|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
956-1019 |
5.47e-44 |
|
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: 154.83 E-value: 5.47e-44
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 956 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDK 64
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
956-1019 |
2.40e-43 |
|
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: 152.88 E-value: 2.40e-43
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 956 LAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDK 64
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
950-1019 |
3.09e-42 |
|
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: 150.22 E-value: 3.09e-42
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 950 KDPLAALAREYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDK 70
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
965-1019 |
6.59e-22 |
|
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: 91.64 E-value: 6.59e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 965 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNR 57
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
963-1027 |
1.57e-19 |
|
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: 84.75 E-value: 1.57e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNsqeKSLCLFNLE 1027
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLS---KSNALYNLQ 63
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
963-1034 |
2.92e-19 |
|
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: 84.00 E-value: 2.92e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSLCL---FNLEEESLvGI 1034
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLnnaFDVAEQEL-GI 75
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
963-1019 |
4.86e-19 |
|
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: 83.50 E-value: 4.86e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNR 57
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
963-1027 |
7.79e-19 |
|
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: 83.18 E-value: 7.79e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKslcLFNLE 1027
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDP---RENLN 71
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
963-1019 |
1.59e-18 |
|
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: 82.02 E-value: 1.59e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNR 57
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
966-1018 |
2.32e-18 |
|
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: 81.18 E-value: 2.32e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 966 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPEN 55
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
965-1019 |
6.74e-18 |
|
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: 80.51 E-value: 6.74e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 965 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANR 57
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
963-1019 |
9.99e-18 |
|
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: 79.62 E-value: 9.99e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNR 57
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
963-1028 |
1.24e-17 |
|
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: 79.66 E-value: 1.24e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELnsqEKSLCLFNLEE 1028
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKL---KKSNARHNLEH 67
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
959-1015 |
1.41e-17 |
|
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: 79.49 E-value: 1.41e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 959 EYGGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELN 1015
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLD 62
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
963-1031 |
1.56e-17 |
|
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: 79.14 E-value: 1.56e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSLCL---FNLEEESL 1031
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLanaFLVAEQEL 75
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
968-1034 |
6.20e-17 |
|
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: 77.47 E-value: 6.20e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 968 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE-KSLCLFNLEEESLVGI 1034
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDiKENCKLAFDAAAKLGI 73
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
967-1034 |
6.81e-16 |
|
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: 74.31 E-value: 6.81e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 967 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL---NSQEKSLCLFNLEEESLvGI 1034
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLskeNVYENNKLAFTVAEKEL-GI 74
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
367-771 |
1.06e-15 |
|
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: 81.99 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSQENEKLMN 445
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNKIKK 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 446 LLQErvKNEEPTTQEGKIIELEQKCTGI------LEQGRFE------REKLLNIQQQLTCSLRKVEEENQgaleMIKRLK 513
Cdd:TIGR04523 268 QLSE--KQKELEQNNKKIKELEKQLNQLkseisdLNNQKEQdwnkelKSELKNQEKKLEEIQNQISQNNK----IISQLN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 514 EENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAT--EASAVEQTAESCEVQEMLKVARAEK 591
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINdlESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 592 DLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTS------------------------LKL 647
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 648 QEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE--QKSDLERQLKTLTK---QMKEETEEWR 722
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKeieELKQTQKSLK 581
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1886396456 723 RFQADLQtavvvaNDIKcEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 771
Cdd:TIGR04523 582 KKQEEKQ------ELID-QKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
963-1015 |
1.12e-15 |
|
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: 73.67 E-value: 1.12e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELN 1015
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLD 53
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
968-1018 |
4.43e-15 |
|
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: 72.08 E-value: 4.43e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 968 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDS 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-726 |
7.72e-15 |
|
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: 79.72 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENhhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 449
Cdd:TIGR02168 679 IEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 450 RvkNEEPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 529
Cdd:TIGR02168 752 L--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 530 NNMMAKTLEECRVTLEGLKMENGSLK--------SHLQGEKQKATEASAVEQ-TAESCEVQEMLKVARAEKDLLELSCNE 600
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSedieslaaEIEELEELIEELESELEAlLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 601 LRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS-RTSLKLQ---EKASESDAEIKDMKETIFELEDQVEQHR 676
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEARRRLKRLENKIKELG 985
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 677 AVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWR-RFQA 726
Cdd:TIGR02168 986 PVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
968-1018 |
2.21e-14 |
|
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: 70.27 E-value: 2.21e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 968 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHD 56
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
964-1034 |
2.95e-14 |
|
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: 69.49 E-value: 2.95e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 964 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL---NSQEKSLCLFNLEEESLvGI 1034
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLkkdNWLENNRLAFRVAETSL-GI 73
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
963-1018 |
3.63e-14 |
|
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: 69.34 E-value: 3.63e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQS 56
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
963-1031 |
9.79e-14 |
|
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: 68.20 E-value: 9.79e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSLCL---FNLEEESL 1031
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLqnaFNLAEQHL 73
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
964-1018 |
9.90e-14 |
|
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: 68.37 E-value: 9.90e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 964 KRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDD 59
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
961-1031 |
1.04e-13 |
|
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: 68.14 E-value: 1.04e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 961 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQ---EKSLCLFNLEEESL 1031
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDdavENNQLAFDVAEREF 75
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
963-1031 |
1.07e-13 |
|
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: 68.55 E-value: 1.07e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL---NSQEKSLCLFNLEEESL 1031
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLkksNAHYNLQNAFNVAEKEL 76
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
963-1018 |
1.77e-13 |
|
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: 67.67 E-value: 1.77e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQD 60
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
965-1018 |
4.00e-13 |
|
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: 66.54 E-value: 4.00e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 965 RNALLKWCQKKTQGY-ANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSE 58
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
963-1028 |
4.81e-13 |
|
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: 67.00 E-value: 4.81e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNsqeKSLCLFNLEE 1028
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLT---KSNATYNLQQ 79
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
966-1027 |
7.80e-13 |
|
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: 65.41 E-value: 7.80e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 966 NALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSL-CLFNLE 1027
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRFkKIENIN 63
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
961-1014 |
2.34e-12 |
|
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: 64.30 E-value: 2.34e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 961 GGSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL 1014
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSEL 54
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
967-1031 |
3.13e-12 |
|
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: 63.64 E-value: 3.13e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 967 ALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQ--EKSLCL-FNLEEESL 1031
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMdaEARLNLaFDFAEKKL 71
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
963-1018 |
4.13e-12 |
|
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: 64.34 E-value: 4.13e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDD 65
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
963-1018 |
7.11e-12 |
|
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: 63.55 E-value: 7.11e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDD 65
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
462-767 |
7.96e-12 |
|
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: 69.70 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 462 KIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLE 538
Cdd:TIGR02168 678 EIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 539 ECRVTLEGLKMENGSLKSHLQgekqkateasavEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSL 618
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELA------------EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 619 LAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 698
Cdd:TIGR02168 826 LESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886396456 699 QKSDLERQLKTLTKQMKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRKLLEEEEKNARLQKEL 767
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
965-1031 |
2.22e-11 |
|
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: 61.42 E-value: 2.22e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 965 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL---NSQEKSLCLFNLEEESL 1031
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLskdNVYENNRLAFEVAEREL 71
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
963-1018 |
3.02e-11 |
|
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: 61.66 E-value: 3.02e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDD 65
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
364-766 |
4.45e-11 |
|
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: 66.97 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 364 SVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQL-SQENEK 442
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIkNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 LMNLLQERVKNEEPTTQEGKIIELEQKctgileqgrfeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 522
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 523 L-----ELERHNNNMMAKT--LEECRVTLEGLKME-----NGSLKSHLQGEKQKATEA-SAVEQTAESC-EVQEMLKVAR 588
Cdd:TIGR04523 269 LsekqkELEQNNKKIKELEkqLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIqNQISQNNKIIsQLNEQISQLK 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 589 AEKDLLELSCNELRQELLKANGEIKHVssllaKVEKDySYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIF 666
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKL-----KKENQ-SYKQEIKNleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 667 ELEDQVEQHRAVKLHNNQLISELES-------SVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVvvandik 739
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE------- 495
|
410 420
....*....|....*....|....*..
gi 1886396456 740 ceaqQELRTVKRKLLEEEEKNARLQKE 766
Cdd:TIGR04523 496 ----KELKKLNEEKKELEEKVKDLTKK 518
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
962-1031 |
8.64e-11 |
|
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: 59.74 E-value: 8.64e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 962 GSKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL--NSQEKSLCL-FNLEEESL 1031
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVknRSPRDNLELaFRIAEQHL 74
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
963-1018 |
1.22e-10 |
|
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: 60.10 E-value: 1.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQE 1018
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDD 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
509-767 |
1.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 509 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngslksHLQGEKQKAtEASAVEQTAESCEVQEMLKVAR 588
Cdd:COG1196 202 LEPLERQAEKAERYRELK--------EELKELEAELLLLKLR------ELEAELEEL-EAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 589 AEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 668
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 669 EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKcEAQQELRT 748
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL-ERLERLEE 421
|
250
....*....|....*....
gi 1886396456 749 VKRKLLEEEEKNARLQKEL 767
Cdd:COG1196 422 ELEELEEALAELEEEEEEE 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
376-765 |
1.41e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 376 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlmnlLQERVKNEE 455
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 456 PTTQEGKIIELEQKCTGIleqgrfeREKLLNIQQQLTcSLRKVEEENQGALEMIKR-----------LKEENEK--LNEF 522
Cdd:PRK03918 386 PEKLEKELEELEKAKEEI-------EEEISKITARIG-ELKKEIKELKKAIEELKKakgkcpvcgreLTEEHRKelLEEY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 523 -LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScnEL 601
Cdd:PRK03918 458 tAELKR-----IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE--KL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 602 RQELLKANGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE--------- 669
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylel 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 670 -DQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLER---QLKTLTK--------QMKEETEEWRRFQADLQTAVVVAND 737
Cdd:PRK03918 608 kDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKkyseeeyeELREEYLELSRELAGLRAELEELEK 687
|
410 420
....*....|....*....|....*...
gi 1886396456 738 IKCEAQQELRTVKRKLLEEEEKNARLQK 765
Cdd:PRK03918 688 RREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-777 |
1.79e-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: 65.46 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 495 LRKVEEENQGALeMIKRLKEENEKLNEFLELERHNNNMM---AKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAV 571
Cdd:TIGR02168 218 LKAELRELELAL-LVLRLEELREELEELQEELKEAEEELeelTAELQELEEKLEELRLEVSELEEEIE-ELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 572 EQTaescEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE-- 649
Cdd:TIGR02168 296 EIS----RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEle 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 650 -KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ--------MKEETEE 720
Cdd:TIGR02168 372 sRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 721 WRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVV 777
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
963-1017 |
1.88e-10 |
|
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: 58.90 E-value: 1.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQ 1017
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQ 58
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-638 |
2.91e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 442
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 LMNLLQE-----RVKNEEPTTQEGKIIELEQKCTGILEQGrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENE 517
Cdd:TIGR02168 321 LEAQLEElesklDELAEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 518 KLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELS 597
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1886396456 598 CNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAE 638
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-768 |
3.48e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 374 TEKIQKMEENHHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---MNLLQER 450
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 451 VKN------------EEPTTQEGKIIELEQKCTGILEQGRFeREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEK 518
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 519 LNEFLELERHNNNMMAKtLEECRVTLEGLKmengSLKSHLQGEKQKATEASaVEqtaescEVQEMLKVARAEKDLLELSC 598
Cdd:PRK03918 340 LEELKKKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRLTGLT-PE------KLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 599 NELRQELLKANGEIKHVSSLLAKVEKdysyLKEICDHQAEQLSRTSLKlqEKASESDAEIKDMKETIFELEDQVEQHRAV 678
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKK----AKGKCPVCGRELTEEHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 679 KLHNNQLISElESSVIKLE---EQKSDLERQLKTLT-KQMKEETEEWRRFQADLQT----AVVVANDIK--CEAQQELRT 748
Cdd:PRK03918 482 LRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklEELKKKLAE 560
|
410 420
....*....|....*....|
gi 1886396456 749 VKRKLLEEEEKNARLQKELG 768
Cdd:PRK03918 561 LEKKLDELEEELAELLKELE 580
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
367-772 |
6.48e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERAEQL 436
Cdd:PRK02224 212 ESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERLEEL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 437 SQENEKLmnLLQERVKNEEPTTQEGKIIELEQKCTGI---LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLK 513
Cdd:PRK02224 292 EEERDDL--LAEAGLDDADAEAVEARREELEDRDEELrdrLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 514 EENEKLNEFLELERHNNNMMAKTLEECR-------VTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--EVQEML 584
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveEAEALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 585 KV---------------------ARAEKDLLELSCNELRQELLKANGEIKHVSSLlAKVEKDYSYLKE-------ICDHQ 636
Cdd:PRK02224 450 EAgkcpecgqpvegsphvetieeDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEErredleeLIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 637 AEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHR-AVKLHNNQL---------ISELESSVIKLEEQKSDL 703
Cdd:PRK02224 529 RETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAReEVAELNSKLaelkeriesLERIRTLLAAIADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 704 ER------QLKTLTKQMKEETEEWRRFQADLQ-----TAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQG 772
Cdd:PRK02224 609 ERlrekreALAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
366-773 |
7.93e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 63.27 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 366 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 443
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 444 -MNLLQERVKNEEPTTQ---------EGKIIELEQKCTGILEQ-GRFEREKLLNIQQQLTCSLRKVEEENQGAL------ 506
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklkn 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 507 -------EMIKRLKEEnEKLNefLELERHNNNMMAKTLE------ECRVTLEGLKMENGSLKSHLQGEKQKATEASAV-- 571
Cdd:pfam01576 184 kheamisDLEERLKKE-EKGR--QELEKAKRKLEGESTDlqeqiaELQAQIAELRAQLAKKEEELQAALARLEEETAQkn 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 572 -------EQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKH-VSSLLAKVEkdysyLKEICDHQAEQLSRT 643
Cdd:pfam01576 261 nalkkirELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtLDTTAAQQE-----LRSKREQEVTELKKA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 644 slkLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELESSVIKLEEQKSDLERQLKTLTkQMKEETE 719
Cdd:pfam01576 336 ---LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQDSE 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 720 EWRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRKLLEEEEKNARLQKELGDVQGH 773
Cdd:pfam01576 405 HKRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
359-720 |
2.48e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 359 GSSPNSVSEL-SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLS 437
Cdd:TIGR02169 664 GGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 438 qenEKLMNLLQERVKNE-EPTTQEGKIIELEQKCTGI-LEQGRFEREKLLNIQQQLTCSLRKVEEENQgalEMIKRLKEE 515
Cdd:TIGR02169 744 ---EDLSSLEQEIENVKsELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 516 NEKLNEfLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKaTEASAVEQTAESCEVQEMLKVARAEKDLLE 595
Cdd:TIGR02169 818 EQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-LEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 596 LSCNELRQELLKANGEI----KHVSSLLAKVEKDYSYLKEICDHQAEQLSrtslklqekASESDAEIKDMKETIFELEDQ 671
Cdd:TIGR02169 896 AQLRELERKIEELEAQIekkrKRLSELKAKLEALEEELSEIEDPKGEDEE---------IPEEELSLEDVQAELQRVEEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1886396456 672 VEQHRAVklhNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEETEE 720
Cdd:TIGR02169 967 IRALEPV---NMLAIQEYEEVLKRLDELKEKRAK-LEEERKAILERIEE 1011
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
968-1031 |
2.85e-09 |
|
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: 55.70 E-value: 2.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 968 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSL----CLFNLEEESL 1031
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSATerldHAFNIARQHL 72
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
966-1013 |
2.98e-09 |
|
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: 56.54 E-value: 2.98e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1886396456 966 NALLKWCQKKTQGYaNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQE 1013
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDA 49
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
963-1019 |
4.63e-09 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 60.34 E-value: 4.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 963 SKRNALLKWCQKKTQGYAN-IDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK 1019
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQKK 182
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
961-1034 |
5.53e-09 |
|
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: 54.63 E-value: 5.53e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1886396456 961 GGSKRnALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQEL---NSQEKSLCLFNLEEESLvGI 1034
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLkrrSNRENLETAFTVAEKEL-GI 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-627 |
6.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 446
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcsLRKVEEENQGALEMIKRLKEENEKLNEFLELE 526
Cdd:COG1196 332 LEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 527 RHNNNmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELscNELRQELL 606
Cdd:COG1196 407 EAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL--EAALAELL 483
|
250 260
....*....|....*....|.
gi 1886396456 607 KANGEIKHVSSLLAKVEKDYS 627
Cdd:COG1196 484 EELAEAAARLLLLLEAEADYE 504
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-764 |
9.55e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 9.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENHhstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKLMNL--- 446
Cdd:COG4717 73 LKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREELEKLEK-LLQLLPLYQELEALEAELAELper 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 ---LQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFEREKLLniqQQLTCSLRKVEEENQGALEMIKRLKEENEK 518
Cdd:COG4717 148 leeLEERLEElreleEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 519 LNEflELERHNNNMMAKTLEEC-------------RVTLEGLKMENGSLKSHLQG----------------EKQKATEAS 569
Cdd:COG4717 225 LEE--ELEQLENELEAAALEERlkearlllliaaaLLALLGLGGSLLSLILTIAGvlflvlgllallflllAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 570 AVEQTAESCEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---T 643
Cdd:COG4717 303 EAEELQALPALEELEEEELEElLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 644 SLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEssvikLEEQKSDLERQLKTLTKQMKEETEEWRR 723
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAE 457
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1886396456 724 FQADLQTAvvVANDIKCEAQQELRTVKRKLLEEEEKNARLQ 764
Cdd:COG4717 458 LEAELEQL--EEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
965-1027 |
1.74e-08 |
|
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: 53.11 E-value: 1.74e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 965 RNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSLCLFNLE 1027
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPFKKRENIN 63
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
370-767 |
1.76e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.83 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENE------K 442
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 LMNLLQERVKNEEPTTQEGKIIELEQKCTGI-------------LEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMI 509
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINRarkaaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 510 KRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENgSLKSHLQGEKQKATEASAVEQTAesCEVQEMLKVARA 589
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHI----RDAHEVATSIREISCQQH-TLTQHIHTLQQQKTTLTQKLQSL--CKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 590 EKDLLELSCNELRQELLKANGEIKhvssllakVEKDYSYLKEI---CDHQAEQLSRTSL-KLQEKASESDAEIKDmKETI 665
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQE--------LQQRYAELCAAaitCTAQCEKLEKIHLqESAQSLKEREQQLQT-KEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 666 FELED---QVEQHRAVKLHNNQ-------------------------LISELESSVIKLEEQKSDLERQLKTLTKQMKEE 717
Cdd:TIGR00618 482 HLQETrkkAVVLARLLELQEEPcplcgscihpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1886396456 718 TEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRKLLEEEEKNARLQKEL 767
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
963-1028 |
1.98e-08 |
|
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: 53.07 E-value: 1.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKslcLFNLEE 1028
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSN---LANLEH 63
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
562-884 |
2.00e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 562 KQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLS 641
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 642 RTSlklqekASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEw 721
Cdd:COG3883 97 RSG------GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 722 rrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRW 801
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 802 PGVCVSRTSPTPPESATTVKSLIKSFDLGRPGGAGQNISVHKTPRSPLSGIPVRTAPAAAVSPMQRHSTYSSVRPASRGV 881
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGA 326
|
...
gi 1886396456 882 TQR 884
Cdd:COG3883 327 SAG 329
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
963-1013 |
3.84e-08 |
|
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: 52.24 E-value: 3.84e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 963 SKRNALLKWCQKKTQGYAnidITNFSSSWSDGLAFCALLHTYLPAHIPYQE 1013
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPDNE 48
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-758 |
3.94e-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: 57.77 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 506 LEMIKRLKEENEKLNEFL--ELERHNNNMMAKT--LEECRVTLEGLKMENGSLKSHLQGEKQKATEA----SAVEQTAEs 577
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLqsELRRIENRLDELSqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlSSLEQEIE- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 578 cEVQEMLKVARAEKDLLELSCNELRQELLK-----ANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLK---LQE 649
Cdd:TIGR02169 755 -NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 650 KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQ 729
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260 270
....*....|....*....|....*....|..
gi 1886396456 730 TAVVVANDIKC---EAQQELRTVKRKLLEEEE 758
Cdd:TIGR02169 914 KKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
351-766 |
4.23e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 351 KSSKCSTAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELT-----------------AENE 413
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 414 KLVDEKTiletsfhQHRERAEQLSQENEKLMNLLQERVKN-EEPTTQEGKIIELEQKCTGILEQGR--FEREKLLNIQQQ 490
Cdd:pfam05483 419 KLLDEKK-------QFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKteLEKEKLKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 491 LTCSLRKVEEEN--QGALEMIKRLKEENEKLNEFLELERHnnnmMAKTLEECRVTLEGLKMENGSLKSHLqgeKQKATEA 568
Cdd:pfam05483 492 AHCDKLLLENKEltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEF---IQKGDEV 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 569 SAVEQTAESCEVQEMLKVARAEKDL--LELSCNELR----------QELLKANGEIKHVSSLLAKVEKDYsylkEICDHQ 636
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMkiLENKCNNLKkqienknkniEELHQENKALKKKGSAENKQLNAY----EIKVNK 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 637 AE-QLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVI-KLEEQKSDLERQLKTLTKQM 714
Cdd:pfam05483 641 LElELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKII 720
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 715 KEETEEWRRFQADLQTAVVVANDIKCE---AQQELRTVKRKLLEEEEKNARLQKE 766
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
968-1027 |
6.83e-08 |
|
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: 51.50 E-value: 6.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 968 LLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPahipyqELNSQEKSLCLFNLE 1027
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKP------DLFSWDKVVKMSPVE 58
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
431-801 |
7.52e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 431 ERAEQLSQENEKL---MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTcSLRKVEEENQGALE 507
Cdd:COG1196 213 ERYRELKEELKELeaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 508 MIKRLKEENEKLNEFLELERHNNnmmaktleecRVTLEGLKMENGSLKSHLQGEKQKATEAsaveqtaescevQEMLKVA 587
Cdd:COG1196 292 ELLAELARLEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEEL------------EEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 588 RAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysylkeicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFE 667
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE-----------ELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 668 LEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandikcEAQQELR 747
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL---------LEELAEA 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 748 TVKRKLLEEEEKNARLQ----KELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGRW 801
Cdd:COG1196 490 AARLLLLLEAEADYEGFlegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAA 547
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
400-809 |
8.54e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 400 DQQQMVQELTAE-NEKLVDEKTILETSFH--QHRERAEQlSQENEKLMNLLQERVKNEepttQEGKIIELEQKCTgiLEQ 476
Cdd:pfam17380 248 DVTTMTPEYTVRyNGQTMTENEFLNQLLHivQHQKAVSE-RQQQEKFEKMEQERLRQE----KEEKAREVERRRK--LEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 477 GRFEREKLLNIQQQLTCSLRKVEEENQGALEmikRLKEENEKLneflELERHNNNMMAKTLEECRvTLEGLKMENGSLKS 556
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQERMAMERERELE---RIRQEERKR----ELERIRQEEIAMEISRMR-ELERLQMERQQKNE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 557 HLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSsllaKVEKDYSYLKEICDHQ 636
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR----LEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 637 AEQLSRTSLKLqEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELE----SSVIKLEEQKSDLERQLKTltk 712
Cdd:pfam17380 469 EEERKRKKLEL-EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEmeerQKAIYEEERRREAEEERRK--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 713 qmKEETEEWRRFQAdlQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARL------------------QKELGDVQGHG 774
Cdd:pfam17380 545 --QQEMEERRRIQE--QMRKATEERSRLEAMEREREMMRQIVESEKARAEYeattpittikpiyrprisEYQPPDVESHM 620
|
410 420 430
....*....|....*....|....*....|....*....
gi 1886396456 775 RVVTSR----AAPPPVDEEPESSEVDAAGRWPGVCVSRT 809
Cdd:pfam17380 621 IRFTTQspewATPSPATWNPEWNTVTAEEETPGIPIIHS 659
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
389-715 |
1.62e-07 |
|
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: 55.41 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 389 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLMNLLQER-VKNEEPTTQEGKIIELE 467
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 468 QKctgileqgrFEREKLLNiqQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERHNN------NMMAKTLEEC 540
Cdd:TIGR04523 398 SK---------IQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSvkeliiKNLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 541 RVTLEGLKMENGSLKSHLQGEKQ--KATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIkhvSSL 618
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI---SDL 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 619 LAKVEKDYSYLKEicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEE 698
Cdd:TIGR04523 544 EDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
330
....*....|....*..
gi 1886396456 699 QKSDLERQLKTLTKQMK 715
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIK 634
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
388-773 |
2.08e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 388 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhreRAEQLSQENEKLMNLLQErvkneEPTTQEGKIIELE 467
Cdd:TIGR00618 448 TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL--------QETRKKAVVLARLLELQE-----EPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 468 QKCTGILEQGRFER--EKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKL-NEFLELERHNN------NMMAKTLE 538
Cdd:TIGR00618 515 PARQDIDNPGPLTRrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIqQSFSILTQCDNrskediPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 539 ECRVTLEGLKMENGSLKSHLQGEKQKATEASA---VEQTAESCEVQEMLKVARAEKDLLELSCNELRQELL--------- 606
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDlqdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALsirvlpkel 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 607 ---------KANGEIKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 671
Cdd:TIGR00618 675 lasrqlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHieeydrEFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 672 VEQHRAVKLHNNqliSELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKR 751
Cdd:TIGR00618 755 VLKARTEAHFNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
410 420
....*....|....*....|..
gi 1886396456 752 KLLEEEEKNARLQKELGDVQGH 773
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLK 853
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
507-767 |
2.46e-07 |
|
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: 55.12 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 507 EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATE-ASAVEQTAESCEVQEMLK 585
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDlRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 586 varaeKDLLELS---CNELRQELLKANGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK-----LQEKASESDAE 657
Cdd:pfam15921 162 -----EDMLEDSntqIEQLRKMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsaISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 658 IKDMKETIFELEDQVEQHRA---------VKLHNN---QLISELESSVIKLEE-------QKSDLERQLKTLTKQMKEET 718
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLTEkassarsQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1886396456 719 EEWRRFQADLQTAVvvandikCEAQQELRTVKRKLleeEEKNARLQKEL 767
Cdd:pfam15921 313 SMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
963-1006 |
3.07e-07 |
|
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: 49.83 E-value: 3.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLP 1006
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRP 48
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
388-796 |
4.63e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 388 AEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLMNLLQERVKNEEPTTQEgkiiELE 467
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAE----EAK 1463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 468 QKCTgilEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGL 547
Cdd:PTZ00121 1464 KKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 548 KMEngslkshlqgEKQKATEASAVEQTAESCEVQEMLKVARAEKD--LLELSCNELRQELLKANGEIKHVSSLLAKVEKD 625
Cdd:PTZ00121 1541 KAE----------EKKKADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 626 YSYLKEICDHQAEQLSrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLE- 704
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEd 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 705 ---------------RQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKN--ARLQKEL 767
Cdd:PTZ00121 1687 ekkaaealkkeaeeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEE 1766
|
410 420
....*....|....*....|....*....
gi 1886396456 768 GDVQGHGRVVTSRAAPPPVDEEPESSEVD 796
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
579-780 |
7.89e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 579 EVQEMLKVARAEKDLLELSCnELRQELLKANGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 653
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 654 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAV 732
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1886396456 733 VVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSR 780
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-651 |
8.04e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEEnhhsTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 446
Cdd:COG1196 238 EAELEELEAELEELEA----ELEELEAELAELEAE---LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 LQERVKNEEptTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 526
Cdd:COG1196 311 RRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 527 ---RHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScNELRQ 603
Cdd:COG1196 389 leaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL-ELLAE 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1886396456 604 ELLKANGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSRTSLKLQEKA 651
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAArlLLLLEAEADYEGFLEGVKAALLLA 517
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
396-754 |
1.10e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.53 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 396 QELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM-NLLQERvkneeptTQEGKIIELeqkctgiL 474
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRkSLLANR-------FSFGPALDE-------L 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 475 EqgrferEKLLNIQQQLTcslRKVEEENQG----ALEMIKRLKEENEKLNEFLE----LERHNNNMMAKTLEECRVTLEG 546
Cdd:PRK04778 171 E------KQLENLEEEFS---QFVELTESGdyveAREILDQLEEELAALEQIMEeipeLLKELQTELPDQLQELKAGYRE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 547 LKMENGSLKsHLQGEKqkateasaveqtaescEVQEML-KVARAEKDLLELSCNELRQELLKANGEIKHVSSLLakvEKD 625
Cdd:PRK04778 242 LVEEGYHLD-HLDIEK----------------EIQDLKeQIDENLALLEELDLDEAEEKNEEIQERIDQLYDIL---ERE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 626 YSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQLISELESSVIKLEEQK---S 701
Cdd:PRK04778 302 VKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-YTLnESELESVRQLEKQLESLEKQYDEITERIAEQEiayS 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 702 DLERQLKTLTKQMKEETEEWRRFQADLQT---AVVVANDIKCEAQQELRTVKRKLL 754
Cdd:PRK04778 380 ELQEELEEILKQLEEIEKEQEKLSEMLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
475-771 |
1.13e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 475 EQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKT----LEECRVTLEGLKME 550
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDylklNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 551 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMlKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKdysylk 630
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK-KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK------ 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 631 eicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQlKTL 710
Cdd:pfam02463 322 -----EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL-KEE 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 711 TKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 771
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
367-756 |
1.59e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEeLQATLQELsdqQQMVQELTAENEKLVD-EKTILE-TSFHQHRERA-EQLSQENEKL 443
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQ-LESTKEML---RKVVEELTAKKMTLESsERTVSDlTASLQEKERAiEATNAEITKL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 444 MNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNI-QQQLTCSLRKVEEENQGA----LEMIKRLKEENEK 518
Cdd:pfam15921 523 RSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIlRQQIENMTQLVGQHGRTAgamqVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 519 LNEFLELERHNNNMMAKTLE-ECRVtleglkmengslkSHLQGEKQKATEASAveqtaescevqEMLkvaRAEKDLlels 597
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRElEARV-------------SDLELEKVKLVNAGS-----------ERL---RAVKDI---- 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 598 cNELRQELLKangEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRA 677
Cdd:pfam15921 652 -KQERDQLLN---EVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMK 727
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886396456 678 VKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRKLLEE 756
Cdd:pfam15921 728 VAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-772 |
3.43e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 443
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 444 -------MNLLQERV--KNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCS-------------------- 494
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 495 ---------------------LRKVEEENQGALEM--------------------IKRLKEENEKLNEFLELER------ 527
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAGRATFLPLNKmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 528 -------------------------------HNNNMMAKTLEECR--------VTLEGL------KMENGSLKSHLQGEK 562
Cdd:TIGR02169 589 dlsilsedgvigfavdlvefdpkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 563 QKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSR 642
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 643 TSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 719
Cdd:TIGR02169 749 LEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 720 EWRRFQADLQTAVVVANDIK------CEAQQELRTVKRKLLEEEEKNA----RLQKELGDVQG 772
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
963-1028 |
3.89e-06 |
|
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: 46.55 E-value: 3.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 963 SKRNALLKWCQKKTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIpyqELNSQEKSLCLFNLEE 1028
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLI---DMNKVYRQTNLENLDQ 64
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
509-767 |
4.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 509 IKRLKEENEKLNEFLELErhnnnmmaKTLEECRVTLEGLKMEngSLKSHLqgEKQKATEASAVEQ----TAESCEVQEML 584
Cdd:TIGR02168 202 LKSLERQAEKAERYKELK--------AELRELELALLVLRLE--ELREEL--EELQEELKEAEEEleelTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 585 KVARAEKDLLELSCNELRQELLKANGEI-------KHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAE 657
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEIsrleqqkQILRERLANLERQLEELEA----QLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 658 IKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQ----------MKEETEEWRRFQAD 727
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEierlearlerLEDRRERLQQEIEE 425
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1886396456 728 LQTAVVVANdiKCEAQQELRTVKRKLLEEEEKNARLQKEL 767
Cdd:TIGR02168 426 LLKKLEEAE--LKELQAELEELEEELEELQEELERLEEAL 463
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
356-766 |
4.59e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 50.74 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 356 STAGSSPNSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQ 435
Cdd:pfam02463 126 ESQGISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 436 LSQENEKLMNLLQERVKneepttqEGKIIELEQKctGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEE 515
Cdd:pfam02463 206 AKKALEYYQLKEKLELE-------EEYLLYLDYL--KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 516 NEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKateasaveqtaescevqemlkvarAEKDLLE 595
Cdd:pfam02463 277 EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK------------------------AEKELKK 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 596 LSCNELRQELLKANGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQH 675
Cdd:pfam02463 333 EKEEIEELEKELKELEIK---REAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 676 RAVKLHNNQLISELESSVI--KLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKL 753
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
410
....*....|...
gi 1886396456 754 LEEEEKNARLQKE 766
Cdd:pfam02463 490 LSRQKLEERSQKE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-800 |
4.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNL 446
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 LQERvkNEEPTTQEGKIIELEQKctgILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELE 526
Cdd:COG1196 423 LEEL--EEALAELEEEEEEEEEA---LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 527 RHNNNMMAKTLE-ECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELScNELRQEL 605
Cdd:COG1196 498 EAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRATF 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 606 LKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLH---N 682
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegG 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 683 NQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNAR 762
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
410 420 430
....*....|....*....|....*....|....*...
gi 1886396456 763 LQKELGDVQGHGRVVTSRAAPPPVDEEPESSEVDAAGR 800
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
435-767 |
4.99e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 435 QLSQENEKLMNL---LQERVKNEEPTTQEG-KIIELEQKCtgiLEQGRFEREKL-LNIQQQLTCSlRKVEEENQGALEMI 509
Cdd:pfam05483 82 KLYKEAEKIKKWkvsIEAELKQKENKLQENrKIIEAQRKA---IQELQFENEKVsLKLEEEIQEN-KDLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 510 KRLKE----ENEKLNEFlELERH---------NNNM--MAKTLEECRVTLEGLKME-NGSLK------SHLQGEKQKatE 567
Cdd:pfam05483 158 NLLKEtcarSAEKTKKY-EYEREetrqvymdlNNNIekMILAFEELRVQAENARLEmHFKLKedhekiQHLEEEYKK--E 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 568 ASAVEQTAESCEVQEMLKVARAeKDLLELscneLRQELLKANgEIKHVSSLLAKVEKDysyLKEICDHQAEQLSRTSLKL 647
Cdd:pfam05483 235 INDKEKQVSLLLIQITEKENKM-KDLTFL----LEESRDKAN-QLEEKTKLQDENLKE---LIEKKDHLTKELEDIKMSL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 648 QEKASESDAEIKDMK---ETIFEL----EDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEE 720
Cdd:pfam05483 306 QRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITME 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1886396456 721 WRRFQADLQTAVVVANDIKCEAqQELRTV---KRKLLEEEEKNARLQKEL 767
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEKKQFEKIAEEL 434
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
495-796 |
5.84e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 495 LRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQT 574
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARE--------RLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 575 AESCEVQEMLKVARAEKDLLELSCN--------ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLK 646
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 647 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKlhnNQLISELESsvikLEEQKSDLERQLKTLTKQMKEETEEWR---R 723
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIAS----LERRKSNIPARLLALRDALAEALGLDEaelP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 724 FQADL----------QTAVVVAndikceaqqeLRTVKRKLLEEEEKNARLQKELGDVQGHGRVVTSRAAPPPVDEEPESS 793
Cdd:COG4913 462 FVGELievrpeeerwRGAIERV----------LGGFALTLLVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRL 531
|
...
gi 1886396456 794 EVD 796
Cdd:COG4913 532 DPD 534
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
480-770 |
8.52e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 480 EREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmmAKTLEECRVTLEGLKMENGSLKSHLQ 559
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE----VKELEELKEEIEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 560 G--EKQKATEASAVEQTAESCEVQEmlKVARAEK-DLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDhQ 636
Cdd:PRK03918 256 KleEKIRELEERIEELKKEIEELEE--KVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-E 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 637 AEQLSRTSLKLQEKASESDAEIKDMK------ETIFELEDQVEQHRAVKLHNNqlISELESSVIKLEEQKSDLERQLKTL 710
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 711 TkqmkEETEEWRRFQADLQTAVvvaNDIKcEAQQELRTVKRKLLEEEEKN--ARLQKELGDV 770
Cdd:PRK03918 411 T----ARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEEHRKEllEEYTAELKRI 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
389-776 |
9.24e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 389 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLMNL--LQERVKNEEPTTQEGKIIEL 466
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 467 EQKctgiLEQGRFEREKLLNIQQQLTcslRKVEEENQGALEMIKRLKEENEKLNEFLELERhnnNMMAKTLEECRVTLEG 546
Cdd:TIGR02169 236 ERQ----KEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 547 LKMENGSLKSHLQ--GEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAK-VE 623
Cdd:TIGR02169 306 LERSIAEKERELEdaEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 624 KDYSYLKEICD--HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKS 701
Cdd:TIGR02169 386 ELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 702 DLERQLKTLTKQMKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHGRV 776
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
372-716 |
1.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 372 SLTEKIQKMEENH---HSTAEELQATLQ----ELSDQQQMVQELTAE----NEKLVDEKTILETSFHQHRERAEQLSQEN 440
Cdd:PRK02224 346 SLREDADDLEERAeelREEAAELESELEeareAVEDRREEIEELEEEieelRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 441 EKLMNL------LQERVKNEEPTTQEGKIIELEQKCTG-----ILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEM- 508
Cdd:PRK02224 426 EREAELeatlrtARERVEEAEALLEAGKCPECGQPVEGsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLv 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 509 -----IKRLKEENEKLNEFLElERHNnnmmakTLEECRVTLEGLKMENGSLKSHLQGEKQKATEAsavEQTAEscEVQEM 583
Cdd:PRK02224 506 eaedrIERLEERREDLEELIA-ERRE------TIEEKRERAEELRERAAELEAEAEEKREAAAEA---EEEAE--EAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 584 LKvaraekdllelSCNELRQELLKANGEIKHVSSLLAKVEKdysylkeiCDHQAEQLSRTSLKLQEKASESDAEIKDMKE 663
Cdd:PRK02224 574 VA-----------ELNSKLAELKERIESLERIRTLLAAIAD--------AEDEIERLREKREALAELNDERRERLAEKRE 634
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 664 TIFELEDQVEQHRAVKLHNN-----QLISELESSVIKLEEQKSDLERQLKTLTKQMKE 716
Cdd:PRK02224 635 RKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
371-667 |
1.22e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 371 ASLTEKIQKMEENH-HSTAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKLmnLLQE 449
Cdd:TIGR00618 602 KLSEAEDMLACEQHaLLRKLQPEQDLQDVRLHLQQCSQ---ELALKLTALHALQLTLTQERVREHALSIRVLPK--ELLA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 450 RVKNEEPTTQEgkiieLEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL-ELERH 528
Cdd:TIGR00618 677 SRQLALQKMQS-----EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQ 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 529 NNNMMAKTLEECRVTLEGLKME--NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELL 606
Cdd:TIGR00618 752 ARTVLKARTEAHFNNNEEVTAAlqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEE 831
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1886396456 607 KANGEIKHVSSLLAKVEKDYSYLKEiCDHQAEQLSRTSLKLQEKasESDAEIKDMKETIFE 667
Cdd:TIGR00618 832 QFLSRLEEKSATLGEITHQLLKYEE-CSKQLAQLTQEQAKIIQL--SDKLNGINQIKIQFD 889
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
390-733 |
1.23e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.40 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 390 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVKNEEPTTQEGKIIE-LE 467
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 468 QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEE----NQGALEMIKRLKEENEKLNEFLELERHNNnmmaKTLEECRVT 543
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEEtrshEAQLQEMRQKHTQALEELTEQLEQAKRNK----ANLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 544 LEGlkmENGSLKSHLQGEKQKATEASAVEQTAEScEVQE-MLKVARAEKDLlelscNELRQELLKANGEIKHVSSLLAKV 622
Cdd:pfam01576 382 LES---ENAELQAELRTLQQAKQDSEHKRKKLEG-QLQElQARLSESERQR-----AELAEKLSKLQSELESVSSLLNEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 623 EKDYSYLKEICDHQAEQLSRTSLKLQEKASESDA------EIKDMKETIFE-LEDQVEQHRAVKLH----NNQL------ 685
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNlstrlrQLEDERNSLQEqLEEEEEAKRNVERQlstlQAQLsdmkkk 532
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 686 ISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEW-------RRFQADLQTAVV 733
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLV 587
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
371-730 |
1.53e-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: 49.27 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 371 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQER 450
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 451 VKNEEPTTQEGKIIELEQKCTGILEQGRFEREKL-LNIQQQLTCS-----------LRKVEEENQGALEMIKRLKEENEK 518
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVeRKIAQQAAKLqgsdldrtvqqVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 519 LNE-----FLELERHNNNM------MAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLK 585
Cdd:TIGR00606 851 LIQdqqeqIQHLKSKTNELkseklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKdqQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 586 VARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEI-----------CDHQAEQLSR---------TSL 645
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETelntvnaqleeCEKHQEKINEdmrlmrqdiDTQ 1010
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 646 KLQEKASESDAEIKDMKETIFELEDQVEQHraVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQ 725
Cdd:TIGR00606 1011 KIQERWLQDNLTLRKRENELKEVEEELKQH--LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 1886396456 726 ADLQT 730
Cdd:TIGR00606 1089 KELRE 1093
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
370-771 |
2.85e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEEN-HHSTAEELQATLQELSDQQQMVQELTAENEklvdektilETSFHQHRERAEQLSQENEKLMNLLQ 448
Cdd:TIGR00606 593 LAKLNKELASLEQNkNHINNELESKEEQLSSYEDKLFDVCGSQDE---------ESDLERLKEEIEKSSKQRAMLAGATA 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 449 ERVKNEEPTTQEgkiielEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERH 528
Cdd:TIGR00606 664 VYSQFITQLTDE------NQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 529 NNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESC--------EVQEMLK---------VARAEK 591
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKdverkiaqqAAKLQG 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 592 DLLELSCNELRQELLKANGEIKHVSS---LLAKVEKDY--------SYLKEICDH---------QAEQLSRTSLKLQEKA 651
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSkieLNRKLIQDQqeqiqhlkSKTNELKSEklqigtnlqRRQQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 652 SESDAEIKDMKETIFELE-----DQVEQHRAV-KLHNNQLISELESSVIK--------------------LEEQKSDLER 705
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLEtflekDQQEKEELIsSKETSNKKAQDKVNDIKekvknihgymkdienkiqdgKDDYLKQKET 977
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 706 QLKTLTKQMKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRKLLEEEEKNARLQKELGDVQ 771
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
967-1028 |
5.09e-05 |
|
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: 43.24 E-value: 5.09e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 967 ALLKWCQKKTQGYAnIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEKSLclfNLEE 1028
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRE---NLED 64
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
565-802 |
5.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 565 ATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTS 644
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 645 LKLQEKASESDAEIKDM------------------KETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQ 706
Cdd:COG4942 93 AELRAELEAQKEELAELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 707 LKTLTKQMKEETEEwrrfQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQghgrvvtsRAAPPPV 786
Cdd:COG4942 173 RAELEALLAELEEE----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE--------AEAAAAA 240
|
250
....*....|....*.
gi 1886396456 787 DEEPESSEVDAAGRWP 802
Cdd:COG4942 241 ERTPAAGFAALKGKLP 256
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
440-771 |
5.70e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 440 NEKLMNLLQERVKNEEPTTQEGKiieLEQKCTGILEQGRFEREKL-LNIQQQLTCSLRKVEEENQgalEMIKRLKEENEK 518
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFI---KLQPLLSLLGSRKEYRSYLaCIIKLQKTIKREKKLRETE---EVEFSLKAEVLI 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 519 LNEFLELERHNnnmMAKTLEECRVTLEGL-KMENgsLKSHLQGEKQKATEASAVEQTAEscevqemlkvaRAEKDLLELS 597
Cdd:COG5022 849 QKFGRSLKAKK---RFSLLKKETIYLQSAqRVEL--AERQLQELKIDVKSISSLKLVNL-----------ELESEIIELK 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 598 CNElrQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTsLKLQEkasesdaEIKDMKETIFELEDQVEQHRA 677
Cdd:COG5022 913 KSL--SSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL-NKLHE-------VESKLKETSEEYEDLLKKSTI 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 678 VKLHNNQLISELESSVIKLEEQKSDLERqLKTLTKQMKEEteewRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEE 757
Cdd:COG5022 983 LVREGNKANSELKNFKKELAELSKQYGA-LQESTKQLKEL----PVEVAELQSASKIISSESTELSILKPLQKLKGLLLL 1057
|
330
....*....|....
gi 1886396456 758 EKNaRLQKELGDVQ 771
Cdd:COG5022 1058 ENN-QLQARYKALK 1070
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
369-767 |
6.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 369 SLASLTEKIQKMEE-NHHSTAEELQATLQELSDQqqmVQELTAENEKLVDEKTILETSFHQHRERAEQLS---QENEKLM 444
Cdd:PRK02224 188 SLDQLKAQIEEKEEkDLHERLNGLESELAELDEE---IERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 445 NLLQERVKN-----EEPTTQEGKIIELEQKCTGILEQGRFE----------REKLLNIQQQLTCSLRKVEEENQGALEMI 509
Cdd:PRK02224 265 ETIAETEREreelaEEVRDLRERLEELEEERDDLLAEAGLDdadaeavearREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 510 KRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLkshlqgEKQKATEASAVEQTAESCE-VQEMLKVAR 588
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL------EEEIEELRERFGDAPVDLGnAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 589 AEKDLLELSCNELRQELLKANGEIKHVSSLLAK---------VEKdysylKEICDHQAEQlsrtslklQEKASESDAEIK 659
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpVEG-----SPHVETIEED--------RERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 660 DMKETIFELEDQVEqhRAVKLhnnqliSELESSVIKLEEQKSDLERQL---KTLTKQMKEETEEWRRFQADLQTAVVVAN 736
Cdd:PRK02224 486 DLEEEVEEVEERLE--RAEDL------VEAEDRIERLEERREDLEELIaerRETIEEKRERAEELRERAAELEAEAEEKR 557
|
410 420 430
....*....|....*....|....*....|.
gi 1886396456 737 DIKCEAQQELRTVKRKLLEEEEKNARLQKEL 767
Cdd:PRK02224 558 EAAAEAEEEAEEAREEVAELNSKLAELKERI 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
600-782 |
7.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 600 ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRtslklQEKASESDAEIKDMKETIFELEDQVEQHRAvk 679
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQE----RREALQR-----LAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 680 lhNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEK 759
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180
....*....|....*....|...
gi 1886396456 760 NARLQKELGDVQGHGRVVTSRAA 782
Cdd:COG4913 761 DAVERELRENLEERIDALRARLN 783
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
370-720 |
7.89e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.89 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEEnhhstaeELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQE 449
Cdd:TIGR00618 551 LTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQP 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 450 RVKNEEPTTQEGKIIELEQKctgileqgrferEKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 529
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL------------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 530 NNMMAKTLEECRVTLEGLKMENGSLKSHLQgEKQKATEASAVEQTAESCEVQEMLKVARAEKDllelscnelrqELLKAN 609
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAREDALNQSLKELMHQAR-----------TVLKAR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 610 GEIKHVSSLLAKVE----KDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHNnqL 685
Cdd:TIGR00618 760 TEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLS--R 836
|
330 340 350
....*....|....*....|....*....|....*...
gi 1886396456 686 ISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEE 720
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQL 874
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
363-762 |
8.25e-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: 46.65 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 363 NSVSELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSQENE- 441
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEv 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 442 --------------------KLMNLLQERVKN------------------------EEPTTQEGKIIELEQK---CTGIL 474
Cdd:pfam15921 279 eitgltekassarsqansiqSQLEIIQEQARNqnsmymrqlsdlestvsqlrselrEAKRMYEDKIEELEKQlvlANSEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 475 EQGRFEREKL------LNIQ-QQLTCSLRKVEEENQGALEMIKRLKEE---NEKLNEFLELERHNNNMMAKTLEecrVTL 544
Cdd:pfam15921 359 TEARTERDQFsqesgnLDDQlQKLLADLHKREKELSLEKEQNKRLWDRdtgNSITIDHLRRELDDRNMEVQRLE---ALL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 545 EGLKME-NGSLKSHL---QGEKQKATEASAVEQTAESceVQEMLK------------VARAEKDLLEL--SCNELRQELL 606
Cdd:pfam15921 436 KAMKSEcQGQMERQMaaiQGKNESLEKVSSLTAQLES--TKEMLRkvveeltakkmtLESSERTVSDLtaSLQEKERAIE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 607 KANGEIKHVSSLLAKVEKDYSYLKEICDH-QAEQLSRTSLKLQekASESDAEIKDMKETIFELEDQVEQH----RAVKLH 681
Cdd:pfam15921 514 ATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKLQ--MAEKDKVIEILRQQIENMTQLVGQHgrtaGAMQVE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 682 NNQLISELESSVIKLEEqksdlerqLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVK--RKLLEEEEK 759
Cdd:pfam15921 592 KAQLEKEINDRRLELQE--------FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKqeRDQLLNEVK 663
|
...
gi 1886396456 760 NAR 762
Cdd:pfam15921 664 TSR 666
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
366-649 |
9.29e-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: 46.65 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 366 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER---AEQLSQENEK 442
Cdd:pfam15921 494 SERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKdkvIEILRQQIEN 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 LMNL-----------------LQERVKNEEPTTQEGKII---------ELEQKCTGIleqgRFEREKLLNIQQQLTCSLR 496
Cdd:pfam15921 574 MTQLvgqhgrtagamqvekaqLEKEINDRRLELQEFKILkdkkdakirELEARVSDL----ELEKVKLVNAGSERLRAVK 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 497 KVEEENQGALEMIKRLKEENEKLNEFLELERHNnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEK-------------- 562
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdgham 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 563 ------QKATEASAVEQTAESCEVQ---EMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIC 633
Cdd:pfam15921 727 kvamgmQKQITAKRGQIDALQSKIQfleEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
330
....*....|....*.
gi 1886396456 634 DHQAEQLSRTSLKLQE 649
Cdd:pfam15921 807 ANMEVALDKASLQFAE 822
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
474-727 |
9.60e-05 |
|
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: 45.57 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 474 LEQGRFEREKLLniqQQLTCSLRKVE----------EENQGALEMIKRLKEENEKLNEFLEL----ERHNNNMMAKTLE- 538
Cdd:pfam15905 85 LVQERGEQDKRL---QALEEELEKVEaklnaavrekTSLSASVASLEKQLLELTRVNELLKAkfseDGTQKKMSSLSMEl 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 539 -ECRVTLEGlKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVAraEKDLLELSCNElrQELLKANGEIKHVSS 617
Cdd:pfam15905 162 mKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST--EKEKIEEKSET--EKLLEYITELSCVSE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 618 LLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveqhravklhnnqliSELESSVIKLE 697
Cdd:pfam15905 237 QVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE-----------------SEKEELLREYE 299
|
250 260 270
....*....|....*....|....*....|
gi 1886396456 698 EQKSDLERQLKTLTKQMKEETEEWRRFQAD 727
Cdd:pfam15905 300 EKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
966-1002 |
1.11e-04 |
|
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: 42.29 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1886396456 966 NALLKWCQKKTQgyaNIDITNFSSSWSDGLAFCALLH 1002
Cdd:cd21185 4 KATLRWVRQLLP---DVDVNNFTTDWNDGRLLCGLVN 37
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
473-765 |
1.12e-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: 46.50 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 473 ILEQGRFEREKLLNIQQ--QLTCSLRKVEEENQGAL---EMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTL--- 544
Cdd:TIGR00618 148 LLPQGEFAQFLKAKSKEkkELLMNLFPLDQYTQLALmefAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLeke 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 545 -----EGLKMENGSLkSHLQGEKQKATEASAVEQTAEscEVQEMLKVARAEKDLLELSCNEL--RQELLKANGEIKHVSS 617
Cdd:TIGR00618 228 lkhlrEALQQTQQSH-AYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVTQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 618 LLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaEIKDMKETIF----ELEDQVEQHRAVKLHNNQLISELEsSV 693
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE--EQRRLLQTLHsqeiHIRDAHEVATSIREISCQQHTLTQ-HI 381
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1886396456 694 IKLEEQKSDLERQLKTLTKQMKEETEEWRRF------QADLQTAVVVANDiKCEAQQELRTVKRKLLEEEEKNARLQK 765
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtsaFRDLQGQLAHAKK-QQELQQRYAELCAAAITCTAQCEKLEK 458
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
355-596 |
1.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 355 CSTAGSSPNSVSELS--LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRER 432
Cdd:COG4942 12 ALAAAAQADAAAEAEaeLEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 433 AEQLSQENEKLMNLLQERVKNeepttqegkiieleqkctgILEQGRFEREKLLNIQQQLTCSLRkveeenqgALEMIKRL 512
Cdd:COG4942 92 IAELRAELEAQKEELAELLRA-------------------LYRLGRQPPLALLLSPEDFLDAVR--------RLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 513 KEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKD 592
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
....
gi 1886396456 593 LLEL 596
Cdd:COG4942 225 LEAL 228
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
968-1010 |
1.95e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.90 E-value: 1.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1886396456 968 LLKWCQK--KTQGYANIDITNFSSSWSDGLAFCALLHTYLPAHIP 1010
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCD 59
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
534-739 |
2.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 534 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES--CEVQEMLKVARAEKDLLELSCNELRQELLKANGE 611
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 612 IKHVSSLLAKV-------------------------EKDYSYLKEICDH---QAEQLSRTSLKLQEKASESDAEIKDMKE 663
Cdd:COG4942 99 LEAQKEELAELlralyrlgrqpplalllspedfldaVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1886396456 664 TIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIK 739
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
534-766 |
3.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 534 AKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAEscevqEMLKVARAEKDLLELscNELRQELLKANGEIK 613
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAEREIAEL--EAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 614 HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASE--------SDAEIKDMKETIFELEDQVEQHrAVKLHNNQL 685
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrlEAAEDLARLELRALLEERFAAA-LGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 686 ISELESSVIKLEEQKSDLERQLktlTKQMKEETEEWRRFQADLQTAVVVANDIkceaQQELRTVKRKLLEE-EEKNARLQ 764
Cdd:COG4913 768 RENLEERIDALRARLNRAEEEL---ERAMRAFNREWPAETADLDADLESLPEY----LALLDRLEEDGLPEyEERFKELL 840
|
..
gi 1886396456 765 KE 766
Cdd:COG4913 841 NE 842
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
367-731 |
3.55e-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: 44.83 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqMVQELTAENEKLVDEKTILETSFHQHR----ERAEQLSQENEK 442
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE--LNGELSAADAAVAKDRSELEALEDQHGafldADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 L------MNLLQERVK---------NEEPTTQEGKIIE-LEQKCTGI---LEQGRFEREKLL----NIQQQLTCSLRKVE 499
Cdd:pfam12128 349 LpswqseLENLEERLKaltgkhqdvTAKYNRRRSKIKEqNNRDIAGIkdkLAKIREARDRQLavaeDDLQALESELREQL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 500 EE-----NQGALEMIKRLKEENEKLN------EFLELERHNN---NMMAKTLEECRVTLEGLKMENGSLKSHL--QGEKQ 563
Cdd:pfam12128 429 EAgklefNEEEYRLKSRLGELKLRLNqatatpELLLQLENFDeriERAREEQEAANAEVERLQSELRQARKRRdqASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 564 KATEASAVEQTAESCEVQEML-----------------------KVARAE----------------KDLLELSCNELRQE 604
Cdd:pfam12128 509 RQASRRLEERQSALDELELQLfpqagtllhflrkeapdweqsigKVISPEllhrtdldpevwdgsvGGELNLYGVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 605 LLKANGEIKHVSSL---LAKVEKDYSYLKEICDHQAEQLSRTSLKLQE-KASESDAE--IKDMKETIFELEDQveqHRAV 678
Cdd:pfam12128 589 RIDVPEWAASEEELrerLDKAEEALQSAREKQAAAEEQLVQANGELEKaSREETFARtaLKNARLDLRRLFDE---KQSE 665
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 679 KLHNNQLISELESSViklEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTA 731
Cdd:pfam12128 666 KDKKNKALAERKDSA---NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
551-717 |
4.71e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 551 NGSLKSHLQGEKQKATEASAVEQTAEScEVQEMLKVARAE-KDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYL 629
Cdd:PRK12705 18 LGVLVVLLKKRQRLAKEAERILQEAQK-EAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 630 KEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRavklhNNQLISELEssvikleeqkSDLERQLKT 709
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQA-----RKLLLKLLD----------AELEEEKAQ 161
|
....*...
gi 1886396456 710 LTKQMKEE 717
Cdd:PRK12705 162 RVKKIEEE 169
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
363-768 |
5.94e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 363 NSVSELSlASLTEKIQKMEENHHS----TAEELQATLQElsDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLsQ 438
Cdd:PRK04863 796 EELAERY-ATLSFDVQKLQRLHQAfsrfIGSHLAVAFEA--DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQA-K 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 439 ENEKLMNLLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE--KLLNIQQQLTCSLRKVEEEnqgaLEMIKRLKEEN 516
Cdd:PRK04863 872 EGLSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQhgNALAQLEPIVSVLQSDPEQ----FEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 517 EKlneflelERHNNNMMAKTLEECRVTLEGLKMENgslkshlqgekqkateasAVEQTAESCEVQEMLkvaRAEKDLLEL 596
Cdd:PRK04863 948 QQ-------TQRDAKQQAFALTEVVQRRAHFSYED------------------AAEMLAKNSDLNEKL---RQRLEQAEQ 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 597 SCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmketifELEDQVEQHR 676
Cdd:PRK04863 1000 ERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRD------ELHARLSANR 1073
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 677 AVKlhnNQLiselessviklEEQKSDLERQLKTLTKQMKEETEEWRrfqaDLQTAVVVANDIKCEAQQELRT--VKRKLL 754
Cdd:PRK04863 1074 SRR---NQL-----------EKQLTFCEAEMDNLTKKLRKLERDYH----EMREQVVNAKAGWCAVLRLVKDngVERRLH 1135
|
410 420
....*....|....*....|.
gi 1886396456 755 EEE-------EKNARLQKELG 768
Cdd:PRK04863 1136 RRElaylsadELRSMSDKALG 1156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
579-778 |
6.07e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 579 EVQEMLKVARAEKDllelSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEIcdHQAEQLSRTSLKLQEKASESDAEI 658
Cdd:COG4717 75 ELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 659 KDMKETIFELEDQVEQhravklhnnqlISELESSVIKLEEQKSDLERQLKTLT----KQMKEETEEWRRFQADLQTAVVV 734
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeeelQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1886396456 735 ANDIKCEAQQELRTVKRKLLEEEEKNaRLQKELGDVQGHGRVVT 778
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLA 260
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
388-771 |
8.07e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.41 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 388 AEELQATLQELSDQQQMVQELTAENEKL----VDEKTILETSFHQHRERAEQLSQENEKLMNLlqeRVKNEEPTTQEGKI 463
Cdd:COG5185 116 ADILISLLYLYKSEIVALKDELIKVEKLdeiaDIEASYGEVETGIIKDIFGKLTQELNQNLKK---LEIFGLTLGLLKGI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 464 IELE----QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEE 539
Cdd:COG5185 193 SELKkaepSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 540 CRVTLEGLKMENGSLKShlqgekqkateasAVEQTAEscEVQEMLKVARAEKDLLELScnelrqELLKANGEIKHVSSLL 619
Cdd:COG5185 273 NAESSKRLNENANNLIK-------------QFENTKE--KIAEYTKSIDIKKATESLE------EQLAAAEAEQELEESK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 620 AKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAE--IKDMKETIFELEDQVE--------QHRAVKLHNNQLISEL 689
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEveLSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 690 ESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQElrTVKRKLLEEEEKNARLQKELGD 769
Cdd:COG5185 412 EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELTQ 489
|
..
gi 1886396456 770 VQ 771
Cdd:COG5185 490 IE 491
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
375-767 |
8.62e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 375 EKIQKMEENHHSTAEELQatlQELSDQQQMVQELTAENEKLVDEKTILetsfhqhreraeqlsqENEKLMNLLQERVKNE 454
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTEL----------------LVEQGRLQLQADRHQE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 455 EPTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTCSLRKVEEENQGalemikrlKEENEKLNEFLELERhnnnMMA 534
Cdd:TIGR00606 362 HIRARDSLIQSLATR----LELDGFERGPFSERQIKNFHTLVIERQEDEA--------KTAAQLCADLQSKER----LKQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 535 KTLEECRVTLEGLKMEngslkshLQGEKQKATEasavEQTAESCEVQEMLKVARAEKDLLELScnelrQELLKANGEIkh 614
Cdd:TIGR00606 426 EQADEIRDEKKGLGRT-------IELKKEILEK----KQEELKFVIKELQQLEGSSDRILELD-----QELRKAEREL-- 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 615 vsSLLAKVEKDYSYLKEICDHQAEQ--LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESS 692
Cdd:TIGR00606 488 --SKAEKNSLTETLKKEVKSLQNEKadLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 693 VIKLEEQKSdLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQ---QELRTVKRKLLE------EEEKNARL 763
Cdd:TIGR00606 566 LGYFPNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEskeEQLSSYEDKLFDvcgsqdEESDLERL 644
|
....
gi 1886396456 764 QKEL 767
Cdd:TIGR00606 645 KEEI 648
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
367-736 |
9.25e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTILETS-FHQHRERAEQLSQENEKLMN 445
Cdd:COG5185 214 NLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDLRLEkLGENAESSKRLNENANNLIK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 446 LLQERVKNEEPTTQEGKIIELEQKCTGILEQGRFERE---KLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEF 522
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 523 LELERhnnnmMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKAteASAVEQTAESCEVQEmlkvaraekdllelscNELR 602
Cdd:COG5185 370 VELSK-----SSEELDSFKDTIESTKESLDEIPQNQRGYAQEI--LATLEDTLKAADRQI----------------EELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 603 QELLKANGEIKHVSSLLAKVEKDYSylKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvklhn 682
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKA----- 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 683 nqliselessviKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVAN 736
Cdd:COG5185 500 ------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
424-762 |
9.96e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 424 TSFHQHRERAE-QLSQENEKLMNLLQERVKNEEPTT--QEGKIIEL---EQKCTGILEQGRFER----EKLLNIQQQLTC 493
Cdd:PLN02939 91 TSSDDDHNRASmQRDEAIAAIDNEQQTNSKDGEQLSdfQLEDLVGMiqnAEKNILLLNQARLQAledlEKILTEKEALQG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 494 SLRKVEEENQGALEMIKRLKEEN---EKLNEFLELERHNNNMMAKTLEECRVT----LEGLKMENGSLKSHLQGEKqkaT 566
Cdd:PLN02939 171 KINILEMRLSETDARIKLAAQEKihvEILEEQLEKLRNELLIRGATEGLCVHSlskeLDVLKEENMLLKDDIQFLK---A 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 567 EASAVEQTAESCEVQEmlkvarAEKDLLELSCNELRQELLKANGEIKHVSSL-----LAKVEKdysyLKEICDHQAEQLS 641
Cdd:PLN02939 248 ELIEVAETEERVFKLE------KERSLLDASLRELESKFIVAQEDVSKLSPLqydcwWEKVEN----LQDLLDRATNQVE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 642 RTSLKLQEKasesdaeiKDMKETIFELEDQVEqhravklhnnqliselESSVIKLEEQKSDLerqlktLTKQMKEETEEW 721
Cdd:PLN02939 318 KAALVLDQN--------QDLRDKVDKLEASLK----------------EANVSKFSSYKVEL------LQQKLKLLEERL 367
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1886396456 722 RRFQADLQTAVVVANDIKCEAQQELrtvkRKLLEEEEKNAR 762
Cdd:PLN02939 368 QASDHEIHSYIQLYQESIKEFQDTL----SKLKEESKKRSL 404
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-757 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 591 KDLLELScnELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELED 670
Cdd:COG1579 7 RALLDLQ--ELDSELDRLEHRLKELPAELAELEDELAALEA----RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 671 QVEQHRAVKLHNN---------QLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVvandiKCE 741
Cdd:COG1579 81 QLGNVRNNKEYEAlqkeieslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA-----ELE 155
|
170
....*....|....*.
gi 1886396456 742 AQQELRTVKRKLLEEE 757
Cdd:COG1579 156 AELEELEAEREELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-772 |
1.57e-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: 42.74 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDE------------KTI--LETSFHQHRER 432
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqiaslnNEIerLEARLERLEDR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 433 AEQLSQENEKLMNLLQERVKNEEPTTQEGKIIELE--QKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIK 510
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEelQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 511 RLKEENEKLNEFLELERHNNNMMAKTLEecrVTLEGLKMENG---SLKSHLQGEKQKA--TEASAVEQTAESCEVQEMLK 585
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILG---VLSELISVDEGyeaAIEAALGGRLQAVvvENLNAAKKAIAFLKQNELGR 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 586 VARAEKDL-----LELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYL---------KEICDHQAEQL----------- 640
Cdd:TIGR02168 573 VTFLPLDSikgteIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddLDNALELAKKLrpgyrivtldg 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 641 -------------SRTSLKLQEKasesDAEIKDMKETIFELEDQV-EQHRAVKLHNNQLiSELESSVIKLEEQKSDLERQ 706
Cdd:TIGR02168 653 dlvrpggvitggsAKTNSSILER----RREIEELEEKIEELEEKIaELEKALAELRKEL-EELEEELEQLRKELEELSRQ 727
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886396456 707 LKTLTKQMKEETEE---WRRFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQG 772
Cdd:TIGR02168 728 ISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-726 |
1.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLM---NL 446
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAarlLL 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 LQERVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSL-----RKVEEENQGALEMIKRLKEENEKLNE 521
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 522 FLELER---------------------------------------------------HNNNMMAKTLEEcRVTLEGLKME 550
Cdd:COG1196 576 FLPLDKiraraalaaalargaigaavdlvasdlreadaryyvlgdtllgrtlvaarlEAALRRAVTLAG-RLREVTLEGE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 551 NGSLKSHLQGEKQKATEASAVEQTAESCEVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLK 630
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 631 EICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVklhnNQL-ISELESsvIK-----LEEQKSDLE 704
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPV----NLLaIEEYEE--LEerydfLSEQREDLE 808
|
410 420
....*....|....*....|....*
gi 1886396456 705 RQLKTL---TKQMKEETEEwrRFQA 726
Cdd:COG1196 809 EARETLeeaIEEIDRETRE--RFLE 831
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
373-540 |
1.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 373 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQERVK 452
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 453 NEEP-TTQEGKIIELEQKCTGILEQ-GRFEREKllniQQQLTCSLRKVEEENQGALEmIKRLKEENEklnefLELERHNN 530
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRvAGLTPEQ----ARKLLLKLLDAELEEEKAQR-VKKIEEEAD-----LEAERKAQ 179
|
170
....*....|
gi 1886396456 531 NMMAKTLEEC 540
Cdd:PRK12705 180 NILAQAMQRI 189
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
579-774 |
1.90e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 579 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSL---KLQEKASESD 655
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEeaeELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 656 AEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVA 735
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190
....*....|....*....|....*....|....*....
gi 1886396456 736 NDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQGHG 774
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-717 |
2.11e-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: 41.06 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 579 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVE---------KDY-SYLKEIcDHQAEQLSrtslKLQ 648
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYeALQKEI-ESLKRRIS----DLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1886396456 649 EKASESDAEIKDMKETIFELEDQVEQHRAvklHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEE 717
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
367-730 |
2.30e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 367 ELSLASLTEKIQKMEENHHSTA----EELQATLQE---LSDQQQmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQE 439
Cdd:PRK10246 175 ELTGTEIYGQISAMVFEQHKSArtelEKLQAQASGvalLTPEQV--QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 440 NEkLMNLLQERVKNEEPTTQEgkiieleqkctgiLEQGRFEREKLLNIQ--QQLTCSLRKVEEENQGALEMIKRLKEENE 517
Cdd:PRK10246 253 DE-LQQEASRRQQALQQALAA-------------EEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 518 KLNEFLELERHNNNMMAKTLEECRVTLEGLKmenGSLKSH----LQGEKQKATEASAVEQTAESCEV---QEMLKVARAE 590
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQQSLN---TWLAEHdrfrQWNNELAGWRAQFSQQTSDREQLrqwQQQLTHAEQK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 591 KDL-----LELSCNE-------------LRQELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKAS 652
Cdd:PRK10246 396 LNAlpaitLTLTADEvaaalaqhaeqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 653 ---------ESDAEIKDMKETIFELED-------------QVEQHRAVKLHNNQL-ISELESSVIKLEEQKSDLERQLKT 709
Cdd:PRK10246 476 qladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrLDALEKEVKKLGEEGAALRGQLDA 555
|
410 420
....*....|....*....|.
gi 1886396456 710 LTKQMKEETEEWRRFQADLQT 730
Cdd:PRK10246 556 LTKQLQRDESEAQSLRQEEQA 576
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
683-766 |
2.38e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 683 NQLISELESSVIKLEEQKSDLE---RQLKTLTKQMKEETEEWR-RFQADLQTAVVVANDIKCEAQQELRTVKRKLLEEEE 758
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQeEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
....*...
gi 1886396456 759 KNARLQKE 766
Cdd:PRK00409 599 GGYASVKA 606
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
366-671 |
2.46e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 366 SELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL 443
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEA 814
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 444 MNLLQErvknEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslrkvEEENQGALEMIKRLKEENEKLNEFL 523
Cdd:pfam02463 815 ELLEEE----QLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELER-------LEEEITKEELLQELLLKEEELEEQK 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 524 ELERhnnnmmaKTLEECRVTLEGLKMENGSLKSHLQGEKQKA----TEASAVEQTAESCEVQEMLKVARAEKDLLELSCN 599
Cdd:pfam02463 884 LKDE-------LESKEEKEKEEKKELEEESQKLNLLEEKENEieerIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1886396456 600 ELRQELLKANGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 671
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
963-1010 |
3.03e-03 |
|
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: 38.13 E-value: 3.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1886396456 963 SKRNALLKWCQKKTQGyanIDITNFSSSWSDGLAFCALLHTYLPAHIP 1010
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCP 45
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
386-551 |
3.07e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 386 STAEELQATLQELSDQQQMVQELTaenEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQErvkneepttQEGKIIE 465
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAAQSQKKI---DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVAS---------QEQEIAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 466 LEQKCTGIleqgrfERekllnIQQQLTCSLrkveeenqgaLEMIKRLKEENEKLNEFLELERHN-----NNMMA----KT 536
Cdd:pfam11932 81 LERQIEEI------ER-----TERELVPLM----------LKMLDRLEQFVALDLPFLLEERQArlarlRELMDdadvSL 139
|
170
....*....|....*
gi 1886396456 537 LEECRVTLEGLKMEN 551
Cdd:pfam11932 140 AEKYRRILEAYQVEA 154
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-550 |
3.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 373 LTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRE---RAEQLSQENEKLMNLLQE 449
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 450 RVKNEEPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLtcslRKVEEENQGALEMIKRLKEENEKLNEFLELERHN 529
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
170 180
....*....|....*....|.
gi 1886396456 530 NNMMAKTLEECRVTLEGLKME 550
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKE 1776
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
169-773 |
3.89e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 169 QVRELLAEAKAKDSEINRLRSELKKY----KEKRTLNAEGTDALGPNVDGTSVSPGDTEPM----IRALEEKNKNFQKEL 240
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKALksrkKQMEKDNSELELKMEKVFQGTDEQLNDLYHNhqrtVREKERELVDCQREL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 241 SDLEEENRVLKEKLIYL--EHSPNSEGAASHTGDSSCPTSITQESSFGSP-TGNQMSSDIDEYKKNIHgnALRTSGSSSS 317
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELlvEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPFSERQIKNFH--TLVIERQEDE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 318 DVTKASLSPDASDFEHITAEtpsrplsstsnpfKSSKCSTAGSSPNSVSELSLASLTEKIQKME----ENHHSTA----- 388
Cdd:TIGR00606 407 AKTAAQLCADLQSKERLKQE-------------QADEIRDEKKGLGRTIELKKEILEKKQEELKfvikELQQLEGssdri 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 389 ----EELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLMNLLQeRVKNEEPTTQEGK 462
Cdd:TIGR00606 474 leldQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM-LTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 463 IIELEQKCTGILEQGRFEREKLL--------NIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEfLELERHNNNMMA 534
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLedwlhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE-QLSSYEDKLFDV 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 535 KTLEECRVTLEGLKME-NGSLKSHLQGEKQKATEASAVEQTAES----CEVQEmlKVARAEKDLLELScNELRQELLKAN 609
Cdd:TIGR00606 632 CGSQDEESDLERLKEEiEKSSKQRAMLAGATAVYSQFITQLTDEnqscCPVCQ--RVFQTEAELQEFI-SDLQSKLRLAP 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 610 GEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAvKLHNNQLI 686
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnKLQKVNRDIQRLKNDIEEQETLLGTIMP-EEESAKVC 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 687 SELESSVIKLEEQKSDLERQLKTLTKQMKeeteewrrfQADLQTAVVVANDIKCEAQQELRTV------KRKLLEEEEKN 760
Cdd:TIGR00606 788 LTDVTIMERFQMELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVvskielNRKLIQDQQEQ 858
|
650
....*....|....
gi 1886396456 761 AR-LQKELGDVQGH 773
Cdd:TIGR00606 859 IQhLKSKTNELKSE 872
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
647-771 |
4.17e-03 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 39.64 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 647 LQEKASESDAEIKDMKEtifeledqveqhRAVKLHNNQLiseleSSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQA 726
Cdd:PRK10884 59 LQVNANTNYAQIRDSKG------------RTAWIPLKQL-----STTPSLRTRVPDLENQVKTLTDKLNNIDNTWNQRTA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1886396456 727 DLQTAVVVANDIKCEAQQELRTVKRKLLEEEEKNARLQKELGDVQ 771
Cdd:PRK10884 122 EMQQKVAQSDSVINGLKEENQKLKNQLIVAQKKVDAANLQLDDKQ 166
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
372-521 |
5.08e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.39 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 372 SLTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRER------AEQLSQENEKL 443
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQ-LDALQEKLRGLEEENLKLRSEASHLktETDTYEEKEQqlmsdcVEQLSEANQQM 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 444 MNLLQERVK--------NEEPTTQEGKIIELEQKCTGILEqgrfEREKLL-------NIQQQLTCSLRKVEEENQGALEM 508
Cdd:pfam04849 220 AELSEELARkmeenlrqQEEITSLLAQIVDLQHKCKELGI----ENEELQqhlqaskEAQRQLTSELQELQDRYAECLGM 295
|
170
....*....|...
gi 1886396456 509 IKRLKEENEKLNE 521
Cdd:pfam04849 296 LHEAQEELKELRK 308
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
984-1027 |
5.67e-03 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 36.89 E-value: 5.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1886396456 984 ITNFSSSWSDGLAFCALLHTYLPAHIPYQELNSQEK---SLCLFNLE 1027
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKESmslADSLYNIQ 59
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-577 |
7.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL---MNL 446
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELeeqLES 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 447 LQERVKNEEPTTQEGKIIELEQKCTGILEQ--GRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFLE 524
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1886396456 525 LERHNNNMMAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAES 577
Cdd:COG4372 242 LELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALE 294
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
369-755 |
7.55e-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: 40.22 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 369 SLASLTEKIQKMEEnhhstaeelqatlqelsDQQQMVQELTAeneklvdektiLETSFHQHRERAEQLSQENEKLMNLLQ 448
Cdd:pfam06160 87 ALDEIEELLDDIEE-----------------DIKQILEELDE-----------LLESEEKNREEVEELKDKYRELRKTLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 449 ERVKNEEPTtqegkIIELEqkctgileqgrferEKLLNIQQQLTcslrKVEEENQG-----ALEMIKRLKEENEKLNEFL 523
Cdd:pfam06160 139 ANRFSYGPA-----IDELE--------------KQLAEIEEEFS----QFEELTESgdyleAREVLEKLEEETDALEELM 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 524 E-----LERHNNNMMAKtLEECRVTLEGLKMENGSLKsHLQGEKQKAteasaveqtaescEVQEMLKvaRAEKDLLELSC 598
Cdd:pfam06160 196 EdipplYEELKTELPDQ-LEELKEGYREMEEEGYALE-HLNVDKEIQ-------------QLEEQLE--ENLALLENLEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 599 NELRQELLKANGEIKHVSSLLAK-------VEKDYSYLKEICDHQAEQLSRTSLKLQEkasesdaeikdMKETiFEL-ED 670
Cdd:pfam06160 259 DEAEEALEEIEERIDQLYDLLEKevdakkyVEKNLPEIEDYLEHAEEQNKELKEELER-----------VQQS-YTLnEN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 671 QVEQHRAVKLHNNQLISELESSVIKLEEQK---SDLERQLKTLTKQMKEETEEwrrfQADLQTAVVVANDIKCEAQQELR 747
Cdd:pfam06160 327 ELERVRGLEKQLEELEKRYDEIVERLEEKEvaySELQEELEEILEQLEEIEEE----QEEFKESLQSLRKDELEAREKLD 402
|
....*...
gi 1886396456 748 TVKRKLLE 755
Cdd:pfam06160 403 EFKLELRE 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
446-766 |
8.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 446 LLQERVKNE--EPTTQEGKIIELEQKCTGILEQGRFEREKLLNIQQQLTCSLRKVEEENQGALEMIKRLKEENEKLNEFL 523
Cdd:COG4717 46 MLLERLEKEadELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 524 ELERHnnnmmAKTLEECRVTLEGLKMENGSLKSHLQGEKQKATEASAVEQTAESCEvqemlkvaRAEKDLLELSCNELRQ 603
Cdd:COG4717 126 QLLPL-----YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ--------EELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 604 ELLKANGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASEsdAEIKDMKETIF-------------ELED 670
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLiaaallallglggSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 671 QVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVK 750
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330
....*....|....*.
gi 1886396456 751 RKLLEEEEKNARLQKE 766
Cdd:COG4717 351 ELLREAEELEEELQLE 366
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
640-730 |
8.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 640 LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLERQLKTLTKQMKEETE 719
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|.
gi 1886396456 720 EWRRFQADLQT 730
Cdd:COG4942 91 EIAELRAELEA 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
496-761 |
8.59e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 496 RKVEE----ENQGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRvtLEGLKMENGSLKSHlqgEKQKATEASAV 571
Cdd:PTZ00121 1212 RKAEEarkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAE---EARKADELKKA 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 572 EQTAESCEVQEMLKVARAEkdllelscnelrqELLKANGEIKHVSSLLAKVEKdysylkeiCDHQAEQLSRtslKLQEKA 651
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKAD-------------EAKKKAEEAKKADEAKKKAEE--------AKKKADAAKK---KAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 652 SESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESSVIKLEEQKSDLErqLKTLTKQMKEETEEWRRFQADLQTa 731
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKK- 1419
|
250 260 270
....*....|....*....|....*....|
gi 1886396456 732 vvvANDIKCEAQQELRTVKRKLLEEEEKNA 761
Cdd:PTZ00121 1420 ---ADEAKKKAEEKKKADEAKKKAEEAKKA 1446
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
579-728 |
8.76e-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: 39.14 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 579 EVQEMLKVARAEKDLLELSCNELRQELLKANGEIKHVSSLLAKVEKDYSYLKE-ICDHQAEQLSRTSLK----LQEKASE 653
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArIKKYEEQLGNVRNNKeyeaLQKEIES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1886396456 654 SDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELESsviKLEEQKSDLERQLKTLTKQMKEETEEWRRFQADL 728
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
376-713 |
8.78e-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: 40.11 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 376 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDektiletsfhQHRERAEQLSQENEKLMNLlqeRVKNEE 455
Cdd:pfam05557 98 QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE----------RLDLLKAKASEAEQLRQNL---EKQQSS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 456 PTTQEGKIIELEQKctgiLEQGRFEREKLLNIQQQLTcSLRKVEEEnqgalemIKRLKEENEKLNEFLElerhNNNMMAK 535
Cdd:pfam05557 165 LAEAEQRIKELEFE----IQSQEQDSEIVKNSKSELA-RIPELEKE-------LERLREHNKHLNENIE----NKLLLKE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 536 TLEECRVTLEglkmengslkshlQGEKQKATEAS-AVEQTAESCEVQEMLKVARAekdllelSCNELRQELLKANgeikh 614
Cdd:pfam05557 229 EVEDLKRKLE-------------REEKYREEAATlELEKEKLEQELQSWVKLAQD-------TGLNLRSPEDLSR----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 615 vssllakvekdysylkeicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVklhnnqlISELESSVI 694
Cdd:pfam05557 284 ---------------------RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK-------IEDLNKKLK 335
|
330
....*....|....*....
gi 1886396456 695 KLEEQKSDLERQLKTLTKQ 713
Cdd:pfam05557 336 RHKALVRRLQRRVLLLTKE 354
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
370-548 |
9.04e-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: 39.84 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 370 LASLTEKIQKM------EENHHSTAEELQATLQElsdqqqMVQELTAENEKLVDEKTILETSFH-QHREraEQLSQENEK 442
Cdd:pfam06160 265 LEEIEERIDQLydllekEVDAKKYVEKNLPEIED------YLEHAEEQNKELKEELERVQQSYTlNENE--LERVRGLEK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 443 LMNLLQERVKNEEPTTQEGKII---------ELEQKCTGI-------------LEQGRFE-REKLLNIQQQLTCSLRKVE 499
Cdd:pfam06160 337 QLEELEKRYDEIVERLEEKEVAyselqeeleEILEQLEEIeeeqeefkeslqsLRKDELEaREKLDEFKLELREIKRLVE 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1886396456 500 EEN-----QGALEMIKRLKEENEKLNEFLELERHNNNMMAKTLEECRVTLEGLK 548
Cdd:pfam06160 417 KSNlpglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLY 470
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
562-720 |
9.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 562 KQKATEAsavEQTAESCeVQEMLKVARAEKDLLELSCNE----LRQELLKangEIKHVSSLLAKVEKDYSYLKEICDHQA 637
Cdd:PRK12704 30 EAKIKEA---EEEAKRI-LEEAKKEAEAIKKEALLEAKEeihkLRNEFEK---ELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1886396456 638 EQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvKLHNnqlISELESSVIK---LEEQKSDLERQLKTLTKQM 714
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ-ELER---ISGLTAEEAKeilLEKVEEEARHEAAVLIKEI 178
|
....*.
gi 1886396456 715 KEETEE 720
Cdd:PRK12704 179 EEEAKE 184
|
|
| |
