|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
980-1091 |
1.67e-80 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 257.65 E-value: 1.67e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 980 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGI 1059
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 987976890 1060 KPSLELSEMLHTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
980-1091 |
2.30e-76 |
|
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: 246.12 E-value: 2.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 980 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGI 1059
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 987976890 1060 KPSLELSEMLHTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
974-1092 |
4.10e-69 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 226.49 E-value: 4.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 974 RDPLAALAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEA 1053
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 987976890 1054 AESVGIKPSLELSEMLHTDRPDWQSVMQYVAQIYKYFET 1092
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
987-1090 |
4.49e-35 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 129.40 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEL 1065
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
989-1090 |
4.48e-34 |
|
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: 126.30 E-value: 4.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 989 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSE 1067
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 987976890 1068 MLH-TDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21200 83 MVRmGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
992-1090 |
1.26e-31 |
|
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: 119.45 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 992 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELSEMLHT 1071
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 987976890 1072 DRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
990-1090 |
7.81e-31 |
|
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: 117.00 E-value: 7.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 990 NALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEM 1068
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 987976890 1069 LHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
987-1090 |
1.52e-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: 116.36 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIkPSLEL 1065
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGI-AKLLD 80
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
983-1090 |
7.27e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 114.55 E-value: 7.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 983 EYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFE-AAESVGIKP 1061
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 987976890 1062 SLELSEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
987-1090 |
1.83e-29 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 113.26 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1065
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
987-1088 |
1.93e-29 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 113.16 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPS-LEL 1065
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQlLDV 80
|
90 100
....*....|....*....|...
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYK 1088
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
991-1091 |
2.07e-28 |
|
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: 110.13 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 991 ALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEML 1069
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 987976890 1070 HTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
987-1090 |
4.80e-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: 109.32 E-value: 4.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1065
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
989-1088 |
7.85e-28 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 109.02 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 989 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVG-IKPSLELSE 1067
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 987976890 1068 MLHTDRPDWQSVMQYVAQIYK 1088
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
987-1090 |
1.30e-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: 108.21 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1065
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 987976890 1066 SEML-HTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21258 81 EDMMiMGKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
988-1090 |
1.35e-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: 104.93 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 988 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLELS 1066
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
992-1090 |
1.59e-26 |
|
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: 104.93 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 992 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELSEMLHT 1071
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 987976890 1072 DRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
987-1090 |
4.34e-26 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 103.79 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1065
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLD- 82
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
987-1091 |
4.60e-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: 103.33 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELS 1066
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
987-1090 |
1.12e-25 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 102.35 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESV-GIKPSLEL 1065
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 987976890 1066 SEMLHTDR-PDWQSVMQYVAQIYKYF 1090
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
987-1090 |
1.17e-25 |
|
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: 102.08 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1065
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21189 80 PEDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
989-1090 |
5.44e-24 |
|
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: 97.63 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 989 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSE 1067
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 987976890 1068 MLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
986-1091 |
6.99e-24 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 97.11 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 986 GSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1064
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 987976890 1065 LSEMLhTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
987-1091 |
7.76e-24 |
|
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: 97.33 E-value: 7.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEL 1065
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
985-1091 |
8.58e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 97.03 E-value: 8.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 985 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSL 1063
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 987976890 1064 ELSEMLHTDRPDWQSVMQYVAQIYKYFE 1091
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
987-1090 |
1.86e-22 |
|
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: 93.18 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLElS 1066
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82
|
90 100
....*....|....*....|....
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
988-1090 |
2.43e-22 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 93.02 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 988 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLELS 1066
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
987-1090 |
2.88e-22 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 93.20 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1065
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
992-1088 |
4.68e-22 |
|
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: 92.11 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 992 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAA-ESVGIKPSLElSEMLH 1070
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 987976890 1071 TDRPDWQSVMQYVAQIYK 1088
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
989-1092 |
2.80e-21 |
|
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: 90.04 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 989 RNALLKWCQKKTEGY-ANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKR--NLLLAFEAAE-SVGIKPSLE 1064
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83
|
90 100
....*....|....*....|....*...
gi 987976890 1065 LSEMLHTdrPDWQSVMQYVAQIYKYFET 1092
Cdd:pfam00307 84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
987-1090 |
3.32e-21 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 90.14 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1065
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
987-1090 |
7.42e-21 |
|
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: 89.34 E-value: 7.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1065
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
987-1090 |
1.69e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 87.85 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1065
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
985-1090 |
3.26e-20 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 86.99 E-value: 3.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 985 GGSKRnALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIkPSL 1063
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI-PRL 81
|
90 100
....*....|....*....|....*..
gi 987976890 1064 ELSEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
987-1090 |
4.21e-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: 87.06 E-value: 4.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1065
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
991-1090 |
5.03e-20 |
|
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: 85.98 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 991 ALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEmL 1069
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 987976890 1070 HTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
987-1090 |
5.71e-20 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 86.70 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1065
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
987-1090 |
1.53e-19 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 85.51 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1065
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
987-1090 |
2.89e-18 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 81.19 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLElS 1066
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
990-1086 |
4.76e-18 |
|
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: 80.44 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 990 NALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY----QELSSQEKKRNLLLAFEAAESVGIKPSLEL 1065
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQI 1086
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
974-1092 |
1.46e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 84.61 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 974 RDPLAALAREYGGSKRNALLKWCQKKTEGYAN-IDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQ--EKKRNLLLA 1050
Cdd:COG5069 112 RLTIATINEEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 987976890 1051 FEAAE-SVGIKPSLELSEMLHTDRPDWQSVMQYVAQIYKYFET 1092
Cdd:COG5069 192 FENANkVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
989-1088 |
2.12e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 75.84 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 989 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY---QELSSQEKKRNLLLAFEAAESVGIKPS--L 1063
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 987976890 1064 ELSEMLhtDRPDWQSVMQYVAQIYK 1088
Cdd:cd00014 81 EPEDLY--EKGNLKKVLGTLWALAL 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
987-1085 |
7.23e-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: 74.20 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYAnidITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1064
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|.
gi 987976890 1065 LSEMLHTDrPDWQSVMQYVAQ 1085
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLSY 97
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
987-1090 |
1.54e-15 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 73.72 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELS 1066
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
|
90 100
....*....|....*....|....
gi 987976890 1067 EMLHTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21244 85 EDVDVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
991-1090 |
3.36e-15 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 72.52 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 991 ALLKWCQKKTEGYAnIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAA-ESVGIKPSLElSEML 1069
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 987976890 1070 HTDRPDWQSVMQYVAQIYKYF 1090
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-723 |
2.18e-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: 78.17 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 353 STTGSSPNNASELS----LASLTEKIQKMEENhhstAEELQATLQELSDQQQmvqELTAENEKLVDEKTILETSFHQHRE 428
Cdd:TIGR02168 661 ITGGSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 429 RAEQLSHENEKLINLLQErvkkeepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcslrKAEEENQGAAEMIQR 508
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQ---------LSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 509 LKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLE-NEKQKAIVTSSMGQTAEGC-EIQEMLKVARA 586
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEeLSEDIESLAAEIEELEELIeELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 587 EKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 666
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976890 667 DQVE-----QHRAVKLHNNQL----------ITELESSVMK---LEGQKADLERQLKTLTKQIKEETEEWR-RFQA 723
Cdd:TIGR02168 961 NKIEddeeeARRRLKRLENKIkelgpvnlaaIEEYEELKERydfLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
990-1085 |
1.29e-13 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 67.71 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 990 NALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTyLPAHIP-YQELSSQEKKRNLLLAFEAAESVGIKPSLELSEM 1068
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 987976890 1069 lhTDrPDWQS--VMQYVAQ 1085
Cdd:cd21185 80 --AD-PEVEHlgIMAYAAQ 95
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
985-1091 |
1.30e-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: 68.15 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 985 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSL 1063
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90 100
....*....|....*....|....*...
gi 987976890 1064 ELSEMLHTDRPdwQSVMQYVAQIYKYFE 1091
Cdd:cd21196 81 SAQAVVAGSDP--LGLIAYLSHFHSAFK 106
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
992-1088 |
2.43e-13 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 67.26 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 992 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKK-RNLLLAFEAAE-SVGIKPSLElSEML 1069
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 987976890 1070 HTDRPDWQSVMQYVAQIYK 1088
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
987-1087 |
3.12e-12 |
|
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: 63.89 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1065
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 987976890 1066 SEMLHTDRPDWQSVMQYVAQIY 1087
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
990-1084 |
4.85e-12 |
|
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: 64.63 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 990 NALLKWCQKKTEGYaNIDITNFSSSWSDGLAFCALLHTYLPAHIP----------------------------------- 1034
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 987976890 1035 -YQELSSQEkKRNLLLAFEAAESVG-IKPSLELSEMLHTdRPDWQSVMQYVA 1084
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELGgVPALLRASDMSNT-IPDEKVVILFLS 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
373-762 |
2.35e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 373 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSHENEKlinlLQERVKKEE 452
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 453 PGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRKAEEENQGA---AEMIQRLKEENEKLNGLLELERQNSGV 529
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK-ELKKAIEELKKAkgkCPVCGRELTEEHRKELLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 530 mAQTLEECTVTLEGLKIENGSLKAYLENEKQkaivTSSMGQTAEGC-EIQEMLKVARAEKdqLELSCTE---LKQELLKA 605
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLkELEEKLKKYNLEE--LEKKAEEyekLKEKLIKL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 606 HGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQVEQH 672
Cdd:PRK03918 538 KGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 673 RAVKLHNNQLITELESSVMKLEGQKADLER---QLKTLTK--------QIKEETEEWRRFQADLQTAVVVANDIKCEAQQ 741
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
410 420
....*....|....*....|.
gi 987976890 742 ELRTVKRRLLEEEEKNARLQK 762
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK 715
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
992-1088 |
5.14e-11 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 60.36 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 992 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLElSEMLH 1070
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 987976890 1071 TDRPDWQSVMQYVAQIYK 1088
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-764 |
5.93e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 457 EGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEE 536
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 537 CTVTLEGLKIENGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLL 616
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEE----------------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 617 AKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQ 696
Cdd:TIGR02168 827 ESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976890 697 KADLERQLKTLTKQIKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKEL 764
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
386-779 |
3.57e-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: 64.32 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 386 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSHENEKLINLLQERVKKEEpgtQEGKVLELEQ 465
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYQALLKEKRE---YEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 466 KCTEI-LEQGRCEREkllSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLElERQNSgvMAQTLEECTVTLEGL 544
Cdd:TIGR02169 233 EALERqKEAIERQLA---SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLR--VKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 545 KienGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS 624
Cdd:TIGR02169 307 E---RSIAEKERELED----------------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 625 YLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQL 704
Cdd:TIGR02169 368 DLRA----ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 987976890 705 KTLTKQIKEETEEWRRFQADLQTAVVVANDIKceaqQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 779
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-764 |
4.04e-10 |
|
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: 64.22 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENE------K 439
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 440 LINLLQERVKKEEPGTQEGKVLELEQKCTEIleqgRCEREKLLSIQQQLTcslrkaeEENQGAAEMIQRLKEENEKLNGL 519
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINR----ARKAAPLAAHIKAVT-------QIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 520 LElERQNSGVMAQTLEECTVTLEGLKIENGSLKayLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTE-- 597
Cdd:TIGR00618 327 LM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIR--DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEld 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 598 ------------------LKQELLKAHGEIKhvssllakVEKDYSYLKEI---CDHQAEQLSRTSL-KLQEKASESDAEI 655
Cdd:TIGR00618 404 ilqreqatidtrtsafrdLQGQLAHAKKQQE--------LQQRYAELCAAaitCTAQCEKLEKIHLqESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 656 KDmKETIFELED---QVEQHRAVKLHNNQ-------------------------LITELESSVMKLEGQKADLERQLKTL 707
Cdd:TIGR00618 476 QT-KEQIHLQETrkkAVVLARLLELQEEPcplcgscihpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 987976890 708 TKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEEEEKNARLQKEL 764
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
478-786 |
5.20e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 478 REKLLSIQQQLTCSLR----KAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQT---LEECTVTLEGLKIENGS 550
Cdd:TIGR02168 199 ERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 551 LkayleNEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIC 630
Cdd:TIGR02168 279 L-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 631 DHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTL 707
Cdd:TIGR02168 354 ESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 708 TKQ--------IKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 779
Cdd:TIGR02168 434 ELKelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
....*..
gi 987976890 780 PEADAPG 786
Cdd:TIGR02168 514 NQSGLSG 520
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
361-768 |
1.82e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERA 430
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 431 EQLSHENEKL-------------INLLQERVKKEEPGTQEgKVLELEQKCTEILEQGRCEREKLLSIQQQ---------- 487
Cdd:PRK02224 289 EELEEERDDLlaeaglddadaeaVEARREELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADDLEERaeelreeaae 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 488 LTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEK-------- 559
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaea 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 560 -QKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSlLAKVEKDYSYLKE-------ICD 631
Cdd:PRK02224 448 lLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEErredleeLIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 632 HQAEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEgqkaDLERQLKTLT 708
Cdd:PRK02224 527 ERRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAIA 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 709 kQIKEETEEWRRFQADLQTavvvANDIKCEAQQELRTvKRRLLEEEEKNARLQKELGDMQ 768
Cdd:PRK02224 603 -DAEDEIERLREKREALAE----LNDERRERLAEKRE-RKRELEAEFDEARIEEAREDKE 656
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
363-770 |
2.70e-09 |
|
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: 61.73 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 363 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL-- 440
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 441 -INLLQERVKKEEPGTQ---------EGKVLELEQKCTEILEQ-GRCEREKLLSIQQQLTCSLRKAEEENQgaAEMIQRL 509
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEK--AKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 510 KEENEKLNGLLELERQNSGVMAQTLEECTVTLEG-----------LKIENGSLKAYL---ENEKQKAIVTSSMGQTAEG- 574
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaeLQAQIAELRAQLakkEEELQAALARLEEETAQKNn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 575 ------------CEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKH-VSSLLAKVEkdysyLKEICDHQAEQLSRTs 641
Cdd:pfam01576 262 alkkireleaqiSELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtLDTTAAQQE-----LRSKREQEVTELKKA- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 642 lkLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliTELESSVMKLEGQKADLERQLKTLTkQIKEETEE 717
Cdd:pfam01576 336 --LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQDSEH 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 987976890 718 WRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRRLLEEEEKNARLQKELGDMQGH 770
Cdd:pfam01576 406 KRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-717 |
3.78e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSHENEK 439
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 440 LINLLQERVKKEEpgTQEGKVLELEQKCTEIleqgrceREKLLSIQQQltcslrKAEEENQGAAEMIQRLKEENEKLNGL 519
Cdd:TIGR04523 265 IKKQLSEKQKELE--QNNKKIKELEKQLNQL-------KSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 520 LELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLEnEKQKAIVTssmgqtaEGCEIQEMLKvaraEKDQLELSCTELK 599
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-EKQNEIEK-------LKKENQSYKQ----EIKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 600 QELLKAHGEIKHVSSLLAKVEKDYsylkeicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 679
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEK-----------ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350
....*....|....*....|....*....|....*...
gi 987976890 680 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEE 717
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
987-1085 |
4.12e-09 |
|
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: 55.08 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTEGyanIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1064
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|.
gi 987976890 1065 LSEMLHTDrPDWQSVMQYVAQ 1085
Cdd:cd21230 78 PEEIINPN-VDEMSVMTYLSQ 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-635 |
4.71e-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: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETS---FHQHRERAEQLSHEN 437
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeLESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 438 EKLINLLQERVK--KEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRK----AEEENQGAAEMIQRLKE 511
Cdd:TIGR02168 343 EEKLEELKEELEslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA-SLNNeierLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 512 ENEKLNGLLELERqnsgvmaqtLEECTVTLEGLKIENGSLKAYLEnekqkaivtssmgqtaegcEIQEMLKVARAEKDQL 591
Cdd:TIGR02168 422 EIEELLKKLEEAE---------LKELQAELEELEEELEELQEELE-------------------RLEEALEELREELEEA 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 987976890 592 ELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAE 635
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
386-735 |
7.48e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 7.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 386 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSHENEKLINLLQER-VKKEEPGTQEGKVLELE 464
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 465 QKCTEILEQgrcerekllsiQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL-ELERQNSGV------MAQTLEEC 537
Cdd:TIGR04523 398 SKIQNQEKL-----------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSVKeliiknLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 538 TVTLEGLKIENGSLKAYLENEKQ--KAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSL 615
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 616 LAKV--EKDYSYLKEICDHQAEQLSR-----TSLK-----LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 683
Cdd:TIGR04523 547 LNKDdfELKKENLEKEIDEKNKEIEElkqtqKSLKkkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 987976890 684 TELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 735
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-624 |
8.94e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL 440
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 441 INLLQERVKKEEpgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLtcsLRKAEEENQGAAEMIQRLKEENEKLNGLL 520
Cdd:COG1196 329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 521 ELERQNSGvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAivTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQ 600
Cdd:COG1196 404 ELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|....
gi 987976890 601 ELLKAHGEIKHVSSLLAKVEKDYS 624
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-621 |
1.64e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEK 439
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 440 LINLLQERVKK-----EEPGTQEGKVLELEQKCTEILEQGrcerEKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENE 514
Cdd:TIGR02168 321 LEAQLEELESKldelaEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 515 KLNGllELERqnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELS 594
Cdd:TIGR02168 397 SLNN--EIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260
....*....|....*....|....*..
gi 987976890 595 CTELKQELLKAHGEIKHVSSLLAKVEK 621
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLER 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
366-763 |
1.97e-08 |
|
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: 58.93 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 366 SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLShenEKLINLLQ 445
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE---EDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 446 ERV-KKEEPGTQEGKVLELEQKCTEI-LEQGRCEREKLLSIQQQLTCSLRKAEEENQgaaEMIQRLKEENEKLNGLLEle 523
Cdd:TIGR02169 752 EIEnVKSELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTL-- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 524 rqnsgvmaqtleectvtleglkiengsLKAYLENEKQKAIvtssmgqtAEGCEIQEMLKVARAEKDQLELSCTELKQELL 603
Cdd:TIGR02169 827 ---------------------------EKEYLEKEIQELQ--------EQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 604 KAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 683
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERD------------------ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 684 TELESSVMKLEGQKADlERQLKTLTKQIKEETEEWRRFQadlqtavvvanDIKCEAQQELRTVKRRLLEEEEKNARLQKE 763
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-761 |
2.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEENHHSTAEELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLL 444
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 445 QERVKKEEPGTQEGKVLELEQKctEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELER 524
Cdd:COG4717 170 AELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 525 QNSGVMAQTLeecTVTLEGLKIENGSLK----------------AYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAE- 587
Cdd:COG4717 248 ARLLLLIAAA---LLALLGLGGSLLSLIltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 588 KDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQEKASESDAEIKDMKETI 662
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 663 FELEDQVEQHRAVKLHNNQLITELEssvmkLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVvvANDIKCEAQQE 742
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLE--EDGELAELLQE 477
|
410
....*....|....*....
gi 987976890 743 LRTVKRRLLEEEEKNARLQ 761
Cdd:COG4717 478 LEELKAELRELAEEWAALK 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-779 |
2.30e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCtELKQELLKAHGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 650
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 651 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAV 729
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 987976890 730 VVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 779
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
504-785 |
2.88e-08 |
|
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: 58.16 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 504 EMIQRLKEENEKLNGLL-----ELERQNSGVMA--QTLEECTVTLEGLKIENGSLKAYLENEKQK-AIVTSSMGQTAEGC 575
Cdd:TIGR02169 674 AELQRLRERLEGLKRELsslqsELRRIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERlEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 E-IQEMLKVARAEKDQLELSCTELKQELLK-----AHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslKLQEKAS 649
Cdd:TIGR02169 754 EnVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR---LTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 650 ESDaEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAV 729
Cdd:TIGR02169 831 LEK-EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 987976890 730 VVANdiKCEAQQELRTVKRRLLEEEEknarlqKELGDMQGHGRPvraESEPEADAP 785
Cdd:TIGR02169 910 AQIE--KKRKRLSELKAKLEALEEEL------SEIEDPKGEDEE---IPEEELSLE 954
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
576-764 |
3.54e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 3.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslkLQEKASESDAEI 655
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 656 KDMKETIFELEDQVEQHRAVKLhnnQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 735
Cdd:COG1196 326 AELEEELEELEEELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180
....*....|....*....|....*....
gi 987976890 736 KcEAQQELRTVKRRLLEEEEKNARLQKEL 764
Cdd:COG1196 403 E-ELEEAEEALLERLERLEEELEELEEAL 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
364-765 |
5.66e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 364 ELSLASLTEKIQKMEENHHSTAEELQAT---LQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLshenEKL 440
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL----KKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 441 INLLQERVKKEEpgtqegkvlELEQKCTEILEQGRcEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL 520
Cdd:PRK03918 275 IEELEEKVKELK---------ELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 521 ELERQNSGVMAQtLEECTVTLEGLKiengSLKAYLENEKQKAivtssMGQTAEgcEIQEMLKVARAEKDQLELSCTELKQ 600
Cdd:PRK03918 345 KKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRL-----TGLTPE--KLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 601 ELLKAHGEIKHVSSLLAKVEKdysyLKEIC---------DHQAEQLSRTSLKL---QEKASESDAEIKDMKETIFELEDQ 668
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK----AKGKCpvcgrelteEHRKELLEEYTAELkriEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 669 VEQHRAVkLHNNQLITELESSVMKLEgqKADLErQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKR 748
Cdd:PRK03918 489 LKKESEL-IKLKELAEQLKELEEKLK--KYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEK 563
|
410
....*....|....*..
gi 987976890 749 RLLEEEEKNARLQKELG 765
Cdd:PRK03918 564 KLDELEEELAELLKELE 580
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
361-753 |
8.60e-08 |
|
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: 56.67 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAEneklvdektiletsfHQHRERA-EQLSHENEK 439
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS---------------LQEKERAiEATNAEITK 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 440 LINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGL 519
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 520 LELERQNSGVMAQTLEECTVTLEGlKIENgslkayLENEKQKAIVTSSmgqtaegceiqEMLkvaRAEKDqlelscteLK 599
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEA-RVSD------LELEKVKLVNAGS-----------ERL---RAVKD--------IK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 600 QELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 679
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 987976890 680 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEE 753
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-700 |
1.50e-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: 55.84 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTaENEKLVDEKTILEtsFHQHRERAEQLSHENEKLINLLQE 446
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-EEEQLRVKEKIGE--LEAEIASLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 447 RVKK--EEPGTQEGKVLELEQKcteiLEQGRCEREKLLSI----QQQLTCSLRKAEEENQGAAEMIQRLKEENEKLngll 520
Cdd:TIGR02169 323 RLAKleAEIDKLLAEIEELERE----IEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKL---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 521 elerqnsgvmaqtleectvtlEGLKIENGSLKA---YLENEKQKAivtssmgqTAEGCEIQEMLKVARAEKDQLELSCTE 597
Cdd:TIGR02169 395 ---------------------EKLKREINELKReldRLQEELQRL--------SEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 598 LKQELLKAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKL 677
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELY------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340
....*....|....*....|...
gi 987976890 678 HNNQLITELESSVMKLEGQKADL 700
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQL 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
423-784 |
3.71e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 423 FHQHRERAEQLSHEneklINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRKAEEENQGA 502
Cdd:COG1196 215 YRELKEELKELEAE----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 503 -AEMIQRLKEENEKLNGLLELERQNsgvmAQTLEEctvtlegLKIENGSLKAYLENEKQKAIvtssmgqtaegcEIQEML 581
Cdd:COG1196 290 eYELLAELARLEQDIARLEERRREL----EERLEE-------LEEELAELEEELEELEEELE------------ELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 582 KVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKET 661
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 662 IFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIK-CEAQ 740
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEAD 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 987976890 741 QELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESEPEADA 784
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
356-761 |
8.79e-07 |
|
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: 53.44 E-value: 8.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 356 GSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSH 435
Cdd:pfam02463 129 GISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 436 ENEKLINLLQERVKKEEPgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEK 515
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYL-LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 516 LNGLLELERQNSGVMAQtLEECTVT----LEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQL 591
Cdd:pfam02463 288 LKLLAKEEEELKSELLK-LERRKVDdeekLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 592 ELScTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQ 671
Cdd:pfam02463 367 KLE-QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 672 HRAVKLH-NNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQElRTVKRRL 750
Cdd:pfam02463 446 LTEEKEElEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK-DGVGGRI 524
|
410
....*....|.
gi 987976890 751 LEEEEKNARLQ 761
Cdd:pfam02463 525 ISAHGRLGDLG 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
576-789 |
2.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEI 655
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 656 KDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVANDI 735
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAERQKL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 987976890 736 KCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGH--GRPVRAESEPEADAPGRWP 789
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEaaAAAERTPAAGFAALKGKLP 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
576-871 |
2.90e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEK-ASESDAE 654
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSgGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 655 IKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVAND 734
Cdd:COG3883 107 VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 735 IKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGhGRPVRAESEPEADAPGRWPGIFASRASAAPLEPATTVKSLIKSF 814
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA-AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 987976890 815 DLGHPGGAGQNVSVHKPPRSPLSGIPVRTAPAAAVSPMQRHSTYSGVRPASKGVAQR 871
Cdd:COG3883 262 AGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGG 318
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
992-1064 |
3.02e-06 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 47.29 E-value: 3.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 987976890 992 LLKWCQK--KTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIP----YQELSSQEKKRNLLLAFEAAESVGIKPSLE 1064
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLT 93
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
372-779 |
5.83e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 372 EKIQKMEENHHSTAEELQATLQELSDQQQMVQEltAENEKLVDE--KTILETSFHQHRERAEQLSHENEKLINLLQERVK 449
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 450 KEE---PGTQEGKVLELEQKCTEilEQGRCEREKLLSIQQQLTCSLRKAEEENQgAAEMiqRLKEENEKLNGLLELERQN 526
Cdd:PTZ00121 1472 ADEakkKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKKAEEAKK-ADEA--KKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 527 SGVMAQTLEECTVTLEGLKIENgslKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKdqlelsctELKQELLKAH 606
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEE---AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK--------KMKAEEAKKA 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 607 GEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSlklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHnnqlitEL 686
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------ED 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 687 ESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNaRLQKELGD 766
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKE 1765
|
410
....*....|...
gi 987976890 767 MQGHGRPVRAESE 779
Cdd:PTZ00121 1766 EEKKAEEIRKEKE 1778
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
987-1088 |
1.21e-05 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 45.47 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1064
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCPdWESWDPQKPVDNAREAMQQADDwLGVPQVIT 84
|
90 100
....*....|....*....|....
gi 987976890 1065 LSEMLHTDrPDWQSVMQYVAQIYK 1088
Cdd:cd21313 85 PEEIIHPD-VDEHSVMTYLSQFPK 107
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
348-763 |
1.43e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 348 KSSKCSTTGSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELT-----------------AENE 410
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 411 KLVDEKTiletsfhQHRERAEQLSHENEKLINLLQERVKK-EEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLT 489
Cdd:pfam05483 419 KLLDEKK-------QFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 490 CSLRKAEEEN----QGAAEMIQRLKEENEKLNGLLELERQnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVT 565
Cdd:pfam05483 492 AHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 566 SSMGQTAEGCEIQEMLKVARAEKdQLELSCTELK----------QELLKAHGEIKHVSSLLAKVEKDYsylkEICDHQAE 635
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMK-ILENKCNNLKkqienknkniEELHQENKALKKKGSAENKQLNAY----EIKVNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 636 -QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKE 713
Cdd:pfam05483 643 lELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEE 722
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 987976890 714 ETEEWRRFQADLQTAVVVANDIKCE---AQQELRTVKRRLLEEEEKNARLQKE 763
Cdd:pfam05483 723 RDSELGLYKNKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
342-733 |
1.93e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 342 STSNPFKSSKCSTTGSSPNNASE--LSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTIL 419
Cdd:COG5185 190 KGISELKKAEPSGTVNSIKESETgnLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 420 ETS-FHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCERE---KLLSIQQQLTCSLRKA 495
Cdd:COG5185 266 RLEkLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 496 EEENQGAAEMIQRLKEENEKLNGLLELERQnsgvmAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmgqtaegc 575
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSKS-----SEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 eIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYsylkeicdhQAEQLSRTSLKLQEKASESDAEI 655
Cdd:COG5185 411 -LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA---------DEESQSRLEEAYDEINRSVRSKK 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976890 656 KDMKETIFELEDQVEQHRAvklhnnqlitelessvmKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVAN 733
Cdd:COG5185 481 EDLNEELTQIESRVSTLKA-----------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
372-764 |
2.01e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 372 EKIQKMEENHHSTAEELQATLQE----LSDQQQMVQELTAENEKLvdeKTILETSFHQHRERAEQlSHENEKLINLLQER 447
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKV---SLKLEEEIQENKDLIKE-NNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 448 VKKEEPGTQEgkvLELEQKCT-EILEQGRCEREKLLSIQQQLtcslrKAEEENqGAAEMIQRLKEENEKLNGLLE----- 521
Cdd:pfam05483 164 CARSAEKTKK---YEYEREETrQVYMDLNNNIEKMILAFEEL-----RVQAEN-ARLEMHFKLKEDHEKIQHLEEeykke 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 522 ---LERQNSGVMAQTLEEctvtleglkiengslkaylENEKQkaivtssmgqtaegcEIQEMLKVARAEKDQLELScTEL 598
Cdd:pfam05483 235 indKEKQVSLLLIQITEK-------------------ENKMK---------------DLTFLLEESRDKANQLEEK-TKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 599 KQELLKAHGEIKHvssllakvekdysylkeicdHQAEQLSRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQ 671
Cdd:pfam05483 280 QDENLKELIEKKD--------------------HLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 672 HRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KR 748
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDE 418
|
410
....*....|....*.
gi 987976890 749 RLLEEEEKNARLQKEL 764
Cdd:pfam05483 419 KLLDEKKQFEKIAEEL 434
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
367-751 |
2.14e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLvdEKTILETSfHQHRERAEQLshenEKLINLLQE 446
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL--RKSLLANR-FSFGPALDEL----EKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 447 RVKKEEPGTQEGKVLEleqkcteileqgrcerekllsiqqqltcslrkaeeenqgAAEMIQRLKEENEKLNGLLElerqn 526
Cdd:PRK04778 180 EFSQFVELTESGDYVE---------------------------------------AREILDQLEEELAALEQIME----- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 527 sgVMAQTLEECTVTLEGL--KIENGslkaYLENEKQKAIVTSsmgQTAEGcEIQEML-KVARAEKDQLELSCTELKQELL 603
Cdd:PRK04778 216 --EIPELLKELQTELPDQlqELKAG----YRELVEEGYHLDH---LDIEK-EIQDLKeQIDENLALLEELDLDEAEEKNE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 604 KAHGEIKHVSSLLakvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQL 682
Cdd:PRK04778 286 EIQERIDQLYDIL---EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-YTLnESELESVRQLEKQLESL 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976890 683 ITELESSVMKLEGQKA-------DLERQLKTLTkQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 751
Cdd:PRK04778 361 EKQYDEITERIAEQEIayselqeELEEILKQLE-EIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
361-768 |
3.28e-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: 48.12 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 361 NASELSLASLTEKIQKMEEN-HHSTAEELQATLQELS------------DQQQMVQELTAENEKLVDEKTILETSFHQHR 427
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNkNHINNELESKEEQLSSyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 428 ERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLE-------LEQKCTE-ILEQGRCEREKLL-------SIQQQLTCSL 492
Cdd:TIGR00606 667 QFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQsklrlapDKLKSTEsELKKKEKRRDEMLglapgrqSIIDLKEKEI 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 493 RKAEEENQGAAEMIQRLKeeneklNGLLELERQNSGVMAQtLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTA 572
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLK------NDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 573 EGCEIQEMLKVARAEKDQLE--LSCTELKQELLKAHGE-IKHVSSLLAKVEKDYSYLKEICdHQAEQLSRTSLKLQEKAS 649
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDtvVSKIELNRKLIQDQQEqIQHLKSKTNELKSEKLQIGTNL-QRRQQFEEQLVELSTEVQ 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 650 ESDAEIKDMKETIFELE-----DQVEQHRAV-KLHNNQLITELESSVMK--------------------LEGQKADLERQ 703
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLEtflekDQQEKEELIsSKETSNKKAQDKVNDIKekvknihgymkdienkiqdgKDDYLKQKETE 978
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 987976890 704 LKTLTKQIKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRRLLEEEEKNARLQKELGDMQ 768
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
985-1085 |
7.28e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 43.23 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 985 GGSKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAESVGIKPSL 1063
Cdd:cd21315 14 GPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDWLDVPQL 90
|
90 100
....*....|....*....|..
gi 987976890 1064 ELSEMLHTDRPDWQSVMQYVAQ 1085
Cdd:cd21315 91 IKPEEMVNPKVDELSMMTYLSQ 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
493-764 |
8.03e-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: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 493 RKAEEENQGAAEMIQRLKEENEklnglleLERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEKQ-KAIVTSSMGQT 571
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNE-------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 572 AEGCEIQEMLKvaraeKDQLELSCTELKQ---ELLKAHGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK----- 643
Cdd:pfam15921 151 VHELEAAKCLK-----EDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsa 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 644 LQEKASESDAEIKDMKETIFELEDQVEQHRA---------VKLHNN---QLITELESSVMKL-------EGQKADLERQL 704
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLtekassaRSQANSIQSQL 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 705 KTLTKQIKEETEEWRRFQADLQTAVvvandikCEAQQELRTVKRRLleeEEKNARLQKEL 764
Cdd:pfam15921 302 EIIQEQARNQNSMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
360-668 |
9.51e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.89 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 360 NNASELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHEN 437
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 438 EKLINLLQERVKKEepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLN 517
Cdd:pfam02463 812 EEAELLEEEQLLIE----QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDE 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 518 GLLELERQNsgvmAQTLEECTVTLEGLKIENGSLKaYLENEKQKAIVtssmgQTAEGCEIQEMLKVARAEKDQLELSCTE 597
Cdd:pfam02463 888 LESKEEKEK----EEKKELEEESQKLNLLEEKENE-IEERIKEEAEI-----LLKYEEEPEELLLEEADEKEKEENNKEE 957
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976890 598 LKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 668
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
987-1088 |
3.32e-04 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 41.59 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 987 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIkPSLE 1064
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWESWDPNQPVQNAREAMQQADDwLGV-PQVI 86
|
90 100
....*....|....*....|....
gi 987976890 1065 LSEMLHTDRPDWQSVMQYVAQIYK 1088
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPK 110
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
444-724 |
3.81e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.03 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 444 LQERVKKEEPGTQEGKVLELEqkcTEILEQGRCEREKLLsiqQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNG-LLEL 522
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKE---IRALVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEKqLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 523 ERQNSGVMAQTLEECT-VTLEGLKIENGSLKAYLENeKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLE--LSCTELK 599
Cdd:pfam15905 135 TRVNELLKAKFSEDGTqKKMSSLSMELMKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEekLVSTEKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 600 --------QELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveq 671
Cdd:pfam15905 214 kieeksetEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE----- 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 987976890 672 hravklhnnqliTELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQAD 724
Cdd:pfam15905 289 ------------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
370-765 |
4.09e-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: 44.44 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 370 LTEKIQKMEENHHSTaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVK 449
Cdd:pfam12128 463 LLQLENFDERIERAR-EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 450 KEEPGTQE--GKVLELEQKC-TEI-------------------LEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQ 507
Cdd:pfam12128 542 KEAPDWEQsiGKVISPELLHrTDLdpevwdgsvggelnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 508 RLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLK----AYLENEKQKA---IVTSSMGQTAEGCEIQEM 580
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKdkknKALAERKDSAnerLNSLEAQLKQLDKKHQAW 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 581 LKvarAEKDQLELSCTELKQELLKAHGEIK-HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKL---QEKASESDAEIK 656
Cdd:pfam12128 702 LE---EQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIR 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 657 DMKETIfeleDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 735
Cdd:pfam12128 779 TLERKI----ERIAVRRQEVLRYFDWYQETWLQRRpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
410 420 430
....*....|....*....|....*....|....*
gi 987976890 736 KCEAQQELRTVKRRL-----LEEEEKNARLQKELG 765
Cdd:pfam12128 855 QVRLSENLRGLRCEMsklatLKEDANSEQAQGSIG 889
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
541-783 |
4.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 541 LEGLKIENGSLKAYLENEKQKAIVTSSmgqtaegcEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVE 620
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELD--------KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 621 KDYSYLKEICDHQAEQLSRTSL---KLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQK 697
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEeaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 698 ADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAE 777
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
....*.
gi 987976890 778 SEPEAD 783
Cdd:COG4372 247 DKEELL 252
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
1008-1070 |
4.48e-04 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 39.98 E-value: 4.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976890 1008 ITNFSSSWSDGLAFCALLHTYLP-----AHIPYQELSSQEKKR-NLLLAFEAA-ESVGIKPS-LELSEMLH 1070
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPqlidlEDICLKESMSLADSLyNIQLLQEFCqRHLGNRCChLTLEDLLY 83
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
359-677 |
4.61e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 44.28 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 359 PNNASELSLAsLTEKIQKMEENHHSTAEELQATLQE---LS----DQQQMVQEL--TAE--NEKLVDEKTILET------ 421
Cdd:pfam15070 77 PAGPSEEEQR-LQEEAEQLQKELEALAGQLQAQVQDneqLSrlnqEQEQRLLELerAAErwGEQAEDRKQILEDmqsdra 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 422 ----SFHQHRERAEQL----------SHENEKLINLLQ--ERVKKE------EPGTQEGKVLE-LEQKCTEI--LEQGR- 475
Cdd:pfam15070 156 tisrALSQNRELKEQLaelqngfvklTNENMELTSALQseQHVKKElakklgQLQEELGELKEtLELKSQEAqsLQEQRd 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 476 -----------------CEREKL---LSIQQQLTCSLRKAEEENQGAAEM-IQRLKEENEKLNgllELERQNSGVMAQtL 534
Cdd:pfam15070 236 qylahlqqyvaayqqlaSEKEELhkqYLLQTQLMDRLQHEEVQGKVAAEMaRQELQETQERLE---ALTQQNQQLQAQ-L 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 535 EECTVTLEGLKIENGSLkaylENEKQKAIVTSSmgqtaEGCEIQEMLK------VARAEKDQLELS---------CTELK 599
Cdd:pfam15070 312 SLLANPGEGDGLESEEE----EEEAPRPSLSIP-----EDFESREAMVaffnsaLAQAEEERAELRrqlkeqkrrCRRLA 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976890 600 QELLKAHGEIKHVSSllAKVEKDYSYLKEIcdHQAEQLSRTslKLQEKASESDAEIKDMKETIFELEdqveqHRAVKL 677
Cdd:pfam15070 383 QQAAPAQEEPEHEAH--APGTGGDSVPVEV--HQALQVAME--KLQSRFTELMQEKADLKERVEELE-----HRCIQL 449
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
372-756 |
5.44e-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: 44.27 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 372 EKIQKMEENHHSTAEELQatlQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQE-RVKK 450
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 451 EEPGTQEGKVLELEQKCTEILEQGRCEREkllsiqqqltcslrkAEEENQGAAEMIQRLKEENEKLNgllELERQNSGvM 530
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDE---------------AKTAAQLCADLQSKERLKQEQAD---EIRDEKKG-L 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 531 AQTLEECTVTLEglkiengslkaylenekqkaivtssmgqtaegcEIQEMLKVARAEKDQLELSCT---ELKQELLKAHG 607
Cdd:TIGR00606 439 GRTIELKKEILE---------------------------------KKQEELKFVIKELQQLEGSSDrilELDQELRKAER 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 608 EIkhvsSLLAKVEKDYSYLKEICDHQAEQ--LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITE 685
Cdd:TIGR00606 486 EL----SKAEKNSLTETLKKEVKSLQNEKadLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976890 686 LESSVMKLEGQKAdLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKceaqQELRTVKRRLLEEEEK 756
Cdd:TIGR00606 562 LTSLLGYFPNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN----NELESKEEQLSSYEDK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
367-717 |
6.83e-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: 43.80 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEEnhhstaeELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhRERAEQLSHENEKLINLLQE 446
Cdd:TIGR00618 551 LTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDMLACEQHAL 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 447 RVKKEEPGTQEGKVLELEQKcteileQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQN 526
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQC------SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 527 SGVMAQTLEECtvtLEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCE--IQEMLKVARAEKDqlelsctelkqELLK 604
Cdd:TIGR00618 692 LTYWKEMLAQC---QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdaLNQSLKELMHQAR-----------TVLK 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 605 AHGEIKHVSSLLAKVE----KDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHNN 680
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSR 836
|
330 340 350
....*....|....*....|....*....|....*...
gi 987976890 681 -QLITELESSVMKLEGQKADLERQLKTLTKQIKEETEE 717
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
335-665 |
7.76e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 335 TPSRPLSSTSNPFKS--SKCSTTGSSPnnaSELSLASLTEKIQKMEENHHSTA-------EELQATLQEL----SDQQQM 401
Cdd:PLN03229 429 TPVRELEGEVEKLKEqiLKAKESSSKP---SELALNEMIEKLKKEIDLEYTEAviamglqERLENLREEFskanSQDQLM 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 402 VQELTAENEKLVDEktiletsFHQHRERA---EQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCeR 478
Cdd:PLN03229 506 HPVLMEKIEKLKDE-------FNKRLSRApnyLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEI-K 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 479 EKLLSIqqqltcslrKAEEENQGA---AEMIQRLKEENEKLNGLLELErqnsgvMAQTLEECTVTLEGLKIENGSLKAYL 555
Cdd:PLN03229 578 EKMEAL---------KAEVASSGAssgDELDDDLKEKVEKMKKEIELE------LAGVLKSMGLEVIGVTKKNKDTAEQT 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 556 ENEKQKAIVTSSMGQTAEgcEIQEMLKVAraekdQLELSCTELKQELLKAHGeikhvSSLLAKVEKDYSYLKEICDHQAE 635
Cdd:PLN03229 643 PPPNLQEKIESLNEEINK--KIERVIRSS-----DLKSKIELLKLEVAKASK-----TPDVTEKEKIEALEQQIKQKIAE 710
|
330 340 350
....*....|....*....|....*....|
gi 987976890 636 QLSRTSLKlqEKASESDAEIKDMKETIFEL 665
Cdd:PLN03229 711 ALNSSELK--EKFEELEAELAAARETAAES 738
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
468-768 |
7.96e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 468 TEILEQGRCEREKLLSIQQQLT-CSLRKAEEENQGAAEMIQRlKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKI 546
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAeLIIDLEELKLQELKLKEQA-KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 547 ENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKV---ARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKdy 623
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK-- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 624 sylkeicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVmKLEGQKADLERQ 703
Cdd:pfam02463 322 ---------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAK 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 987976890 704 LKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQ 768
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
491-784 |
8.97e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 43.13 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 491 SLRKAEEENQGAAEMIQRLKEENEKLNGLL-ELERQNSGVMAqtlEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMG 569
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELaGLTRRLSAAEG---ELEELVARLAKLEAALREAEAAKEELRIELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 570 QtAEGCEIQ-----EMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKL 644
Cdd:pfam19220 119 Q-AEALERQlaaetEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 645 QEKASESDAEIKDMKETIFEL-EDQVEQHRAVKLHNNQLI---TELESSVMKLEGQKADLERQLKTLTK---QIKEETEE 717
Cdd:pfam19220 198 AELETQLDATRARLRALEGQLaAEQAERERAEAQLEEAVEahrAERASLRMKLEALTARAAATEQLLAEarnQLRDRDEA 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 987976890 718 WRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKELGDMQghgrPVRAESEPEADA 784
Cdd:pfam19220 278 IRAAERRLK-----------EASIERDTLERRLAGLEADLERRTQQFQEMQ----RARAELEERAEM 329
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
428-757 |
9.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 428 ERAEQLSHENEKLINLLQERVKKEEPGTQ--EGKVLELEQKCTEILEQGRCEREKLlsiqqqltcslRKAEEENQGAAEM 505
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSEL-----------PELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 506 IQRLKEENEKLNGL---LELERQNSGVMAQTLEECTVTLEGLKIENGSLkaylenEKQKAIVTSSMGQTAEGCEIQEMLK 582
Cdd:PRK03918 230 VKELEELKEEIEELekeLESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 583 VARAEKDQLELSCTELKQellkahgEIKHVSSLLAKVEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESdaeikdmkETI 662
Cdd:PRK03918 304 EYLDELREIEKRLSRLEE-------EINGIEERIKELEEKEERLEEL-KKKLKELEKRLEELEERHELY--------EEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 663 FELEDQVEQHRAVKLHNNqlITELESSVMKLEGQKADLERQLKTLTKQIKE-ETEEwrrfqADLQTAVvvaNDIKcEAQQ 741
Cdd:PRK03918 368 KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGElKKEI-----KELKKAI---EELK-KAKG 436
|
330
....*....|....*.
gi 987976890 742 ELRTVKRRLLEEEEKN 757
Cdd:PRK03918 437 KCPVCGRELTEEHRKE 452
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
360-711 |
1.05e-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: 43.19 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 360 NNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETS-FHQHRERAEQ---- 432
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLknELSeLRRQIQRAELelqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 433 LSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEM---IQRL 509
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELekeLERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 510 KEENEKLNGLLElerqnsgvmaqtleectvTLEGLKIENGSLKAYLENEKQkaivtssmgqtaegceiqemlkvARAEKD 589
Cdd:pfam05557 210 REHNKHLNENIE------------------NKLLLKEEVEDLKRKLEREEK-----------------------YREEAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 590 QLELSCTELKQELlKAHGEIKHVSSLLAKVEKDYSylkeicdHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQV 669
Cdd:pfam05557 249 TLELEKEKLEQEL-QSWVKLAQDTGLNLRSPEDLS-------RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 987976890 670 EQHRAVklhnnqlITELESSVMKLEGQKADLERQLKTLTKQI 711
Cdd:pfam05557 321 AQYLKK-------IEDLNKKLKRHKALVRRLQRRVLLLTKER 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
576-713 |
1.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKV--EKDY-SYLKEIcDHQAEQLSrtslKLQEKASESD 652
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYeALQKEI-ESLKRRIS----DLEDEILELM 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976890 653 AEIKDMKETIFELEDQVEQHRAvklhnnqlitELESSVMKLEGQKADLERQLKTLTKQIKE 713
Cdd:COG1579 117 ERIEELEEELAELEAELAELEA----------ELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-766 |
1.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 588 KDQLElsctELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRtslklQEKASESDAEIKDMKETIFELED 667
Cdd:COG4913 609 RAKLA----ALEAELAELEEELAEAEERLEALEAELDALQE----RREALQR-----LAEYSWDEIDVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 668 QVEQHRAvklhNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTV- 746
Cdd:COG4913 676 ELERLDA----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALl 751
|
170 180
....*....|....*....|..
gi 987976890 747 --KRRLLEEEEKNARLQKELGD 766
Cdd:COG4913 752 eeRFAAALGDAVERELRENLEE 773
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
360-716 |
1.19e-03 |
|
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: 43.18 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 360 NNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSHENEK 439
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 440 LINLLQERVKkeepgTQEGKVLELEQKCTEILEQGR-------CEREKLLSIQQQLTCSLRKAEEENQGAAEMIQR-LKE 511
Cdd:pfam15921 279 EITGLTEKAS-----SARSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 512 ENEKLNGlLELER----QNSGVMAQTLEECTVTLEGLKIEngslkAYLENEKQKAIVTSSMGQTA-----------EGCE 576
Cdd:pfam15921 354 ANSELTE-ARTERdqfsQESGNLDDQLQKLLADLHKREKE-----LSLEKEQNKRLWDRDTGNSItidhlrrelddRNME 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 577 IQEMLKVARAEKDQLElscTELKQELLKAHGE---IKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRT------S 641
Cdd:pfam15921 428 VQRLEALLKAMKSECQ---GQMERQMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEEltakkmTLESSERTvsdltaS 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 987976890 642 LKLQEKASE-SDAEIKDMKETIfELEDQVEQH-RAVKLHNNQLITELESsvmkLEGQKADLERQLKTLTKQIKEETE 716
Cdd:pfam15921 505 LQEKERAIEaTNAEITKLRSRV-DLKLQELQHlKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQ 576
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
445-755 |
1.73e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 445 QERVKK-EEPGTQEGKVLELEQKCTEILEQGRCE-REKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLEL 522
Cdd:TIGR00606 188 LETLRQvRQTQGQKVQEHQMELKYLKQYKEKACEiRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 523 ERQnsgvmaqtleecTVTLEGLKIENGSLKAYLENEKQKAIvtssMGQTAEGCEIQEMLKVARAEKDQLELSCtelKQEL 602
Cdd:TIGR00606 268 DNE------------IKALKSRKKQMEKDNSELELKMEKVF----QGTDEQLNDLYHNHQRTVREKERELVDC---QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 603 LKAHGEIKHVSSLLAKVEKDYSYLKEICD-HQAEQLSRTSLKLQ----------EKASESDAEIKDMKETIfeLEDQVEQ 671
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELLVEQGRLQLQADrHQEHIRARDSLIQSlatrleldgfERGPFSERQIKNFHTLV--IERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 672 HRAVklhnNQLITELES-------SVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIkCEAQQELR 744
Cdd:TIGR00606 407 AKTA----AQLCADLQSkerlkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI-LELDQELR 481
|
330
....*....|.
gi 987976890 745 TVKRRLLEEEE 755
Cdd:TIGR00606 482 KAERELSKAEK 492
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1008-1090 |
2.07e-03 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 38.91 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 1008 ITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAESV-GIKPSLElSEMLHTDRPDWQSVMQYVAq 1085
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIPMVLS-PEDLSSPHLDELSGMTYLS- 98
|
....*
gi 987976890 1086 iykYF 1090
Cdd:cd21229 99 ---YF 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
362-752 |
2.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 362 ASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL- 440
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAa 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 441 --INLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSL-----RKAEEENQGAAEMIQRLKEEN 513
Cdd:COG1196 491 arLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 514 EKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYleNEKQKAIVTSSMGQTAEgCEIQEMLKVARAEKDQLEL 593
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTLLGRTLV-AARLEAALRRAVTLAGRLR 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 594 SCTELKQELL----KAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQV 669
Cdd:COG1196 648 EVTLEGEGGSaggsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 670 EQHRAVKLHNNQLITELESSVMKLEGQK-------ADLERQLKTLTKQIK-------------EETEEWRRF----QADL 725
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEalgpvnllaieeyEELEERYDFlseqREDL 807
|
410 420
....*....|....*....|....*...
gi 987976890 726 QTAVvvaNDIKcEAQQEL-RTVKRRLLE 752
Cdd:COG1196 808 EEAR---ETLE-EAIEEIdRETRERFLE 831
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
364-763 |
2.31e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 364 ELSLASLTEKIQKMEENHHSTA----EELQATLQE---LSDQQQmvQELTAENEKLVDEKTILETSFHQHRERAEQLSHE 436
Cdd:PRK10246 175 ELTGTEIYGQISAMVFEQHKSArtelEKLQAQASGvalLTPEQV--QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 437 NEklinlLQervkkeepgTQEGKVLELEQKCTEILEQGRCEREKLLSIQ--QQLTCSLRKAEEENQGAAEMIQRLKEENE 514
Cdd:PRK10246 253 DE-----LQ---------QEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 515 KLNGLLELERQNSGVMAQTLEECTVTLeglkienGSLKAYLENEKQKAIVTSSMG--------QTAEGCEI---QEMLKV 583
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQ-------QSLNTWLAEHDRFRQWNNELAgwraqfsqQTSDREQLrqwQQQLTH 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 584 ARAEKDQ-----LELSCTE-------------LKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ 645
Cdd:PRK10246 392 AEQKLNAlpaitLTLTADEvaaalaqhaeqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 646 EKAS---------ESDAEIKDMKETIFELED-------------QVEQHRAVKLHNNQL-ITELESSVMKLEGQKADLER 702
Cdd:PRK10246 472 EKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrLDALEKEVKKLGEEGAALRG 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 703 QLKTLTKQIKEE--------------TEEWRRFQADLQTAVVVANDI------KCEAQQELRTVKRRLLEEEEKNARLQK 762
Cdd:PRK10246 552 QLDALTKQLQRDeseaqslrqeeqalTQQWQAVCASLNITLQPQDDIqpwldaQEEHERQLRLLSQRHELQGQIAAHNQQ 631
|
.
gi 987976890 763 E 763
Cdd:PRK10246 632 I 632
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
578-769 |
2.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 578 QEMLKVARAEKDQLElsctelkqELLKAHGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLqEKASESDAEIKD 657
Cdd:PRK03918 168 GEVIKEIKRRIERLE--------KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 658 MKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLtKQIKEETEEWRRFQADLQTAVVVANDIKC 737
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 987976890 738 EA---QQELRTVKRRLLEEEEKNAR----------LQKELGDMQG 769
Cdd:PRK03918 315 RLsrlEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEE 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
581-764 |
2.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 581 LKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ-EKASESDAEIKdmk 659
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAElERLDASSDDLA--- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 660 etifELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQ---IKEETEEWRRFQADLQtavvVANDIK 736
Cdd:COG4913 689 ----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaAEDLARLELRALLEER----FAAALG 760
|
170 180
....*....|....*....|....*....
gi 987976890 737 CEAQQELR-TVKRRLLEEEEKNARLQKEL 764
Cdd:COG4913 761 DAVERELReNLEERIDALRARLNRAEEEL 789
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
387-770 |
2.43e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 387 ELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENE------KLINLLQERVK--KEEPGTQEG 458
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDsgtpggKKYLLLQKQLEqlQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 459 KVLELEQKCtEILEQgrcereKLLSIQQQltcslrkaEEENQGAAEMIQRLKEENEKLnglleleRQNS---GVMAQTLE 535
Cdd:pfam05622 81 ARDDYRIKC-EELEK------EVLELQHR--------NEELTSLAEEAQALKDEMDIL-------RESSdkvKKLEATVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 536 ECTVTLEGLkienGSLKayleneKQ-KAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELscteLKQELLKAHGEIKHVSS 614
Cdd:pfam05622 139 TYKKKLEDL----GDLR------RQvKLLEERNAEYMQRTLQLEEELKKANALRGQLET----YKRQVQELHGKLSEESK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 615 LLAKVEKDYSYLKEicDHQAEQLSRTSLklqekASESDAeikdMKETIFELE-DQVEQHRAVKLHNNQLITELESSVMKL 693
Cdd:pfam05622 205 KADKLEFEYKKLEE--KLEALQKEKERL-----IIERDT----LRETNEELRcAQLQQAELSQADALLSPSSDPGDNLAA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 694 EGQKADLERQLKTL---TKQIKEETEE-WRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQG 769
Cdd:pfam05622 274 EIMPAEIREKLIRLqheNKMLRLGQEGsYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGS 353
|
.
gi 987976890 770 H 770
Cdd:pfam05622 354 K 354
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
366-526 |
2.91e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 366 SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERaeqlshenEKLINLLQ 445
Cdd:cd00176 55 RVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 446 ERVKKEEPGTQEGKVLELEQKCTEI---LEQGRCEREKLLSIQQQLTCSLRKAEEENqgAAEMIQRLKEENEKLNGLLEl 522
Cdd:cd00176 127 AALASEDLGKDLESVEELLKKHKELeeeLEAHEPRLKSLNELAEELLEEGHPDADEE--IEEKLEELNERWEELLELAE- 203
|
....
gi 987976890 523 ERQN 526
Cdd:cd00176 204 ERQK 207
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
501-645 |
3.03e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.84 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 501 GAAEM----IQRLKEENEKLNG-LLELERQNSGV------MAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmg 569
Cdd:pfam15294 126 GGSALlhmeIERLKEENEKLKErLKTLESQATQAldekskLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALK---- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 570 qtaegCEIQEMLKVARAEKDQLELSCTELKQELLKahgeikhVSSLLAKVEKD----------YSYLKEICDHQAEQLSR 639
Cdd:pfam15294 202 -----SDLEKTLNASTALQKSLEEDLASTKHELLK-------VQEQLEMAEKElekkfqqtaaYRNMKEMLTKKNEQIKE 269
|
....*.
gi 987976890 640 TSLKLQ 645
Cdd:pfam15294 270 LRKRLS 275
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
230-770 |
3.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 230 EEKNKNFQKELSDLEEENRALKEKLRYFEHSEAGSSHTADSSCPTSLTQESSFGSptgNQVSGEVDEYKRHAPQNIlptS 309
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSER---Q 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 310 GSSSSDVTKASLSPDASDFEHLTADTPSRPLSSTSNPFK-SSKCSTTGSSPNNASELSLASLTEKIQKMEENHHSTA--- 385
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssd 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 386 ------EELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKeepgtqe 457
Cdd:TIGR00606 472 rileldQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK------- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 458 gkvLELEQKCTEILEQGRCEREKLLSI---QQQLTCSLRKAEEENQGAAEMIQRLKEENEKL--------NGLLELERQN 526
Cdd:TIGR00606 545 ---MDKDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqnknhinNELESKEEQL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 527 SGVMAQTLEECTVTLEGLKIENgsLKAYLEN-EKQKAI-----------VTSSMGQTAEGCEIQEmlKVARAEKDQLELS 594
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLER--LKEEIEKsSKQRAMlagatavysqfITQLTDENQSCCPVCQ--RVFQTEAELQEFI 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 595 cTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQ 671
Cdd:TIGR00606 698 -SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnKLQKVNRDIQRLKNDIEEQETLLGT 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 672 HRAVKLHNNQLITELeSSVMKLEGQKADLERQLKTLTKQIKeeteewrrfQADLQTAVVVANDIKCEAQQELRTV----- 746
Cdd:TIGR00606 777 IMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVvskie 846
|
570 580
....*....|....*....|....*.
gi 987976890 747 -KRRLLEEEEKNAR-LQKELGDMQGH 770
Cdd:TIGR00606 847 lNRKLIQDQQEQIQhLKSKTNELKSE 872
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
576-763 |
3.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLElsctELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIcdHQAEQLSRTSLKLQEKASESDAEI 655
Cdd:COG4717 75 ELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 656 KDMKETIFELEDQVEQhravklhnnqlITELESSVMKLEGQKADLERQLKTLT-KQIKEETEEWRRFQADLQTAvvvaND 734
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAEL----EE 213
|
170 180
....*....|....*....|....*....
gi 987976890 735 IKCEAQQELRTVKRRLLEEEEKNARLQKE 763
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
366-750 |
3.85e-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: 40.99 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 366 SLASLTEKIQKMEEnhhstaeelqatlqelsDQQQMVQELTAeneklvdektiLETSFHQHRERAEQLSHENEKLINLLQ 445
Cdd:pfam06160 87 ALDEIEELLDDIEE-----------------DIKQILEELDE-----------LLESEEKNREEVEELKDKYRELRKTLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 446 ERvkkeepGTQEGKVLELeqkcteiLEqgrcerEKLLSIQQQLTcslrKAEEENQG-----AAEMIQRLKEENEKLNGLL 520
Cdd:pfam06160 139 AN------RFSYGPAIDE-------LE------KQLAEIEEEFS----QFEELTESgdyleAREVLEKLEEETDALEELM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 521 ElerqnsgVMAQTLEECTVTLEG--LKIENGslkaYLENEKQKAIVTsSMGQTAEGCEIQEMLKVARAEKDQLELscTEL 598
Cdd:pfam06160 196 E-------DIPPLYEELKTELPDqlEELKEG----YREMEEEGYALE-HLNVDKEIQQLEEQLEENLALLENLEL--DEA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 599 KQELLKAHGEIKHVSSLLAK-------VEKDYSYLKEICDHQAEQLSRTSLKLQEkasesdaeikdMKETiFEL-EDQVE 670
Cdd:pfam06160 262 EEALEEIEERIDQLYDLLEKevdakkyVEKNLPEIEDYLEHAEEQNKELKEELER-----------VQQS-YTLnENELE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 671 QHRAVKLHNNQLITELESSVMKLEGQKA-------DLERQLKTLtKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQEL 743
Cdd:pfam06160 330 RVRGLEKQLEELEKRYDEIVERLEEKEVayselqeELEEILEQL-EEIEEEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
....*..
gi 987976890 744 RTVKRRL 750
Cdd:pfam06160 409 REIKRLV 415
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
368-547 |
4.07e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 368 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQEltaENEKLVDEKtiLETSFHQHRERAEQLSHENEKLINLLQER 447
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---EEEKKKVEQ--LKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 448 VKKEEPGTQEG----KVLELEQKCTEILEQGRCEREKLLSIQQQL------TCSLRKAEEENQGAAEMIQRLKEENEKLN 517
Cdd:PTZ00121 1667 AKKAEEDKKKAeeakKAEEDEKKAAEALKKEAEEAKKAEELKKKEaeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
170 180 190
....*....|....*....|....*....|
gi 987976890 518 GLLELERQNSGVMAQTLEECTVTLEGLKIE 547
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-742 |
4.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 367 LASLTEKIQKMEENHHSTAEELQATLQELS-DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQ 445
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 446 ERVKKEEPGTQE------GKVLELEQKCTEILEQGRCEREKLLSIQQQLTC---SLRKAEEENQGAAEMIQRLKE----E 512
Cdd:COG4717 238 AAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflLLAREKASLGKEAEELQALPAleelE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 513 NEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmgqtaegcEIQEMLKVARAEKDQLE 592
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ----------EIAALLAEAGVEDEEEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 593 LSCTELKQELLKAHGEIKHVSSLLAkvEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQh 672
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLE--ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ- 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 673 ravklhnnqlitelessvMKLEGQKADLERQLKTLTKQIKEETEEWRRfqadLQTAVVVANDIKCEAQQE 742
Cdd:COG4717 465 ------------------LEEDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAREEYREE 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-514 |
5.86e-03 |
|
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: 40.81 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 162 EKAVLESQVRELLAEAKAKDSEINRLRSELKKCRekrtlntAGTDTSDPKTDGTSVSAADSEPLIQALEEKNKNFQKELS 241
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 242 DLEEENRALKEKLryfehseagsshtadsscpTSLTQESSFGSPTGNQVSGEVDEYKRHAPQNILptsgssssdvTKASL 321
Cdd:TIGR02168 758 ELEAEIEELEERL-------------------EEAEEELAEAEAEIEELEAQIEQLKEELKALRE----------ALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 322 SPDASDFEHLTADTPSRPLSSTSNpfksskcsttgsspnnaselsLASLTEKIQKMEENHHSTAEELQATLQELSDQQQM 401
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERR---------------------IAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 402 VQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLinllqervkkeepgtqEGKVLELEQKCTEILEQGRCEREKL 481
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELREL----------------ESKRSELRRELEELREKLAQLELRL 931
|
330 340 350
....*....|....*....|....*....|...
gi 987976890 482 LSIQQQLTCSLRKAEEENQGAAEMIQRLKEENE 514
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-562 |
6.72e-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: 40.13 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 383 STAEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSHENEKLINLLQERVKK--EEPGTQEGKV 460
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELAEleKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 461 LELEQKCTEIL----EQGRCEREKLLSIQQQLTCSLRKAE------EENQGAAEMIQRLKEENEKLNGLLELERQNSGVM 530
Cdd:COG4942 100 EAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|..
gi 987976890 531 AQTLEECTVTLEGLKIENGSLKAYLENEKQKA 562
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
370-552 |
7.05e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 370 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVK 449
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 450 KEEP-GTQEGKVLELEQKCTEILEQGRCEREKllSIQQQLTCSL-RKAEEEnqgAAEMIQRLKEENEklnglLELERQNS 527
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRVAGLTPE--QARKLLLKLLdAELEEE---KAQRVKKIEEEAD-----LEAERKAQ 179
|
170 180 190
....*....|....*....|....*....|.
gi 987976890 528 GVMAQTLEECT------VTLEGLKIENGSLK 552
Cdd:PRK12705 180 NILAQAMQRIAsetasdLSVSVVPIPSDAMK 210
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
381-763 |
7.10e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 40.27 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 381 HHSTAEeLQATLQELSDQQQMVQELTAENEKL------------VDEKTILETSFHQHRERAEQLS---HENEKLI--NL 443
Cdd:pfam15964 124 HHLEAE-VKFCKEELSEMKQRVQVVVLENEKLqqelksqtqeetLREQTLLDSSGNMQNSWCTPEDsrvHQTSKRPasHN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 444 LQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEeenqgaaEMIQRLKEE--------NEK 515
Cdd:pfam15964 203 LAERLKSATTGEDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCE-------DLKERLKHKeslvaastSSR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 516 LNGLLELERQNSGVMAQTLEECTV-TLEGLKIENGSLKAYLENEKQKAIVTSSMGQTA--EGCEIQEMLKVARAEKDQLE 592
Cdd:pfam15964 276 VGGLCLKCAQHEAVLAQTHTNVHMqTIERLTKERDDLMSALVSVRSSLAEAQQRESSAyeQVKQAVQMTEEANFEKTKAL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 593 LSCTELKQELLKAHGEI-KHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKasesdaeikdmketIFELEDQVEQ 671
Cdd:pfam15964 356 IQCEQLKSELERQKERLeKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQN--------------VAQLEAQVEK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 672 hraVKLHNNQLITELESSVMKLEGQKADLE------RQLKTLTKQIKEETE-EWRRFQADLQTAVVVANDIKCEAQQELR 744
Cdd:pfam15964 422 ---VTREKNSLVSQLEEAQKQLASQEMDVTkvcgemRYQLNQTKMKKDEAEkEHREYRTKTGRQLEIKDQEIEKLGLELS 498
|
410
....*....|....*....
gi 987976890 745 TVKRRLLEEEEKNARLQKE 763
Cdd:pfam15964 499 ESKQRLEQAQQDAARAREE 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
166-525 |
7.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 166 LESQVRELLAEAKAKDSEINRLRSELKKCREKrtLNTAGTDTSDPKTDgtsvsAADSEPL---IQALEEKNKNFQKELSD 242
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK--LQKVNRDIQRLKND-----IEEQETLlgtIMPEEESAKVCLTDVTI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 243 LEEENRALKEKLRYFEHSEAGSshtadsscptsltqESSFGSPTGNQVSGEVDEyKRHAPQNIlptsgSSSSDVTKASLS 322
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKL--------------QGSDLDRTVQQVNQEKQE-KQHELDTV-----VSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 323 PDASDFEHLtadtpsrplSSTSNPFKSSKcsttgsspnnaseLSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMV 402
Cdd:TIGR00606 854 DQQEQIQHL---------KSKTNELKSEK-------------LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 403 QELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEI------LEQGRC 476
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELntvnaqLEECEK 991
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 987976890 477 EREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEklngLLELERQ 525
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE----LKEVEEE 1036
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
576-767 |
8.12e-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: 40.39 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 576 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDH---QAEQLSRTSLKLQEKASESD 652
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDlkkQKEELENELNLLEKEKLNIQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 653 AEIKDMKETIFELEdqveqhraVKLHN----NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTA 728
Cdd:TIGR04523 187 KNIDKIKNKLLKLE--------LLLSNlkkkIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL 258
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 987976890 729 VVVANDIK---CEAQQELRTVKRRLLEEEEKNARLQKELGDM 767
Cdd:TIGR04523 259 KDEQNKIKkqlSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
580-768 |
8.15e-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: 39.88 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 580 MLKVARAEKDQLELS-CTELKQELLKAHgeiKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDM 658
Cdd:pfam07888 23 LLVVPRAELLQNRLEeCLQERAELLQAQ---EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 659 KETIFELEDQVEQHR-------AVKLHNNQLITELESSVMKLEGQKADLERQL-------KTLTKQIKEETEEWRRFQAD 724
Cdd:pfam07888 100 EEKYKELSASSEELSeekdallAQRAAHEARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 987976890 725 LQTAVVVAndikCEAQQELRTVKRRLLEEEEKNARLQKELGDMQ 768
Cdd:pfam07888 180 LQQTEEEL----RSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
503-789 |
9.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 503 AEMIQRLKEENEKLNGLLELERQNSGVMA--QTLEECTVTLEGLKIENGSLKAYLENEKQKAIvtssmgqtaegcEIQEM 580
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESLEGSKRKLEEKIR------------ELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 581 LKVARAEKDQLELSCTELKQellkahgeikhvsslLAKVEKDYSYLKEICDHQAEQLSRtslkLQEKASESDAEIKDMKE 660
Cdd:PRK03918 268 IEELKKEIEELEEKVKELKE---------------LKEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976890 661 TIFELEDQVEQHRAVKlhnnQLITELESSVMKLEGQKADLERqlktlTKQIKEETEEWRRFQADLQtavvvandiKCEAQ 740
Cdd:PRK03918 329 RIKELEEKEERLEELK----KKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTGLT---------PEKLE 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 987976890 741 QELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESEPEADAPGRWP 789
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
|
| |
