNMT-LEKLRSELEEKDTERSDMKETifeledEVEQhravklhdnLIISDLENTVKKLQDQKHD 728
Cdd:PTZ00108 1083 GAAVSYDYLLSMPIWSLTKEkVEKLNAELEKKEKELEKLKNT------TPKD---------MWLEDLDKFEEALEEQEEV 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 729 MEREI----------KTLHRRLR------EESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEK-LTK 791
Cdd:PTZ00108 1148 EEKEIakeqrlksktKGKASKLRkpklkkKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSdQED 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 792 ELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNaaaaaiPRTPLSPS 871
Cdd:PTZ00108 1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPD------GESNGGSK 1301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 872 PMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRSnygelpvQEHLLRTSSTSRPASLPRVPAMESAKTISvsrrSSEE 951
Cdd:PTZ00108 1302 PSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKS-------KTRVKQASASQSSRLLRRPRKKKSDSSSE----DDDD 1370
|
....*....
gi 1720362509 952 MKRDISASE 960
Cdd:PTZ00108 1371 SEVDDSEDE 1379
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1034-1081 |
1.56e-04 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 41.99 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720362509 1034 ITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKKRNFTLAFQAAE 1081
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAK 69
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
656-826 |
1.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 656 QEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDMEREIKT 735
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 736 LHRRLREesaeWRQFQADLQTAvviANDIKsEAQEEIGDLKRRLHEAQEKN-EKLTKELEEIKSRKQ--EEERGRVYNYM 812
Cdd:COG4717 151 LEERLEE----LRELEEELEEL---EAELA-ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAelEEELEEAQEEL 222
|
170
....*....|....
gi 1720362509 813 NAVERDLAALRQGM 826
Cdd:COG4717 223 EELEEELEQLENEL 236
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
626-804 |
2.06e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 626 SLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHR 702
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaeKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 703 AVKlhdNLIISDLENtVKKLQDQKHDMEREIKTLHRRLREEsaEWRQfqadlQTAVVianDIKSEAQ--EEIGDLKRRLH 780
Cdd:COG1340 85 EKL---NELREELDE-LRKELAELNKAGGSIDKLRKEIERL--EWRQ-----QTEVL---SPEEEKElvEKIKELEKELE 150
|
170 180
....*....|....*....|....*...
gi 1720362509 781 EAQ---EKNEKLTKELEEIKS-RKQEEE 804
Cdd:COG1340 151 KAKkalEKNEKLKELRAELKElRKEAEE 178
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
489-826 |
2.22e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 489 YMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKE------------AQEMIGALKERSHHMERIIESEQKGk 556
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKAleyyqlkeklelEEEYLLYLDYLKLNEERIDLLQELL- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 557 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 636
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE-----ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 637 DANRLQDTI----------AKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKL 706
Cdd:pfam02463 322 EKKKAEKELkkekeeieelEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 707 HDNLIISDLentvKKLQDQKHDMEREIKTLHRRLREESAEWRQFQaDLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKN 786
Cdd:pfam02463 402 EEEKEAQLL----LELARQLEDLLKEEKKEELEILEEEEESIELK-QGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720362509 787 EKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGM 826
Cdd:pfam02463 477 TQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
482-793 |
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 1720362509 482 EDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK-AALA 560
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 561 ATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN- 639
Cdd:pfam12128 308 GELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS-WQSELENLEERLKALTGKHQDVTAKYNRRRSKIKe 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 640 RLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELeekdteRSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTV 719
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATP 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720362509 720 KKLQDQKHDMEReiktLHRrLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL 793
Cdd:pfam12128 461 ELLLQLENFDER----IER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
576-677 |
3.23e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKAQLenekQKVAELYSIHNSGdKSDIQDLLESVRLDKEKAETLASSLQ---EDLAHTRNDANRLQDTIAKVEDEY 652
Cdd:PRK09039 54 ALDRLNSQI----AELADLLSLERQG-NQDLQDSVANLRASLSAAEAERSRLQallAELAGAGAAAEGRAGELAQELDSE 128
|
90 100
....*....|....*....|....*
gi 1720362509 653 RAFQEEAKKQIEDLNMTLEKLRSEL 677
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQL 153
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
364-823 |
3.35e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 364 LDAPSSSESEGVPSIER--------SRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNS- 434
Cdd:PRK01156 206 IADDEKSHSITLKEIERlsieynnaMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKi 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 435 ENERLGEEKVILMESLCQQSDkLEHFGRQIEYFRSLLDEHHISYVIDEDVKSGR--YMELEQRYMDLAEnarfEREQLLG 512
Cdd:PRK01156 286 INDPVYKNRNYINDYFKYKND-IENKKQILSNIDAEINKYHAIIKKLSVLQKDYndYIKKKSRYDDLNN----QILELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 513 VQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVA 592
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 593 ELysihnsgdkSDIQDLLESVRLDKEKAETLASSLQEDLA-HTRNDANRLQDTIAKVEDEYRAFQEEAKKQI-------- 663
Cdd:PRK01156 441 EL---------SRNMEMLNGQSVCPVCGTTLGEEKSNHIInHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeyles 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 664 EDLNMT------LEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHD-----------NLIISDLEntVKKLQDQK 726
Cdd:PRK01156 512 EEINKSineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDldskrtswlnaLAVISLID--IETNRSRS 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 727 HDMEREIKTLHRRLREESAEWRQFQADLQTAV-VIANDIKS--EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRkqEE 803
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIrEIENEANNlnNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI--IP 667
|
490 500
....*....|....*....|
gi 1720362509 804 ERGRVYNYMNAVERDLAALR 823
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSR 687
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
534-807 |
3.40e-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: 44.78 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 534 MIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLEnekQKVAELYSIHNSGDKSDIQ--DLLE 611
Cdd:pfam01576 188 MISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA---KKEEELQAALARLEEETAQknNALK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 612 SVRldkeKAETLASSLQEDLahtrndanrlqdtiakveDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETI 691
Cdd:pfam01576 265 KIR----ELEAQISELQEDL------------------ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 692 FELEDEVEQHRAVklhdnliisdLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEE 771
Cdd:pfam01576 323 SKREQEVTELKKA----------LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAE 392
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720362509 772 IGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:pfam01576 393 LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQR 428
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
539-805 |
3.80e-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: 44.73 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 539 KERSHHMERIiESEQKGkAALAATLEEYKATVASDQIEMNRLKAQlENEKQKVaelysihnsgdksdIQDLLESVRLDKE 618
Cdd:pfam05557 21 MELEHKRARI-ELEKKA-SALKRQLDRESDRNQELQKRIRLLEKR-EAEAEEA--------------LREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 619 KAETLASSLQEDLAhTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELE--- 695
Cdd:pfam05557 84 YLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 696 ----------DEVEQHRAVKLHDNLIIsdleNTVKKLQDQKHDMEREIKtlhrRLREESAEWRQFQADlqtavviandiK 765
Cdd:pfam05557 163 sslaeaeqriKELEFEIQSQEQDSEIV----KNSKSELARIPELEKELE----RLREHNKHLNENIEN-----------K 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1720362509 766 SEAQEEIGDLKRRLH---EAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:pfam05557 224 LLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVK 266
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-800 |
4.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 517 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVaelys 596
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL----- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 597 ihnsgdkSDIQDLLESVRLDKEKaetlassLQEDLAHTRNDANRLQDTIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSE 676
Cdd:TIGR04523 471 -------KVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 677 LEEKDTERSDMKETIFELEDeveqhravklhdnliisdlENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQT 756
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDF-------------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720362509 757 AVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKELEEIKSRK 800
Cdd:TIGR04523 594 KEKEKKDLIKEIEEkekKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
409-660 |
4.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 409 HSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEhhisyvIDEDVKsgr 488
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 489 ymELEQRYMDLAENARFEREQLlgvQQHLSNTLKMAEQDNKE---AQEMIGALKERSHHMERIIESEQKGKAALAATLEE 565
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 566 YKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEdlahtrnDANRLQDTI 645
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQ-------EAEELEALI 229
|
250
....*....|....*
gi 1720362509 646 AKVEDEYRAFQEEAK 660
Cdd:COG4942 230 ARLEAEAAAAAERTP 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
514-807 |
4.46e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.43 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 514 QQH---LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQK-------GKAALAATLEEYKATVASDQIEMNRLKAQ 583
Cdd:pfam10174 323 KQHievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKqlqdlteEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 584 LENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQI 663
Cdd:pfam10174 403 IENLQEQLRD-----KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 664 EDLNMTLEKLRSELEEKDTERSDMKE--------------TIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQ---- 725
Cdd:pfam10174 478 KDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEE-------CSKLENQLKKAHNAeeav 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 726 --KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI---KSEAQEEIGDLKRRlheAQEKNEKLTKELEEIKSRK 800
Cdd:pfam10174 551 rtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVeneKNDKDKKIAELESL---TLRQMKEQNKKVANIKHGQ 627
|
....*..
gi 1720362509 801 QEEERGR 807
Cdd:pfam10174 628 QEMKKKG 634
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
491-797 |
4.99e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 491 ELEQRYMDLAEN--ARFErEQLLGVQQhLSNTLKM--AEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAAT 562
Cdd:PRK04778 68 EWRQKWDEIVTNslPDIE-EQLFEAEE-LNDKFRFrkAKHEINEIESLLDLIEEDIEQIleelQELLESEEKNREEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 563 LEEY---KATV---------ASDQIEmnrlkAQLENEKQKVAELYSIHNSGDKsdiqdllesvrldkEKAETLASSLQED 630
Cdd:PRK04778 146 KDLYrelRKSLlanrfsfgpALDELE-----KQLENLEEEFSQFVELTESGDY--------------VEAREILDQLEEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 631 LAHTRNDANRLQDTIAKVEDEYRAfqeeakkQIEDLNMTLEKLR------------SELEEKDTERSDMKETIFELE-DE 697
Cdd:PRK04778 207 LAALEQIMEEIPELLKELQTELPD-------QLQELKAGYRELVeegyhldhldieKEIQDLKEQIDENLALLEELDlDE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 698 VEQhravklhdnlIISDLENTVKKLQDQkhdMEREIKTlhrrlreesaewrqfqadlqtavviandiKSEAQEEIGDLKR 777
Cdd:PRK04778 280 AEE----------KNEEIQERIDQLYDI---LEREVKA-----------------------------RKYVEKNSDTLPD 317
|
330 340
....*....|....*....|
gi 1720362509 778 RLHEAQEKNEKLTKELEEIK 797
Cdd:PRK04778 318 FLEHAKEQNKELKEEIDRVK 337
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
576-726 |
5.13e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 576 EMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYraf 655
Cdd:smart00787 155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720362509 656 qEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 726
Cdd:smart00787 221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
202-779 |
5.68e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 202 LRNELRDMRAQLGISEDHCEGEDRSEVKETIIAHQPTdVESTLLQLQEQNTAIREELNQLKNEnrmLKDRLNALgfslEQ 281
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSKMRSRAKL---LMKRAAHV----KQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 282 RLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSAPGSVEDLLSQDENTLMDHQHSNS----MDNLDSECSEVyQPL 357
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSlckeLDILQREQATI-DTR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 358 TSSDDALDAP-SSSESEGVPSIERSRKGSSgnASEVSVACLTERIHQMEENQHSTSEELQatlqELADLQQITQ------ 430
Cdd:TIGR00618 416 TSAFRDLQGQlAHAKKQQELQQRYAELCAA--AITCTAQCEKLEKIHLQESAQSLKEREQ----QLQTKEQIHLqetrkk 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 431 -------ELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEyfrSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENA 503
Cdd:TIGR00618 490 avvlarlLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ---RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 504 RFEREQLLGVQQ------HLSNTLKMAE------QDNKEAQEMIG--------------ALKERSHHMERIIESEQKGKA 557
Cdd:TIGR00618 567 EIQQSFSILTQCdnrskeDIPNLQNITVrlqdltEKLSEAEDMLAceqhallrklqpeqDLQDVRLHLQQCSQELALKLT 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 558 ALAATL-----EEYKATVASDQIEMNRLKAQLENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETL--------- 623
Cdd:TIGR00618 647 ALHALQltltqERVREHALSIRVLPKELLASRQLALQKMQSEKE-QLTYWKEMLAQCQTLLRELETHIEEYdrefneien 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 624 -ASSLQEDLA-------HTRNDANRLQDTI--AKVEDEYRAFQEEAKKqiEDLNMTLEKLRSELEEKDTERSDMKETIFE 693
Cdd:TIGR00618 726 aSSSLGSDLAaredalnQSLKELMHQARTVlkARTEAHFNNNEEVTAA--LQTGAELSHLAAEIQFFNRLREEDTHLLKT 803
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 694 LEDEVEQHR-----AVKLHDNLIISDLENTVKKLQdQKHDMEREIKTLHRRLREES---AEWRQFQADLQTAVVIANDIK 765
Cdd:TIGR00618 804 LEAEIGQEIpsdedILNLQCETLVQEEEQFLSRLE-EKSATLGEITHQLLKYEECSkqlAQLTQEQAKIIQLSDKLNGIN 882
|
650
....*....|....
gi 1720362509 766 SEAQEEIGDLKRRL 779
Cdd:TIGR00618 883 QIKIQFDGDALIKF 896
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
619-834 |
6.49e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 619 KAETLASSLQEDLaHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDlnmTLEKLRSELEEKDTERSDMKETIFELE--- 695
Cdd:pfam07888 28 RAELLQNRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEeky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 696 -------DEVEQHRAVKLHDN----LIISDLENTVKKLQDQKHDMEREI-------KTLHRRLREESAEWRQFQADLQTA 757
Cdd:pfam07888 104 kelsassEELSEEKDALLAQRaaheARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720362509 758 VVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynyMNAVERDLAALRQGMGLSRRSST 834
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKVE 254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
509-807 |
6.68e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 509 QLLGVQQHLSNTLKMAEQDN--KEAQEMIGALKE-RSHHMERIIESEQKGKAALAATleEYKATVASDQ----IEMNRLK 581
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQermaMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 582 AQLENEKQKvAELYSIHNSGDKSDIQDLLESVRLDKEKAEtlasslqedlahtRNDANRLQDTIAKvedEYRAFQEEAKK 661
Cdd:pfam17380 351 ERIRQEERK-RELERIRQEEIAMEISRMRELERLQMERQQ-------------KNERVRQELEAAR---KVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 662 QIEDLNMTLEKLRSELEEKDTERSDMKETifELEDEVEQHRAVKLhdnliisDLENTVKKLQDQKHDMEReiktlhRRLR 741
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQ-------ERQQQVERLRQQEEERKR------KKLE 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362509 742 EESAEWRQFQADLQTAVVIandikseaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 807
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKIL--------EKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR 536
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
506-818 |
7.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 506 EREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKaTVASDQIEMNRLKAQLE 585
Cdd:TIGR00606 724 RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 586 NEKQKVAELYSIHNSGD-----------KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD---TIAKVEDE 651
Cdd:TIGR00606 803 DVERKIAQQAAKLQGSDldrtvqqvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQR 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 652 YRAFQEeakkQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKH---- 727
Cdd:TIGR00606 883 RQQFEE----QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymk 958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 728 ---------------DMEREIKTLHRRLREESAEWRQFQADLQTavvIANDIKSEAQEE------IGDLKRR--LHEAQE 784
Cdd:TIGR00606 959 dienkiqdgkddylkQKETELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnLTLRKREneLKEVEE 1035
|
330 340 350
....*....|....*....|....*....|....
gi 1720362509 785 KNEKLTKELEEIKSRKQEEERGRVYNYMNAVERD 818
Cdd:TIGR00606 1036 ELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRN 1069
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
517-824 |
7.89e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 517 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIiESEQKGKAALAATLEEYKAtVASDQIEMNRLKAQLENEKQKVAELYs 596
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELE- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 597 ihnsgdksdiQDLLESVRLDKEKAEtlassLQEDLAHTRNDANRLQDTIAKVEDEYrafQEEAKKQIEDLNMTLEKLRSE 676
Cdd:COG4717 153 ----------ERLEELRELEEELEE-----LEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 677 LEEKDTERSDMKETIFELEDEVEQHRAV-KLHDN------------------------------------LIISDLENTV 719
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEeRLKEArlllliaaallallglggsllsliltiagvlflvlgLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 720 KKLQDQKHDMErEIKTLHRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSR 799
Cdd:COG4717 295 REKASLGKEAE-ELQALPALEELEEEELEELLAALGLP-------PDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340
....*....|....*....|....*
gi 1720362509 800 KQEEERGRVYNYMNAveRDLAALRQ 824
Cdd:COG4717 367 ELEQEIAALLAEAGV--EDEEELRA 389
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
728-785 |
8.50e-04 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 41.95 E-value: 8.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720362509 728 DMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 785
Cdd:PRK10884 97 DLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNQLIVAQKK 154
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
657-805 |
1.28e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 657 EEAKKQI----EDLN---MTLEKLRSELEEKDTERSdmketifELEDEVEqhravKLHDnliisDLENTVKKLQDQKhdm 729
Cdd:PRK00409 505 EEAKKLIgedkEKLNeliASLEELERELEQKAEEAE-------ALLKEAE-----KLKE-----ELEEKKEKLQEEE--- 564
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720362509 730 EREIKTLHRRLREESAEWRqfqadlQTAVVIANDIKSEAQEEIGDLKRrlHEAQEKNEKLTKELEEIKSRKQEEER 805
Cdd:PRK00409 565 DKLLEEAEKEAQQAIKEAK------KEADEIIKELRQLQKGGYASVKA--HELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
413-802 |
1.36e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQATLQELADLQQitqELNSENERLGEEKVILMESLCQQSDKLEHFGRQIEYFRSLLDEHhisyvideDVKSGRYMEL 492
Cdd:pfam10174 331 ESLTAKEQRAAILQT---EVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML--------DVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 493 EQRYMDLAENARFEREQLLGvqqhLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKA----ALAATLEEYKA 568
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREredrERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 569 TVASDQIEMNRLKAQLENEKQKVAEL----YSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANR---- 640
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLkehaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpe 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 641 LQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRseleEKDTERSDMKETIFELEDEVEQHravklhdnliISDLENTVK 720
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAELESLTLRQ----------MKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 721 KLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSeaQEEIGDLKRRLHEAQ----EKNEKLT------ 790
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQqslaEKDGHLTnlraer 699
|
410
....*....|...
gi 1720362509 791 -KELEEIKSRKQE 802
Cdd:pfam10174 700 rKQLEEILEMKQE 712
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
657-824 |
1.50e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 657 EEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKtl 736
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEELE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 737 hrRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVE 816
Cdd:COG4372 105 --SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*...
gi 1720362509 817 RDLAALRQ 824
Cdd:COG4372 183 QALDELLK 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
608-824 |
1.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 608 DLLESVRLDKEKAETLASSLQEDLAHTR-------------NDANRLQDTIAKVEDEYRAFQ-----EEAKKQIEDLNMT 669
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPvkgsnvieisytsPDPELAAAVANALAEAYLEQNlelrrEEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 670 LEKLRSELEEKDTERSDMKET--IFELEDEVEQHRAvklhdnlIISDLENTVKKLQDQKhdmeREIKTLHRRLREESAEW 747
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQ-------QLSELESQLAEARAEL----AEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362509 748 RQFQADLQTAVVIANDIK--SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvyNYMNAVERDLAALRQ 824
Cdd:COG3206 253 PDALPELLQSPVIQQLRAqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----RILASLEAELEALQA 327
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
521-804 |
1.80e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 521 LKMAEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAATLEEYKAtvASDQIEMNR---------LKAQLENE 587
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQIleelDELLESEEKNREEVEELKDKYRE--LRKTLLANRfsygpaideLEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 588 KQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDanrLQDTIAKVEDEYRAFQEE--------- 658
Cdd:pfam06160 159 EEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE---LPDQLEELKEGYREMEEEgyalehlnv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 659 ------AKKQIEDLNMTLEKLR-SELEEKDTERSDMKETIFE-LEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDME 730
Cdd:pfam06160 236 dkeiqqLEEQLEENLALLENLElDEAEEALEEIEERIDQLYDlLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 731 REIKTLHrrLRE-ESAEWRQFQADLQTAV----VIANDIK------SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIksR 799
Cdd:pfam06160 316 RVQQSYT--LNEnELERVRGLEKQLEELEkrydEIVERLEekevaySELQEELEEILEQLEEIEEEQEEFKESLQSL--R 391
|
....*
gi 1720362509 800 KQEEE 804
Cdd:pfam06160 392 KDELE 396
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
496-802 |
1.94e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 496 YMDLAENARFEREQLLGVQQHLSN---TLKMAEQDNKEAQEMIGALKERSHHMERIIESeQKGKAALAATLEEYKATVAS 572
Cdd:PRK04863 274 YMRHANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 573 DQIEMNRLKAQLENEKQKVAElysihnsgdksdIQDLLESVRLDKEKAET----LASSL---QE--DLAHTR----NDAN 639
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEE------------ADEQQEENEARAEAAEEevdeLKSQLadyQQalDVQQTRaiqyQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 640 RLQD-----------TIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEKD---------------TERSDMKETIFE 693
Cdd:PRK04863 421 QALErakqlcglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSqfeqayqlvrkiageVSRSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 694 LEDEVEQHRAvklhdnliisdlentvkkLQDQKHDMEREIKTLHRRLREESAEWR-------QFQADLQTAVViANDIKS 766
Cdd:PRK04863 501 LLRRLREQRH------------------LAEQLQQLRMRLSELEQRLRQQQRAERllaefckRLGKNLDDEDE-LEQLQE 561
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720362509 767 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
517-803 |
2.02e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 517 LSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQkgkaalaatleEYKATVASDQIEMNRLKAQLENEKQKVAELYS 596
Cdd:TIGR04523 347 LKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 597 -IHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFqeeaKKQIEDLNMTLEKLR 674
Cdd:TIGR04523 413 qIKKlQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 675 SELEEKDTERSDMKETIFELEDEVeqhraVKLHDNliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADl 754
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKV-----KDLTKK--ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE- 560
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720362509 755 qtavvianDIKSEAQEEIgdlkRRLHEAQEKNEKLTKELEEIKSRKQEE 803
Cdd:TIGR04523 561 --------KEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
413-809 |
2.09e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQATLQELADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHFGRQIEYFRSLLDEHHISYVIDEDVKs 486
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskseLARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLK- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 487 gRYMELEQRYMDLAENARFEREQLLG--------VQQH---------LSNTLKMAEQDNKEAQEMIGALKERSHHMERII 549
Cdd:pfam05557 235 -RKLEREEKYREEAATLELEKEKLEQelqswvklAQDTglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 550 -ESEQKGKAALAATLEEYKATVASDQI-------------EMNRLKAQLEN-EKQKVAELYSIHNSGDKSDIQDLLESVR 614
Cdd:pfam05557 314 rELEQELAQYLKKIEDLNKKLKRHKALvrrlqrrvllltkERDGYRAILESyDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 615 LDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEdeyrafQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFEL 694
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 695 EDEVEQH-----------RAVKLHDNliisdleNTVKKLQDQKHDMER---EIKTLHRRLreesaewRQFQADLQTAVVI 760
Cdd:pfam05557 468 EMELERRclqgdydpkktKVLHLSMN-------PAAEAYQQRKNQLEKlqaEIERLKRLL-------KKLEDDLEQVLRL 533
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1720362509 761 ANDIKSEAQEEIGDLKRRLHEAQEKNEKltkeLEEIKSRKQEEERGRVY 809
Cdd:pfam05557 534 PETTSTMNFKEVLDLRKELESAELKNQR----LKEVFQAKIQEFRDVCY 578
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
540-660 |
2.11e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 540 ERSHHMERII-------ESEQKGKAALAATLEEykatvasdqieMNRLKAQLENEKQKVAELYSihnsgDKSDIQDLLES 612
Cdd:PRK11637 149 EESQRGERILayfgylnQARQETIAELKQTREE-----------LAAQKAELEEKQSQQKTLLY-----EQQAQQQKLEQ 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 613 VRLDKEKAET-LASSLQED---LAHTRNDANRLQDTIAKVEDEYRAFQE-EAK 660
Cdd:PRK11637 213 ARNERKKTLTgLESSLQKDqqqLSELRANESRLRDSIARAEREAKARAErEAR 265
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
603-802 |
2.26e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 603 KSDIQDLLESvRLDKEKAEtLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQeeakkqiedlNMTLEKLRSELEEKDT 682
Cdd:TIGR01612 662 KSELSKIYED-DIDALYNE-LSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ----------NMETATVELHLSNIEN 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 683 ERSDMKETIFELEDEVeqHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHrRLREESAEWRQFQADlqtAVVIAN 762
Cdd:TIGR01612 730 KKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSKISEIKNHYND---QINIDN 803
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720362509 763 DIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 802
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
405-795 |
2.42e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 405 EENQH--STSEELQATLQELADLQQITQELNSENERLGEEKVILM----ESLCQQSDKLEHFGRQIEYFRSLLDEhhisy 478
Cdd:pfam10174 67 EENQHlqLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelteENFRRLQSEHERQAKELFLLRKTLEE----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 479 videdvksgryMELEQRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGAlKERSHHMERIIESEQKGKA 557
Cdd:pfam10174 142 -----------MELRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIAEA-EMQLGHLEVLLDQKEKENI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 558 ALAATLeEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDL------ 631
Cdd:pfam10174 210 HLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSL--------ERNIRDLEDEVQMLKTNGLLHTEDREEEIkqmevy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 632 -AHT---RNDANRLQDTIAKVEDEYRAFQ----------EEAKKQIEDLNMTL--------------EKLRSELEEKDTE 683
Cdd:pfam10174 281 kSHSkfmKNKIDQLKQELSKKESELLALQtkletltnqnSDCKQHIEVLKESLtakeqraailqtevDALRLRLEEKESF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 684 RSDMKETIFELEDE--VEQHRAVKLHDNLIISD-----LENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQAD 753
Cdd:pfam10174 361 LNKKTKQLQDLTEEksTLAGEIRDLKDMLDVKErkinvLQKKIENLQEQLRDKDKQLAGLKERvksLQTDSSNTDTALTT 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1720362509 754 LQTAVVIANDI-----------KSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 795
Cdd:pfam10174 441 LEEALSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-805 |
2.52e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 521 LKMAEQDNKEAQEMIGAlkERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS 600
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 601 GDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSELEEK 680
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 681 DTERSDMKETIFELEDEVEQHRAVKlhdnliisdlENTVKKLQDQKHDME--REIKTLHRRLREESAEWRQFQADLQTAV 758
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAE----------EDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1720362509 759 VIANDIKSEAQEEigdlKRRLHEAQ--EKNEKLTKELEEIKSRKQEEER 805
Cdd:PTZ00121 1730 IKAEEAKKEAEED----KKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| CH_AtFIM_like_rpt2 |
cd21296 |
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1018-1089 |
3.78e-03 |
|
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409145 Cd Length: 109 Bit Score: 38.27 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720362509 1018 LLKWC--QKKTEGYQNIdITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKKRNFTLAFQAAESVGIKSTL 1089
Cdd:cd21296 15 LLKWMnfHLKKAGYKKT-VTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEKMNCKRYL 87
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
661-755 |
5.05e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.59 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 661 KQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDeVEQHRAV--KLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 738
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELEL-LDEDTKVykLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
|
90
....*....|....*..
gi 1720362509 739 RLREESAEWRQFQADLQ 755
Cdd:pfam01920 81 QLEKLEKELEELKEELY 97
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-674 |
5.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 413 EELQATLQELADLQQITQELNSENERLgeekvilmeslcqqSDKLEHFGRQIEYFRSLLDehhISYVIDEdvksgrYMEL 492
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDAL--------------QERREALQRLAEYSWDEID---VASAERE------IAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 493 EQRYMDL-AENARFE--REQLLGVQQhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIES--------EQKGKAALAA 561
Cdd:COG4913 674 EAELERLdASSDDLAalEEQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 562 TLEEYKATVASDQIE----------MNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDL 631
Cdd:COG4913 750 LLEERFAAALGDAVErelrenleerIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1720362509 632 AHTRNDANRL--QDTIAKVED---EYRAFQEEAKKQIEDLNMTLEKLR 674
Cdd:COG4913 830 PEYEERFKELlnENSIEFVADllsKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
487-807 |
5.64e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.65 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 487 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQdnkEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEy 566
Cdd:pfam07888 73 RQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE---LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLER- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 567 katvasdQIEMNRLKaqlenEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIA 646
Cdd:pfam07888 149 -------ETELERMK-----ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 647 KVEDEYrafqEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQ--HRAVKLHdnliisdlentvkKLQD 724
Cdd:pfam07888 217 TLTQKL----TTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQrdRTQAELH-------------QARL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 725 QKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL--EEIKSRKQE 802
Cdd:pfam07888 280 QAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELgrEKDCNRVQL 359
|
....*
gi 1720362509 803 EERGR 807
Cdd:pfam07888 360 SESRR 364
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
655-822 |
5.77e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 655 FQEEAKKQIEDLNMTLEKLRSELEEKDTERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIK 734
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 735 TLHRRLR---EESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLheAQEKNEKLTKELEEIksrkqEEERGRVYNY 811
Cdd:TIGR02169 741 ELEEDLSsleQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKL-----EEEVSRIEAR 813
|
170
....*....|.
gi 1720362509 812 MNAVERDLAAL 822
Cdd:TIGR02169 814 LREIEQKLNRL 824
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-593 |
5.81e-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: 40.52 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 397 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEkvilmesLCQQSDKLEHFGRQiEYFRSLLDehhi 476
Cdd:COG4942 60 LERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE-------LAELLRALYRLGRQ-PPLALLLS---- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 477 SYVIDEDVKSGRYMEleqrymDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGK 556
Cdd:COG4942 128 PEDFLDAVRRLQYLK------YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720362509 557 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE 593
Cdd:COG4942 202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
349-805 |
6.02e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 349 ECSEVYQPLTSSDDALDAPSSSESEGVPSIERSRKGSsgNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQI 428
Cdd:PTZ00121 1113 EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKA 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 429 TQELNSENERLGEEkvilmeslcqqSDKLEHFgRQIEYFRSLLDEHHISYVidEDVKSGRYMELEQRYMDLAENARFERE 508
Cdd:PTZ00121 1191 EELRKAEDARKAEA-----------ARKAEEE-RKAEEARKAEDAKKAEAV--KKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 509 QLLGVQQHLSNTLKMAE-QDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQlenE 587
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---A 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 588 KQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAEtlASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEEAKKQIEDLN 667
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE--AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELK 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 668 MTLEKLRSELEEKdtERSDMKETIFELEDEVEQHRAVklhdnliisdlENTVKKLQDQKHDMEREIKTLHRRLREESAEw 747
Cdd:PTZ00121 1412 KAAAAKKKADEAK--KKAEEKKKADEAKKKAEEAKKA-----------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK- 1477
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720362509 748 rqfqadlqtavviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIK----SRKQEEER 805
Cdd:PTZ00121 1478 -----------------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadeAKKAEEAK 1522
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
617-741 |
7.26e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 617 KEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEE------AKKQIEDLNMTL-----EKLRSELEE---KDT 682
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEElrqlkqLEDELEDCDPTEldrakEKLKKLLQEimiKVK 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720362509 683 ERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENtvKKLQDQKHDmEREIKTLHRRLR 741
Cdd:smart00787 226 KLEELEEELQELESKIEDLTNKKSELNTEIAEAEK--KLEQCRGFT-FKEIEKLKEQLK 281
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
604-804 |
9.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 604 SDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDTIAKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSELEEK 680
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAElaqAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720362509 681 DTERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVI 760
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1720362509 761 ANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 804
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
|
| |
