|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
923-1034 |
9.66e-81 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 257.65 E-value: 9.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 923 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGI 1002
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 987976900 1003 KPSLELSEMLHTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
923-1034 |
1.46e-76 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 246.12 E-value: 1.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 923 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGI 1002
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 987976900 1003 KPSLELSEMLHTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
917-1035 |
2.68e-69 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 226.49 E-value: 2.68e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 917 RDPLAALAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEA 996
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 987976900 997 AESVGIKPSLELSEMLHTDRPDWQSVMQYVAQIYKYFET 1035
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
930-1033 |
4.24e-35 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 129.40 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEL 1008
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
932-1033 |
4.23e-34 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 126.30 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 932 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSE 1010
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 987976900 1011 MLH-TDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21200 83 MVRmGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
935-1033 |
1.19e-31 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 119.45 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 935 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELSEMLHT 1014
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 987976900 1015 DRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
933-1033 |
7.90e-31 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 117.00 E-value: 7.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 933 NALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEM 1011
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 987976900 1012 LHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
930-1033 |
1.44e-30 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 116.36 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIkPSLEL 1008
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGI-AKLLD 80
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
926-1033 |
6.87e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 114.55 E-value: 6.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 926 EYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFE-AAESVGIKP 1004
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 987976900 1005 SLELSEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
930-1033 |
1.73e-29 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 113.26 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1008
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
930-1031 |
1.82e-29 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 113.16 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPS-LEL 1008
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQlLDV 80
|
90 100
....*....|....*....|...
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYK 1031
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
934-1034 |
1.96e-28 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 110.13 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 934 ALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEML 1012
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 987976900 1013 HTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
930-1033 |
4.53e-28 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 109.32 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1008
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
932-1031 |
7.41e-28 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 109.02 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 932 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVG-IKPSLELSE 1010
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 987976900 1011 MLHTDRPDWQSVMQYVAQIYK 1031
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
930-1033 |
1.23e-27 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 108.21 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1008
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 987976900 1009 SEML-HTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21258 81 EDMMiMGKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
931-1033 |
1.28e-26 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 104.93 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 931 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLELS 1009
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
935-1033 |
1.50e-26 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 104.93 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 935 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELSEMLHT 1014
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 987976900 1015 DRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
930-1033 |
4.10e-26 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 103.79 E-value: 4.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1008
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLD- 82
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
930-1034 |
4.35e-26 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 103.33 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELS 1009
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
930-1033 |
9.31e-26 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 102.47 E-value: 9.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1008
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21189 80 PEDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
930-1033 |
1.06e-25 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 102.35 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESV-GIKPSLEL 1008
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 987976900 1009 SEMLHTDR-PDWQSVMQYVAQIYKYF 1033
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
932-1033 |
4.85e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 97.63 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 932 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSE 1010
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 987976900 1011 MLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
929-1034 |
6.61e-24 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 97.11 E-value: 6.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 929 GSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1007
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 987976900 1008 LSEMLhTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
930-1034 |
7.85e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 97.33 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEL 1008
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
928-1034 |
8.51e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 97.03 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 928 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSL 1006
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 987976900 1007 ELSEMLHTDRPDWQSVMQYVAQIYKYFE 1034
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
930-1033 |
1.76e-22 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 93.18 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLElS 1009
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82
|
90 100
....*....|....*....|....
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
931-1033 |
2.66e-22 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 92.64 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 931 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLELS 1009
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
930-1033 |
2.97e-22 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 93.20 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1008
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
935-1031 |
4.42e-22 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 92.11 E-value: 4.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 935 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAA-ESVGIKPSLElSEMLH 1013
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 987976900 1014 TDRPDWQSVMQYVAQIYK 1031
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
932-1035 |
2.65e-21 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 90.04 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 932 RNALLKWCQKKTEGY-ANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKR--NLLLAFEAAE-SVGIKPSLE 1007
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83
|
90 100
....*....|....*....|....*...
gi 987976900 1008 LSEMLHTdrPDWQSVMQYVAQIYKYFET 1035
Cdd:pfam00307 84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
930-1033 |
3.20e-21 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 90.14 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1008
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
930-1033 |
7.07e-21 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 89.34 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1008
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
930-1033 |
1.66e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 87.46 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEl 1008
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
928-1033 |
2.83e-20 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 86.99 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 928 GGSKRnALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIkPSL 1006
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI-PRL 81
|
90 100
....*....|....*....|....*..
gi 987976900 1007 ELSEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
930-1033 |
4.10e-20 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 87.06 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1008
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
930-1033 |
5.09e-20 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 86.70 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1008
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
934-1033 |
5.45e-20 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 85.98 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 934 ALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLELSEmL 1012
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 987976900 1013 HTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
930-1033 |
1.42e-19 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 85.51 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLEL 1008
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
930-1033 |
2.74e-18 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 81.19 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLElS 1009
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
933-1029 |
4.50e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 80.44 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 933 NALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY----QELSSQEKKRNLLLAFEAAESVGIKPSLEL 1008
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQI 1029
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
917-1035 |
1.71e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 84.22 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 917 RDPLAALAREYGGSKRNALLKWCQKKTEGYAN-IDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQ--EKKRNLLLA 993
Cdd:COG5069 112 RLTIATINEEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 987976900 994 FEAAE-SVGIKPSLELSEMLHTDRPDWQSVMQYVAQIYKYFET 1035
Cdd:COG5069 192 FENANkVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
932-1031 |
2.00e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 75.84 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 932 RNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPY---QELSSQEKKRNLLLAFEAAESVGIKPS--L 1006
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 987976900 1007 ELSEMLhtDRPDWQSVMQYVAQIYK 1031
Cdd:cd00014 81 EPEDLY--EKGNLKKVLGTLWALAL 103
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
930-1028 |
6.83e-16 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 74.20 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYAnidITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1007
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|.
gi 987976900 1008 LSEMLHTDrPDWQSVMQYVAQ 1028
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLSY 97
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
930-1033 |
1.37e-15 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 73.72 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAESVGIKPSLELS 1009
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLEP 84
|
90 100
....*....|....*....|....
gi 987976900 1010 EMLHTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21244 85 EDVDVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
934-1033 |
2.80e-15 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 72.52 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 934 ALLKWCQKKTEGYAnIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAA-ESVGIKPSLElSEML 1012
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 987976900 1013 HTDRPDWQSVMQYVAQIYKYF 1033
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-666 |
3.88e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 296 STTGSSPNNASELS----LASLTEKIQKMEENhhstAEELQATLQELSDQQQmvqELTAENEKLVDEKTILETSFHQHRE 371
Cdd:TIGR02168 661 ITGGSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 372 RAEQLSHENEKLINLLQErvkkeepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcslrKAEEENQGAAEMIQR 451
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQ---------LSKELTELEAEIEELEERLEEAEEELAEAEAEIE----ELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 452 LKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLE-NEKQKAIVTSSMGQTAEGC-EIQEMLKVARA 529
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEeLSEDIESLAAEIEELEELIeELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 530 EKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 609
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALE 960
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976900 610 DQVE-----QHRAVKLHNNQL----------ITELESSVMK---LEGQKADLERQLKTLTKQIKEETEEWR-RFQA 666
Cdd:TIGR02168 961 NKIEddeeeARRRLKRLENKIkelgpvnlaaIEEYEELKERydfLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
928-1034 |
1.10e-13 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 68.15 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 928 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSL 1006
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90 100
....*....|....*....|....*...
gi 987976900 1007 ELSEMLHTDRPdwQSVMQYVAQIYKYFE 1034
Cdd:cd21196 81 SAQAVVAGSDP--LGLIAYLSHFHSAFK 106
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
933-1028 |
1.22e-13 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 67.71 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 933 NALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTyLPAHIP-YQELSSQEKKRNLLLAFEAAESVGIKPSLELSEM 1011
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 987976900 1012 lhTDrPDWQS--VMQYVAQ 1028
Cdd:cd21185 80 --AD-PEVEHlgIMAYAAQ 95
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
935-1031 |
2.21e-13 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 67.26 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 935 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKK-RNLLLAFEAAE-SVGIKPSLElSEML 1012
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 987976900 1013 HTDRPDWQSVMQYVAQIYK 1031
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
930-1030 |
2.95e-12 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 63.89 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAE-SVGIKPSLEl 1008
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 987976900 1009 SEMLHTDRPDWQSVMQYVAQIY 1030
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
933-1027 |
4.58e-12 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 64.63 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 933 NALLKWCQKKTEGYaNIDITNFSSSWSDGLAFCALLHTYLPAHIP----------------------------------- 977
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 987976900 978 -YQELSSQEkKRNLLLAFEAAESVG-IKPSLELSEMLHTdRPDWQSVMQYVA 1027
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELGgVPALLRASDMSNT-IPDEKVVILFLS 131
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
935-1031 |
4.32e-11 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 60.74 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 935 LLKWCQKKTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQEKKRNLLLAFEAAES-VGIKPSLElSEMLH 1013
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 987976900 1014 TDRPDWQSVMQYVAQIYK 1031
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
316-705 |
4.67e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 316 KIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSHENEKlinlLQERVKKEE 395
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 396 PGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRKAEEENQGA---AEMIQRLKEENEKLNGLLELERQNSGV 472
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIK-ELKKAIEELKKAkgkCPVCGRELTEEHRKELLEEYTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 473 mAQTLEECTVTLEGLKIENGSLKAYLENEKQkaivTSSMGQTAEGC-EIQEMLKVARAEKdqLELSCTE---LKQELLKA 548
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLkELEEKLKKYNLEE--LEKKAEEyekLKEKLIKL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 549 HGEIKHVSSLLAKV---EKDYSYLKEICDHQAEQLSRTSLKLQEKASESdaeIKDMKETIFELE----------DQVEQH 615
Cdd:PRK03918 538 KGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFES---VEELEERLKELEpfyneylelkDAEKEL 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 616 RAVKLHNNQLITELESSVMKLEGQKADLERQLKTLT-----------KQIKEETEEWRRFQADLQTAVVVANDIKCEAQQ 684
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseeeyEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
410 420
....*....|....*....|.
gi 987976900 685 ELRTVKRRLLEEEEKNARLQK 705
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
400-707 |
7.95e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 400 EGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEE 479
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 480 CTVTLEGLKIENGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLL 559
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEE----------------LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 560 AKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQ 639
Cdd:TIGR02168 827 ESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976900 640 KADLERQLKTLTKQIKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKEL 707
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEYSLTLEEAEAL 959
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-722 |
6.12e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 329 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSHENEKLINLLQERVKKEEpgtQEGKVLELEQ 408
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYQALLKEKRE---YEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 409 KCTEI-LEQGRCEREkllSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLElERQNSgvMAQTLEECTVTLEGL 487
Cdd:TIGR02169 233 EALERqKEAIERQLA---SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE-EEQLR--VKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 488 KienGSLKAYLENEKQkaivtssmgqtaegceIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS 567
Cdd:TIGR02169 307 E---RSIAEKERELED----------------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 568 YLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQL 647
Cdd:TIGR02169 368 DLRA----ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 987976900 648 KTLTKQIKEETEEWRRFQADLQTAVVVANDIKceaqQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 722
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLK----EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
421-729 |
7.85e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 7.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 421 REKLLSIQQQLTCSLR----KAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQT---LEECTVTLEGLKIENGS 493
Cdd:TIGR02168 199 ERQLKSLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELEELtaeLQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 494 LkayleNEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIC 573
Cdd:TIGR02168 279 L-----EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 574 DHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTL 650
Cdd:TIGR02168 354 ESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 651 TKQ--------IKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 722
Cdd:TIGR02168 434 ELKelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
....*..
gi 987976900 723 PEADAPG 729
Cdd:TIGR02168 514 NQSGLSG 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
310-707 |
9.49e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.06 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKmeeNHHSTAEELQATLQELSD-QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENE------K 382
Cdd:TIGR00618 181 LALMEFAKKK---SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqeeqlK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 383 LINLLQERVKKEEPGTQEGKVLELEQKCTEIleqgRCEREKLLSIQQQLTcslrkaeEENQGAAEMIQRLKEENEKLNGL 462
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERINR----ARKAAPLAAHIKAVT-------QIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 463 LElERQNSGVMAQTLEECTVTLEGLKIENGSLKayLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTE-- 540
Cdd:TIGR00618 327 LM-KRAAHVKQQSSIEEQRRLLQTLHSQEIHIR--DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEld 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 541 ------------------LKQELLKAHGEIKhvssllakVEKDYSYLKEI---CDHQAEQLSRTSL-KLQEKASESDAEI 598
Cdd:TIGR00618 404 ilqreqatidtrtsafrdLQGQLAHAKKQQE--------LQQRYAELCAAaitCTAQCEKLEKIHLqESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 599 KDmKETIFELED---QVEQHRAVKLHNNQ-------------------------LITELESSVMKLEGQKADLERQLKTL 650
Cdd:TIGR00618 476 QT-KEQIHLQETrkkAVVLARLLELQEEPcplcgscihpnparqdidnpgpltrRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 987976900 651 TKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEEEEKNARLQKEL 707
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
304-711 |
2.95e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEENHH---STAEELQATLQELSDQQQMVQELTAENEKLVD-------EKTILETSFHQHRERA 373
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLREtiaeterEREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 374 EQLSHENEKL-------------INLLQERVKKEEPGTQEgKVLELEQKCTEILEQGRCEREKLLSIQQQ---------- 430
Cdd:PRK02224 289 EELEEERDDLlaeaglddadaeaVEARREELEDRDEELRD-RLEECRVAAQAHNEEAESLREDADDLEERaeelreeaae 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 431 LTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEK-------- 502
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaea 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 503 -QKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSlLAKVEKDYSYLKE-------ICD 574
Cdd:PRK02224 448 lLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEErredleeLIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 575 HQAEQLSRTSLKLQEK---ASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEgqkaDLERQLKTLT 651
Cdd:PRK02224 527 ERRETIEEKRERAEELrerAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE----RIRTLLAAIA 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 652 kQIKEETEEWRRFQADLQTavvvANDIKCEAQQELRTvKRRLLEEEEKNARLQKELGDMQ 711
Cdd:PRK02224 603 -DAEDEIERLREKREALAE----LNDERRERLAEKRE-RKRELEAEFDEARIEEAREDKE 656
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
930-1028 |
3.89e-09 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 55.08 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTEGyanIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1007
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|.
gi 987976900 1008 LSEMLHTDrPDWQSVMQYVAQ 1028
Cdd:cd21230 78 PEEIINPN-VDEMSVMTYLSQ 97
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
306-713 |
4.84e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 60.57 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 306 SELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL-- 383
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 384 -INLLQERVKKEEPGTQ---------EGKVLELEQKCTEILEQ-GRCEREKLLSIQQQLTCSLRKAEEENQgaAEMIQRL 452
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQklqlekvttEAKIKKLEEDILLLEDQnSKLSKERKLLEERISEFTSNLAEEEEK--AKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 453 KEENEKLNGLLELERQNSGVMAQTLEECTVTLEG-----------LKIENGSLKAYL---ENEKQKAIVTSSMGQTAEG- 517
Cdd:pfam01576 182 KNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGestdlqeqiaeLQAQIAELRAQLakkEEELQAALARLEEETAQKNn 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 518 ------------CEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKH-VSSLLAKVEkdysyLKEICDHQAEQLSRTs 584
Cdd:pfam01576 262 alkkireleaqiSELQEDLESERAARNKAEKQRRDLGEELEALKTELEDtLDTTAAQQE-----LRSKREQEVTELKKA- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 585 lkLQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliTELESSVMKLEGQKADLERQLKTLTkQIKEETEE 660
Cdd:pfam01576 336 --LEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQDSEH 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 987976900 661 WRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRRLLEEEEKNARLQKELGDMQGH 713
Cdd:pfam01576 406 KRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-578 |
6.83e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETS---FHQHRERAEQLSHEN 380
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQleeLESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 381 EKLINLLQERVK--KEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRK----AEEENQGAAEMIQRLKE 454
Cdd:TIGR02168 343 EEKLEELKEELEslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA-SLNNeierLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 455 ENEKLNGLLELERqnsgvmaqtLEECTVTLEGLKIENGSLKAYLEnekqkaivtssmgqtaegcEIQEMLKVARAEKDQL 534
Cdd:TIGR02168 422 EIEELLKKLEEAE---------LKELQAELEELEEELEELQEELE-------------------RLEEALEELREELEEA 473
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 987976900 535 ELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAE 578
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
304-660 |
9.74e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEEnhhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSHENEK 382
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 383 LINLLQERVKKEEpgTQEGKVLELEQKCTEIleqgrceREKLLSIQQQltcslrKAEEENQGAAEMIQRLKEENEKLNGL 462
Cdd:TIGR04523 265 IKKQLSEKQKELE--QNNKKIKELEKQLNQL-------KSEISDLNNQ------KEQDWNKELKSELKNQEKKLEEIQNQ 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 463 LELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLEnEKQKAIVTssmgqtaEGCEIQEMLKvaraEKDQLELSCTELK 542
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-EKQNEIEK-------LKKENQSYKQ----EIKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 543 QELLKAHGEIKHVSSLLAKVEKDYsylkeicdhqaEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 622
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEK-----------ELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350
....*....|....*....|....*....|....*...
gi 987976900 623 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEE 660
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-567 |
1.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL 383
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 384 INLLQERVKKEEpgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLtcsLRKAEEENQGAAEMIQRLKEENEKLNGLL 463
Cdd:COG1196 329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 464 ELERQNSGvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAivTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQ 543
Cdd:COG1196 404 ELEEAEEA-LLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260
....*....|....*....|....
gi 987976900 544 ELLKAHGEIKHVSSLLAKVEKDYS 567
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
329-678 |
1.88e-08 |
|
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: 58.49 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 329 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSHENEKLINLLQER-VKKEEPGTQEGKVLELE 407
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENqSYKQEIKNLESQINDLE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 408 QKCTEILEQgrcerekllsiQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL-ELERQNSGV------MAQTLEEC 480
Cdd:TIGR04523 398 SKIQNQEKL-----------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkDLTNQDSVKeliiknLDNTRESL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 481 TVTLEGLKIENGSLKAYLENEKQ--KAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSL 558
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 559 LAKV--EKDYSYLKEICDHQAEQLSR-----TSLK-----LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 626
Cdd:TIGR04523 547 LNKDdfELKKENLEKEIDEKNKEIEElkqtqKSLKkkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 987976900 627 TELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 678
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
310-564 |
2.26e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEENHHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEK 382
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 383 LINLLQERVKK-----EEPGTQEGKVLELEQKCTEILEQGrcerEKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENE 457
Cdd:TIGR02168 321 LEAQLEELESKldelaEELAELEEKLEELKEELESLEAEL----EELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 458 KLNGllELERqnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELS 537
Cdd:TIGR02168 397 SLNN--EIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260
....*....|....*....|....*..
gi 987976900 538 CTELKQELLKAHGEIKHVSSLLAKVEK 564
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLER 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
519-722 |
2.46e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLELSCtELKQELLKAHGEIKHVSSLLAKV-----EKDYSYLKEICDHQAEQLSRtslkLQEKASE 593
Cdd:COG4913 239 RAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR----LEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 594 SDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAV 672
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 987976900 673 VVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESE 722
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-706 |
2.95e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 309 SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLShenEKLINLLQ 388
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE---EDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 389 ERV-KKEEPGTQEGKVLELEQKCTEI-LEQGRCEREKLLSIQQQLTCSLRKAEEENQgaaEMIQRLKEENEKLNGLLEle 466
Cdd:TIGR02169 752 EIEnVKSELKELEARIEELEEDLHKLeEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTL-- 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 467 rqnsgvmaqtleectvtleglkiengsLKAYLENEKQKAIvtssmgqtAEGCEIQEMLKVARAEKDQLELSCTELKQELL 546
Cdd:TIGR02169 827 ---------------------------EKEYLEKEIQELQ--------EQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 547 KAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLI 626
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERD------------------ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 627 TELESSVMKLEGQKADlERQLKTLTKQIKEETEEWRRFQadlqtavvvanDIKCEAQQELRTVKRRLLEEEEKNARLQKE 706
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYEEVLKRLDELKEKRAKLEEE 1001
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
447-726 |
3.87e-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: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 447 EMIQRLKEENEKLNGLL-----ELERQNSGVMA--QTLEECTVTLEGLKIENGSLKAYLENEKQK-AIVTSSMGQTAEGC 518
Cdd:TIGR02169 674 AELQRLRERLEGLKRELsslqsELRRIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERlEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 E-IQEMLKVARAEKDQLELSCTELKQELLK-----AHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslKLQEKAS 592
Cdd:TIGR02169 754 EnVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR---LTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 593 ESDaEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAV 672
Cdd:TIGR02169 831 LEK-EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 987976900 673 VVANdiKCEAQQELRTVKRRLLEEEEknarlqKELGDMQGHGRPVRAESEPEAD 726
Cdd:TIGR02169 910 AQIE--KKRKRLSELKAKLEALEEEL------SEIEDPKGEDEEIPEEELSLED 955
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
310-704 |
3.96e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEENHHSTAEELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLL 387
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 388 QERVKKEEPGTQEGKVLELEQKctEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELER 467
Cdd:COG4717 170 AELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 468 QNSGVMAQTLeecTVTLEGLKIENGSLK----------------AYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAE- 530
Cdd:COG4717 248 ARLLLLIAAA---LLALLGLGGSLLSLIltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEl 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 531 KDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYS--YLKEICDHQAEQLSR---TSLKLQEKASESDAEIKDMKETI 605
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 606 FELEDQVEQHRAVKLHNNQLITELEssvmkLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVvvANDIKCEAQQE 685
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQLE--EDGELAELLQE 477
|
410
....*....|....*....
gi 987976900 686 LRTVKRRLLEEEEKNARLQ 704
Cdd:COG4717 478 LEELKAELRELAEEWAALK 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
519-707 |
4.08e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRtslkLQEKASESDAEI 598
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 599 KDMKETIFELEDQVEQHRAVKLhnnQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 678
Cdd:COG1196 326 AELEEELEELEEELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180
....*....|....*....|....*....
gi 987976900 679 KcEAQQELRTVKRRLLEEEEKNARLQKEL 707
Cdd:COG1196 403 E-ELEEAEEALLERLERLEEELEELEEAL 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
307-708 |
1.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 307 ELSLASLTEKIQKMEENHHSTAEELQAT---LQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLshenEKL 383
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL----KKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 384 INLLQERVKKEEpgtqegkvlELEQKCTEILEQGRcEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLL 463
Cdd:PRK03918 275 IEELEEKVKELK---------ELKEKAEEYIKLSE-FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 464 ELERQNSGVMAQtLEECTVTLEGLKiengSLKAYLENEKQKAivtssMGQTAEgcEIQEMLKVARAEKDQLELSCTELKQ 543
Cdd:PRK03918 345 KKLKELEKRLEE-LEERHELYEEAK----AKKEELERLKKRL-----TGLTPE--KLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 544 ELLKAHGEIKHVSSLLAKVEKdysyLKEIC---------DHQAEQLSRTSLKL---QEKASESDAEIKDMKETIFELEDQ 611
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK----AKGKCpvcgrelteEHRKELLEEYTAELkriEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 612 VEQHRAVkLHNNQLITELESSVMKLEgqKADLErQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKR 691
Cdd:PRK03918 489 LKKESEL-IKLKELAEQLKELEEKLK--KYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEK 563
|
410
....*....|....*..
gi 987976900 692 RLLEEEEKNARLQKELG 708
Cdd:PRK03918 564 KLDELEEELAELLKELE 580
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
304-696 |
1.27e-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: 55.89 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAEneklvdektiletsfHQHRERA-EQLSHENEK 382
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS---------------LQEKERAiEATNAEITK 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 383 LINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGL 462
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 463 LELERQNSGVMAQTLEECTVTLEGlKIENgslkayLENEKQKAIVTSSmgqtaegceiqEMLkvaRAEKDqlelscteLK 542
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEA-RVSD------LELEKVKLVNAGS-----------ERL---RAVKD--------IK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 543 QELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 622
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 987976900 623 NQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEE 696
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-643 |
2.28e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTaENEKLVDEKTILEtsFHQHRERAEQLSHENEKLINLLQE 389
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-EEEQLRVKEKIGE--LEAEIASLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 390 RVKK--EEPGTQEGKVLELEQKcteiLEQGRCEREKLLSI----QQQLTCSLRKAEEENQGAAEMIQRLKEENEKLngll 463
Cdd:TIGR02169 323 RLAKleAEIDKLLAEIEELERE----IEEERKRRDKLTEEyaelKEELEDLRAELEEVDKEFAETRDELKDYREKL---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 464 elerqnsgvmaqtleectvtlEGLKIENGSLKA---YLENEKQKAivtssmgqTAEGCEIQEMLKVARAEKDQLELSCTE 540
Cdd:TIGR02169 395 ---------------------EKLKREINELKReldRLQEELQRL--------SEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 541 LKQELLKAHGEIKHVSSLLAKVEKDYSylkeicdhqaeqlsrtslKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKL 620
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELY------------------DLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340
....*....|....*....|...
gi 987976900 621 HNNQLITELESSVMKLEGQKADL 643
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVAQL 530
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
366-727 |
4.44e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 366 FHQHRERAEQLSHEneklINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTcSLRKAEEENQGA 445
Cdd:COG1196 215 YRELKEELKELEAE----LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 446 -AEMIQRLKEENEKLNGLLELERQNSgvmaqtleectVTLEGLKIENGSLKAYLENEKQKAIvtssmgqtaegcEIQEML 524
Cdd:COG1196 290 eYELLAELARLEQDIARLEERRRELE-----------ERLEELEEELAELEEELEELEEELE------------ELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 525 KVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKET 604
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----AAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 605 IFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIK-CEAQ 683
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLeAEAD 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 987976900 684 QELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAESEPEADA 727
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
299-704 |
1.65e-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: 52.28 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 299 GSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSH 378
Cdd:pfam02463 129 GISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 379 ENEKLINLLQERVKKEEPgTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEK 458
Cdd:pfam02463 209 ALEYYQLKEKLELEEEYL-LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 459 LNGLLELERQNSGVMAQtLEECTVT----LEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQL 534
Cdd:pfam02463 288 LKLLAKEEEELKSELLK-LERRKVDdeekLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 535 ELScTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQ 614
Cdd:pfam02463 367 KLE-QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 615 HRAVKLH-NNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQElRTVKRRL 693
Cdd:pfam02463 446 LTEEKEElEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK-DGVGGRI 524
|
410
....*....|.
gi 987976900 694 LEEEEKNARLQ 704
Cdd:pfam02463 525 ISAHGRLGDLG 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-732 |
2.68e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEI 598
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 599 KDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVANDI 678
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE----RAALEALKAERQKL 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 987976900 679 KCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGH--GRPVRAESEPEADAPGRWP 732
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEaaAAAERTPAAGFAALKGKLP 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
519-814 |
2.74e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEK-ASESDAE 597
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSgGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 598 IKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVVVAND 677
Cdd:COG3883 107 VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 678 IKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGhGRPVRAESEPEADAPGRWPGIFASRASAAPLEPATTVKSLIKSF 757
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA-AAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGS 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 987976900 758 DLGHPGGAGQNVSVHKPPRSPLSGIPVRTAPAAAVSPMQRHSTYSGVRPASKGVAQR 814
Cdd:COG3883 262 AGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGG 318
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
935-1007 |
3.11e-06 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 46.91 E-value: 3.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 987976900 935 LLKWCQK--KTEGYANIDITNFSSSWSDGLAFCALLHTYLPAHIP----YQELSSQEKKRNLLLAFEAAESVGIKPSLE 1007
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLT 93
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
315-722 |
6.25e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 315 EKIQKMEENHHSTAEELQATLQELSDQQQMVQEltAENEKLVDE--KTILETSFHQHRERAEQLSHENEKLINLLQERVK 392
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--AEEKKKADEakKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 393 KEE---PGTQEGKVLELEQKCTEilEQGRCEREKLLSIQQQLTCSLRKAEEENQgAAEMiqRLKEENEKLNGLLELERQN 469
Cdd:PTZ00121 1472 ADEakkKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKKAEEAKK-ADEA--KKAEEAKKADEAKKAEEKK 1546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 470 SGVMAQTLEECTVTLEGLKIENgslKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKVARAEKdqlelsctELKQELLKAH 549
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEE---AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK--------KMKAEEAKKA 1615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 550 GEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSlklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHnnqlitEL 629
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------ED 1686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 630 ESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNaRLQKELGD 709
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK-KIAHLKKE 1765
|
410
....*....|...
gi 987976900 710 MQGHGRPVRAESE 722
Cdd:PTZ00121 1766 EEKKAEEIRKEKE 1778
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
930-1031 |
8.94e-06 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 45.85 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIKPSLE 1007
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCPdWESWDPQKPVDNAREAMQQADDwLGVPQVIT 84
|
90 100
....*....|....*....|....
gi 987976900 1008 LSEMLHTDrPDWQSVMQYVAQIYK 1031
Cdd:cd21313 85 PEEIIHPD-VDEHSVMTYLSQFPK 107
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
291-706 |
3.66e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 291 KSSKCSTTGSSPNNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELT-----------------AENE 353
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeveleelkkilAEDE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 354 KLVDEKTiletsfhQHRERAEQLSHENEKLINLLQERVKK-EEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLT 432
Cdd:pfam05483 419 KLLDEKK-------QFEKIAEELKGKEQELIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 433 CSLRKAEEEN----QGAAEMIQRLKEENEKLNGLLELERQnsgvMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVT 508
Cdd:pfam05483 492 AHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 509 SSMGQTAEGCEIQEMLKVARAEKdQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSY------LKEICDHQAE-QLS 581
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMK-ILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAenkqlnAYEIKVNKLElELA 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 582 RTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKEETEE 660
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSE 726
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 987976900 661 WRRFQADLQTAVVVANDIKCE---AQQELRTVKRRLLEEEEKNARLQKE 706
Cdd:pfam05483 727 LGLYKNKEQEQSSAKAALEIElsnIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
285-676 |
3.69e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 285 STSNPFKSSKCSTTGSSPNNASE--LSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTIL 362
Cdd:COG5185 190 KGISELKKAEPSGTVNSIKESETgnLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 363 ETS-FHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCERE---KLLSIQQQLTCSLRKA 438
Cdd:COG5185 266 RLEkLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEleeSKRETETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 439 EEENQGAAEMIQRLKEENEKLNGLLELERQnsgvmAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmgqtaegc 518
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSKS-----SEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT---------- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 eIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYsylkeicdhQAEQLSRTSLKLQEKASESDAEI 598
Cdd:COG5185 411 -LEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREA---------DEESQSRLEEAYDEINRSVRSKK 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976900 599 KDMKETIFELEDQVEQHRAvklhnnqlitelessvmKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVAN 676
Cdd:COG5185 481 EDLNEELTQIESRVSTLKA-----------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
310-694 |
4.52e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLvdEKTILETSfHQHRERAEQLshenEKLINLLQE 389
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL--RKSLLANR-FSFGPALDEL----EKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 390 RVKKEEPGTQEGKVLEleqkcteileqgrcerekllsiqqqltcslrkaeeenqgAAEMIQRLKEENEKLNGLLElerqn 469
Cdd:PRK04778 180 EFSQFVELTESGDYVE---------------------------------------AREILDQLEEELAALEQIME----- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 470 sgVMAQTLEECTVTLEGL--KIENGslkaYLENEKQKAIVTSsmgQTAEGcEIQEML-KVARAEKDQLELSCTELKQELL 546
Cdd:PRK04778 216 --EIPELLKELQTELPDQlqELKAG----YRELVEEGYHLDH---LDIEK-EIQDLKeQIDENLALLEELDLDEAEEKNE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 547 KAHGEIKHVSSLLakvEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQL 625
Cdd:PRK04778 286 EIQERIDQLYDIL---EREVKARKYV-EKNSDTLPDFLEHAKEQNKELKEEIDRVKQS-YTLnESELESVRQLEKQLESL 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 987976900 626 ITELESSVMKLEGQKA-------DLERQLKTLTkQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 694
Cdd:PRK04778 361 EKQYDEITERIAEQEIayselqeELEEILKQLE-EIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLE 435
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
304-711 |
5.66e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 304 NASELSLASLTEKIQKMEEN-HHSTAEELQATLQELS------------DQQQMVQELTAENEKLVDEKTILETSFHQHR 370
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNkNHINNELESKEEQLSSyedklfdvcgsqDEESDLERLKEEIEKSSKQRAMLAGATAVYS 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 371 ERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLE-------LEQKCTE-ILEQGRCEREKLL-------SIQQQLTCSL 435
Cdd:TIGR00606 667 QFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQsklrlapDKLKSTEsELKKKEKRRDEMLglapgrqSIIDLKEKEI 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 436 RKAEEENQGAAEMIQRLKeeneklNGLLELERQNSGVMAQtLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMGQTA 515
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLK------NDIEEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSD 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 516 EGCEIQEMLKVARAEKDQLE--LSCTELKQELLKAHGE-IKHVSSLLAKVEKDYSYLKEICdHQAEQLSRTSLKLQEKAS 592
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDtvVSKIELNRKLIQDQQEqIQHLKSKTNELKSEKLQIGTNL-QRRQQFEEQLVELSTEVQ 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 593 ESDAEIKDMKETIFELE-----DQVEQHRAV-KLHNNQLITELESSVMK--------------------LEGQKADLERQ 646
Cdd:TIGR00606 899 SLIREIKDAKEQDSPLEtflekDQQEKEELIsSKETSNKKAQDKVNDIKekvknihgymkdienkiqdgKDDYLKQKETE 978
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 987976900 647 LKTLTKQIKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRRLLEEEEKNARLQKELGDMQ 711
Cdd:TIGR00606 979 LNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
928-1028 |
5.95e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 43.62 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 928 GGSKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAESVGIKPSL 1006
Cdd:cd21315 14 GPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDWLDVPQL 90
|
90 100
....*....|....*....|..
gi 987976900 1007 ELSEMLHTDRPDWQSVMQYVAQ 1028
Cdd:cd21315 91 IKPEEMVNPKVDELSMMTYLSQ 112
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
315-707 |
6.42e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 315 EKIQKMEENHHSTAEELQATLQE----LSDQQQMVQELTAENEKLvdeKTILETSFHQHRERAEQlSHENEKLINLLQER 390
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKV---SLKLEEEIQENKDLIKE-NNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 391 VKKEEPGTQEgkvLELEQKCT-EILEQGRCEREKLLSIQQQLtcslrKAEEENqGAAEMIQRLKEENEKLNGLLE----- 464
Cdd:pfam05483 164 CARSAEKTKK---YEYEREETrQVYMDLNNNIEKMILAFEEL-----RVQAEN-ARLEMHFKLKEDHEKIQHLEEeykke 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 465 ---LERQNSGVMAQTLEEctvtleglkiengslkaylENEKQkaivtssmgqtaegcEIQEMLKVARAEKDQLELScTEL 541
Cdd:pfam05483 235 indKEKQVSLLLIQITEK-------------------ENKMK---------------DLTFLLEESRDKANQLEEK-TKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 542 KQELLKAHGEIKHvssllakvekdysylkeicdHQAEQLSRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQ 614
Cdd:pfam05483 280 QDENLKELIEKKD--------------------HLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 615 HRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KR 691
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDE 418
|
410
....*....|....*.
gi 987976900 692 RLLEEEEKNARLQKEL 707
Cdd:pfam05483 419 KLLDEKKQFEKIAEEL 434
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
436-707 |
1.10e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 436 RKAEEENQGAAEMIQRLKEENEklnglleLERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEKQ-KAIVTSSMGQT 514
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNE-------LHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 515 AEGCEIQEMLKvaraeKDQLELSCTELKQ---ELLKAHGEIKHVSSLLAKVEKDYSylKEIcdHQAEQLSRTSLK----- 586
Cdd:pfam15921 151 VHELEAAKCLK-----EDMLEDSNTQIEQlrkMMLSHEGVLQEIRSILVDFEEASG--KKI--YEHDSMSTMHFRslgsa 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 587 LQEKASESDAEIKDMKETIFELEDQVEQHRA---------VKLHNN---QLITELESSVMKL-------EGQKADLERQL 647
Cdd:pfam15921 222 ISKILRELDTEISYLKGRIFPVEDQLEALKSesqnkiellLQQHQDrieQLISEHEVEITGLtekassaRSQANSIQSQL 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 648 KTLTKQIKEETEEWRRFQADLQTAVvvandikCEAQQELRTVKRRLleeEEKNARLQKEL 707
Cdd:pfam15921 302 EIIQEQARNQNSMYMRQLSDLESTV-------SQLRSELREAKRMY---EDKIEELEKQL 351
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
303-611 |
1.89e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 303 NNASELSLASLTEKIQKMEE--NHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHEN 380
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEeeKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 381 EKLINLLQERVKKEepgtQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKL- 459
Cdd:pfam02463 812 EEAELLEEEQLLIE----QEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDe 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 460 NGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEKQKaivtssmgqtaEGCEIQEMLKVARAEKDQLELSCT 539
Cdd:pfam02463 888 LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK-----------YEEEPEELLLEEADEKEKEENNKE 956
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 987976900 540 ELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQ 611
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
930-1031 |
2.87e-04 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 41.59 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 930 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAES-VGIkPSLE 1007
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWESWDPNQPVQNAREAMQQADDwLGV-PQVI 86
|
90 100
....*....|....*....|....
gi 987976900 1008 LSEMLHTDRPDWQSVMQYVAQIYK 1031
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPK 110
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
951-1013 |
4.24e-04 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 39.98 E-value: 4.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976900 951 ITNFSSSWSDGLAFCALLHTYLP-----AHIPYQELSSQEKKR-NLLLAFEAA-ESVGIKPS-LELSEMLH 1013
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPqlidlEDICLKESMSLADSLyNIQLLQEFCqRHLGNRCChLTLEDLLY 83
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
313-708 |
4.40e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 313 LTEKIQKMEENHHSTaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVK 392
Cdd:pfam12128 463 LLQLENFDERIERAR-EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 393 KEEPGTQE--GKVLELEQKC-TEI-------------------LEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQ 450
Cdd:pfam12128 542 KEAPDWEQsiGKVISPELLHrTDLdpevwdgsvggelnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 451 RLKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLK----AYLENEKQKA---IVTSSMGQTAEGCEIQEM 523
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKdkknKALAERKDSAnerLNSLEAQLKQLDKKHQAW 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 524 LKvarAEKDQLELSCTELKQELLKAHGEIK-HVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKL---QEKASESDAEIK 599
Cdd:pfam12128 702 LE---EQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIR 778
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 600 DMKETIfeleDQVEQHRAVKLHNNQLITELESSVM-KLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 678
Cdd:pfam12128 779 TLERKI----ERIAVRRQEVLRYFDWYQETWLQRRpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
410 420 430
....*....|....*....|....*....|....*
gi 987976900 679 KCEAQQELRTVKRRL-----LEEEEKNARLQKELG 708
Cdd:pfam12128 855 QVRLSENLRGLRCEMsklatLKEDANSEQAQGSIG 889
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
387-667 |
5.00e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 387 LQERVKKEEPGTQEGKVLELEqkcTEILEQGRCEREKLLsiqQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNG-LLEL 465
Cdd:pfam15905 61 LKKKSQKNLKESKDQKELEKE---IRALVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSASVASLEKqLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 466 ERQNSGVMAQTLEECT-VTLEGLKIENGSLKAYLENeKQKAIVTSSMGQTAEGCEIQEMLKVARAEKDQLE--LSCTELK 542
Cdd:pfam15905 135 TRVNELLKAKFSEDGTqKKMSSLSMELMKLRNKLEA-KMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEekLVSTEKE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 543 --------QELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEdqveq 614
Cdd:pfam15905 214 kieeksetEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLE----- 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 987976900 615 hravklhnnqliTELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQAD 667
Cdd:pfam15905 289 ------------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
278-608 |
8.00e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 278 TPSRPLSSTSNPFKS--SKCSTTGSSPnnaSELSLASLTEKIQKMEENHHSTA-------EELQATLQEL----SDQQQM 344
Cdd:PLN03229 429 TPVRELEGEVEKLKEqiLKAKESSSKP---SELALNEMIEKLKKEIDLEYTEAviamglqERLENLREEFskanSQDQLM 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 345 VQELTAENEKLVDEktiletsFHQHRERA---EQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCeR 421
Cdd:PLN03229 506 HPVLMEKIEKLKDE-------FNKRLSRApnyLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEI-K 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 422 EKLLSIqqqltcslrKAEEENQGA---AEMIQRLKEENEKLNGLLELErqnsgvMAQTLEECTVTLEGLKIENGSLKAYL 498
Cdd:PLN03229 578 EKMEAL---------KAEVASSGAssgDELDDDLKEKVEKMKKEIELE------LAGVLKSMGLEVIGVTKKNKDTAEQT 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 499 ENEKQKAIVTSSMGQTAEgcEIQEMLKVAraekdQLELSCTELKQELLKAHGeikhvSSLLAKVEKDYSYLKEICDHQAE 578
Cdd:PLN03229 643 PPPNLQEKIESLNEEINK--KIERVIRSS-----DLKSKIELLKLEVAKASK-----TPDVTEKEKIEALEQQIKQKIAE 710
|
330 340 350
....*....|....*....|....*....|
gi 987976900 579 QLSRTSLKlqEKASESDAEIKDMKETIFEL 608
Cdd:PLN03229 711 ALNSSELK--EKFEELEAELAAARETAAES 738
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
484-726 |
8.35e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 484 LEGLKIENGSLKAYLENEKQKAIVTSSmgqtaegcEIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVE 563
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELD--------KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 564 KDYSYLKEICDHQAEQLSRTSL---KLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQK 640
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEeaeELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 641 ADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQGHGRPVRAE 720
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
....*.
gi 987976900 721 SEPEAD 726
Cdd:COG4372 247 DKEELL 252
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
315-699 |
8.56e-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: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 315 EKIQKMEENHHSTAEELQatlQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQE-RVKK 393
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 394 EEPGTQEGKVLELEQKCTEILEQGRCEREkllsiqqqltcslrkAEEENQGAAEMIQRLKEENEKLNgllELERQNSGvM 473
Cdd:TIGR00606 378 ELDGFERGPFSERQIKNFHTLVIERQEDE---------------AKTAAQLCADLQSKERLKQEQAD---EIRDEKKG-L 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 474 AQTLEECTVTLEglkiengslkaylenekqkaivtssmgqtaegcEIQEMLKVARAEKDQLELSCT---ELKQELLKAHG 550
Cdd:TIGR00606 439 GRTIELKKEILE---------------------------------KKQEELKFVIKELQQLEGSSDrilELDQELRKAER 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 551 EIkhvsSLLAKVEKDYSYLKEICDHQAEQ--LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITE 628
Cdd:TIGR00606 486 EL----SKAEKNSLTETLKKEVKSLQNEKadLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976900 629 LESSVMKLEGQKAdLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKceaqQELRTVKRRLLEEEEK 699
Cdd:TIGR00606 562 LTSLLGYFPNKKQ-LEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN----NELESKEEQLSSYEDK 627
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
302-620 |
9.69e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.13 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 302 PNNASELSLAsLTEKIQKMEENHHSTAEELQATLQE---LS----DQQQMVQEL--TAE--NEKLVDEKTILET------ 364
Cdd:pfam15070 77 PAGPSEEEQR-LQEEAEQLQKELEALAGQLQAQVQDneqLSrlnqEQEQRLLELerAAErwGEQAEDRKQILEDmqsdra 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 365 ----SFHQHRERAEQL----------SHENEKLINLLQ--ERVKKE------EPGTQEGKVLE-LEQKCTEI--LEQGR- 418
Cdd:pfam15070 156 tisrALSQNRELKEQLaelqngfvklTNENMELTSALQseQHVKKElakklgQLQEELGELKEtLELKSQEAqsLQEQRd 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 419 -----------------CEREKL---LSIQQQLTCSLRKAEEENQGAAEM-IQRLKEENEKLNgllELERQNSGVMAQtL 477
Cdd:pfam15070 236 qylahlqqyvaayqqlaSEKEELhkqYLLQTQLMDRLQHEEVQGKVAAEMaRQELQETQERLE---ALTQQNQQLQAQ-L 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 478 EECTVTLEGLKIENGSLkaylENEKQKAIVTSSmgqtaEGCEIQEMLK------VARAEKDQLELS---------CTELK 542
Cdd:pfam15070 312 SLLANPGEGDGLESEEE----EEEAPRPSLSIP-----EDFESREAMVaffnsaLAQAEEERAELRrqlkeqkrrCRRLA 382
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 987976900 543 QELLKAHGEIKHVSSllAKVEKDYSYLKEIcdHQAEQLSRTslKLQEKASESDAEIKDMKETIFELEdqveqHRAVKL 620
Cdd:pfam15070 383 QQAAPAQEEPEHEAH--APGTGGDSVPVEV--HQALQVAME--KLQSRFTELMQEKADLKERVEELE-----HRCIQL 449
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
434-727 |
1.00e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 434 SLRKAEEENQGAAEMIQRLKEENEKLNGLL-ELERQNSGVMAqtlEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMG 512
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELaGLTRRLSAAEG---ELEELVARLAKLEAALREAEAAKEELRIELRDKTA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 513 QtAEGCEIQ-----EMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKL 587
Cdd:pfam19220 119 Q-AEALERQlaaetEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 588 QEKASESDAEIKDMKETIFEL-EDQVEQHRAVKLHNNQLI---TELESSVMKLEGQKADLERQLKTLTK---QIKEETEE 660
Cdd:pfam19220 198 AELETQLDATRARLRALEGQLaAEQAERERAEAQLEEAVEahrAERASLRMKLEALTARAAATEQLLAEarnQLRDRDEA 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 987976900 661 WRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEEKNARLQKELGDMQghgrPVRAESEPEADA 727
Cdd:pfam19220 278 IRAAERRLK-----------EASIERDTLERRLAGLEADLERRTQQFQEMQ----RARAELEERAEM 329
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
310-660 |
1.10e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEEnhhstaeELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqhRERAEQLSHENEKLINLLQE 389
Cdd:TIGR00618 551 LTSERKQRASLKE-------QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDMLACEQHAL 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 390 RVKKEEPGTQEGKVLELEQKcteileQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLELERQN 469
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQC------SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQ 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 470 SGVMAQTLEECtvtLEGLKIENGSLKAYLENEKQKAIVTSSMGQTAEGCE--IQEMLKVARAEKDqlelsctelkqELLK 547
Cdd:TIGR00618 692 LTYWKEMLAQC---QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREdaLNQSLKELMHQAR-----------TVLK 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 548 AHGEIKHVSSLLAKVE----KDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLHNN 623
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFLSR 836
|
330 340 350
....*....|....*....|....*....|....*...
gi 987976900 624 -QLITELESSVMKLEGQKADLERQLKTLTKQIKEETEE 660
Cdd:TIGR00618 837 lEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
540-709 |
1.20e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 540 ELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIcdhqaeqlsRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAvk 619
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQER---------REALQRLAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 620 lhNNQLITELESSVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTV---KRRLLEE 696
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleeRFAAALG 760
|
170
....*....|...
gi 987976900 697 EEKNARLQKELGD 709
Cdd:COG4913 761 DAVERELRENLEE 773
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
411-711 |
1.37e-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: 42.65 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 411 TEILEQGRCEREKLLSIQQQLT-CSLRKAEEENQGAAEMIQRlKEENEKLNGLLELERQNSGVMAQTLEECTVTLEGLKI 489
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAeLIIDLEELKLQELKLKEQA-KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 490 ENGSLKAYLENEKQKAIVTSSMGQTAEGCEIQEMLKV---ARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKdy 566
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK-- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 567 sylkeicdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLITELESSVmKLEGQKADLERQ 646
Cdd:pfam02463 322 ---------EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAK 391
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 987976900 647 LKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQ 711
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
519-656 |
1.42e-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: 41.45 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKV--EKDY-SYLKEIcDHQAEQLSrtslKLQEKASESD 595
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYeALQKEI-ESLKRRIS----DLEDEILELM 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 987976900 596 AEIKDMKETIFELEDQVEQHRAvklhnnqlitELESSVMKLEGQKADLERQLKTLTKQIKE 656
Cdd:COG1579 117 ERIEELEEELAELEAELAELEA----------ELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
303-654 |
1.60e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 303 NNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETS-FHQHRERAEQ---- 375
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLknELSeLRRQIQRAELelqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 376 LSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEEENQGAAEM---IQRL 452
Cdd:pfam05557 130 TNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELekeLERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 453 KEENEKLNGLLElerqnsgvmaqtleectvTLEGLKIENGSLKAYLENEKQkaivtssmgqtaegceiqemlkvARAEKD 532
Cdd:pfam05557 210 REHNKHLNENIE------------------NKLLLKEEVEDLKRKLEREEK-----------------------YREEAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 533 QLELSCTELKQELlKAHGEIKHVSSLLAKVEKDYSylkeicdHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQV 612
Cdd:pfam05557 249 TLELEKEKLEQEL-QSWVKLAQDTGLNLRSPEDLS-------RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQEL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 987976900 613 EQHRAVklhnnqlITELESSVMKLEGQKADLERQLKTLTKQI 654
Cdd:pfam05557 321 AQYLKK-------IEDLNKKLKRHKALVRRLQRRVLLLTKER 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
371-700 |
1.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 371 ERAEQLSHENEKLINLLQERVKKEEPGTQ--EGKVLELEQKCTEILEQGRCEREKLlsiqqqltcslRKAEEENQGAAEM 448
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSEL-----------PELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 449 IQRLKEENEKLNGL---LELERQNSGVMAQTLEECTVTLEGLKIENGSLkaylenEKQKAIVTSSMGQTAEGCEIQEMLK 525
Cdd:PRK03918 230 VKELEELKEEIEELekeLESLEGSKRKLEEKIRELEERIEELKKEIEEL------EEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 526 VARAEKDQLELSCTELKQellkahgEIKHVSSLLAKVEKDYSYLKEIcDHQAEQLSRTSLKLQEKASESdaeikdmkETI 605
Cdd:PRK03918 304 EYLDELREIEKRLSRLEE-------EINGIEERIKELEEKEERLEEL-KKKLKELEKRLEELEERHELY--------EEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 606 FELEDQVEQHRAVKLHNNqlITELESSVMKLEGQKADLERQLKTLTKQIKEETEEwrrfQADLQTAVvvaNDIKcEAQQE 685
Cdd:PRK03918 368 KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKE----IKELKKAI---EELK-KAKGK 437
|
330
....*....|....*
gi 987976900 686 LRTVKRRLLEEEEKN 700
Cdd:PRK03918 438 CPVCGRELTEEHRKE 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
303-659 |
1.87e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 303 NNASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSHENEK 382
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 383 LINLLQERVKkeepgTQEGKVLELEQKCTEILEQGR-------CEREKLLSIQQQLTCSLRKAEEENQGAAEMIQR-LKE 454
Cdd:pfam15921 279 EITGLTEKAS-----SARSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 455 ENEKLNGlLELER----QNSGVMAQTLEECTVTLEGLKIEngslkAYLENEKQKAIVTSSMGQTA-----------EGCE 519
Cdd:pfam15921 354 ANSELTE-ARTERdqfsQESGNLDDQLQKLLADLHKREKE-----LSLEKEQNKRLWDRDTGNSItidhlrrelddRNME 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 520 IQEMLKVARAEKDQLElscTELKQELLKAHGE---IKHVSSLLAKVEKDYSYLKEICDH------QAEQLSRT------S 584
Cdd:pfam15921 428 VQRLEALLKAMKSECQ---GQMERQMAAIQGKnesLEKVSSLTAQLESTKEMLRKVVEEltakkmTLESSERTvsdltaS 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 987976900 585 LKLQEKASE-SDAEIKDMKETIfELEDQVEQH-RAVKLHNNQLITELESsvmkLEGQKADLERQLKTLTKQIKEETE 659
Cdd:pfam15921 505 LQEKERAIEaTNAEITKLRSRV-DLKLQELQHlKNEGDHLRNVQTECEA----LKLQMAEKDKVIEILRQQIENMTQ 576
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
951-1033 |
1.96e-03 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 38.91 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 951 ITNFSSSWSDGLAFCALLHTYLPAHIP-YQELSSQEKKRNLLLAFEAAESV-GIKPSLElSEMLHTDRPDWQSVMQYVAq 1028
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIPMVLS-PEDLSSPHLDELSGMTYLS- 98
|
....*
gi 987976900 1029 iykYF 1033
Cdd:cd21229 99 ---YF 100
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
388-698 |
2.44e-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: 41.96 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 388 QERVKK-EEPGTQEGKVLELEQKCTEILEQGRCE-REKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEKLNGLLEL 465
Cdd:TIGR00606 188 LETLRQvRQTQGQKVQEHQMELKYLKQYKEKACEiRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 466 ERQnsgvmaqtleecTVTLEGLKIENGSLKAYLENEKQKAIvtssMGQTAEGCEIQEMLKVARAEKDQLELSCtelKQEL 545
Cdd:TIGR00606 268 DNE------------IKALKSRKKQMEKDNSELELKMEKVF----QGTDEQLNDLYHNHQRTVREKERELVDC---QREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 546 LKAHGEIKHVSSLLAKVEKDYSYLKEICD-HQAEQLSRTSLKLQ----------EKASESDAEIKDMKETIfeLEDQVEQ 614
Cdd:TIGR00606 329 EKLNKERRLLNQEKTELLVEQGRLQLQADrHQEHIRARDSLIQSlatrleldgfERGPFSERQIKNFHTLV--IERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 615 HRAVklhnNQLITELES-------SVMKLEGQKADLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIkCEAQQELR 687
Cdd:TIGR00606 407 AKTA----AQLCADLQSkerlkqeQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI-LELDQELR 481
|
330
....*....|.
gi 987976900 688 TVKRRLLEEEE 698
Cdd:TIGR00606 482 KAERELSKAEK 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
305-695 |
2.53e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 305 ASELSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKL- 383
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAa 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 384 --INLLQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSL-----RKAEEENQGAAEMIQRLKEEN 456
Cdd:COG1196 491 arLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAAK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 457 EKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYleNEKQKAIVTSSMGQTAEgCEIQEMLKVARAEKDQLEL 536
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTLLGRTLV-AARLEAALRRAVTLAGRLR 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 537 SCTELKQELL----KAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQV 612
Cdd:COG1196 648 EVTLEGEGGSaggsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 613 EQHRAVKLHNNQLITELESSVMKLEGQK-------ADLERQLKTLTKQIK-------------EETEEWRRF----QADL 668
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEalgpvnllaieeyEELEERYDFlseqREDL 807
|
410 420
....*....|....*....|....*...
gi 987976900 669 QTAVvvaNDIKcEAQQEL-RTVKRRLLE 695
Cdd:COG1196 808 EEAR---ETLE-EAIEEIdRETRERFLE 831
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
307-706 |
2.53e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.09 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 307 ELSLASLTEKIQKMEENHHSTA----EELQATLQE---LSDQQQmvQELTAENEKLVDEKTILETSFHQHRERAEQLSHE 379
Cdd:PRK10246 175 ELTGTEIYGQISAMVFEQHKSArtelEKLQAQASGvalLTPEQV--QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 380 NEklinlLQervkkeepgTQEGKVLELEQKCTEILEQGRCEREKLLSIQ--QQLTCSLRKAEEENQGAAEMIQRLKEENE 457
Cdd:PRK10246 253 DE-----LQ---------QEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 458 KLNGLLELERQNSGVMAQTLEECTVTLeglkienGSLKAYLENEKQKAIVTSSMG--------QTAEGCEI---QEMLKV 526
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQ-------QSLNTWLAEHDRFRQWNNELAgwraqfsqQTSDREQLrqwQQQLTH 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 527 ARAEKDQ-----LELSCTE-------------LKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ 588
Cdd:PRK10246 392 AEQKLNAlpaitLTLTADEvaaalaqhaeqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYK 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 589 EKAS---------ESDAEIKDMKETIFELED-------------QVEQHRAVKLHNNQL-ITELESSVMKLEGQKADLER 645
Cdd:PRK10246 472 EKTQqladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrLDALEKEVKKLGEEGAALRG 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 646 QLKTLTKQIKEE--------------TEEWRRFQADLQTAVVVANDI------KCEAQQELRTVKRRLLEEEEKNARLQK 705
Cdd:PRK10246 552 QLDALTKQLQRDeseaqslrqeeqalTQQWQAVCASLNITLQPQDDIqpwldaQEEHERQLRLLSQRHELQGQIAAHNQQ 631
|
.
gi 987976900 706 E 706
Cdd:PRK10246 632 I 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
524-707 |
2.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 524 LKVARAEKDQLELSCTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQ-EKASESDAEIKdmk 602
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAElERLDASSDDLA--- 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 603 etifELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLTKQ---IKEETEEWRRFQADLQtavvVANDIK 679
Cdd:COG4913 689 ----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaAEDLARLELRALLEER----FAAALG 760
|
170 180
....*....|....*....|....*....
gi 987976900 680 CEAQQELR-TVKRRLLEEEEKNARLQKEL 707
Cdd:COG4913 761 DAVERELReNLEERIDALRARLNRAEEEL 789
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-712 |
2.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 521 QEMLKVARAEKDQLElsctelkqELLKAHGEIKhvsSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLqEKASESDAEIKD 600
Cdd:PRK03918 168 GEVIKEIKRRIERLE--------KFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 601 MKETIFELEDQVEQHRAVKLHNNQLITELESSVMKLEGQKADLERQLKTLtKQIKEETEEWRRFQADLQTAVVVANDIKC 680
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 987976900 681 EA---QQELRTVKRRLLEEEEKNAR----------LQKELGDMQG 712
Cdd:PRK03918 315 RLsrlEEEINGIEERIKELEEKEERleelkkklkeLEKRLEELEE 359
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
309-469 |
3.77e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.12 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 309 SLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERaeqlshenEKLINLLQ 388
Cdd:cd00176 55 RVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDL--------EQWLEEKE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 389 ERVKKEEPGTQEGKVLELEQKCTEI---LEQGRCEREKLLSIQQQLTCSLRKAEEENqgAAEMIQRLKEENEKLNGLLEl 465
Cdd:cd00176 127 AALASEDLGKDLESVEELLKKHKELeeeLEAHEPRLKSLNELAEELLEEGHPDADEE--IEEKLEELNERWEELLELAE- 203
|
....
gi 987976900 466 ERQN 469
Cdd:cd00176 204 ERQK 207
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
444-588 |
3.99e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 444 GAAEM----IQRLKEENEKLNG-LLELERQNSGV------MAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTSSMG 512
Cdd:pfam15294 126 GGSALlhmeIERLKEENEKLKErLKTLESQATQAldekskLEKALKDLQKEQGAKKDVKSNLKEISDLEEKMAALKSDLE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 513 QTaegceiqemLKVARAEKDQLELSCTELKQELLKahgeikhVSSLLAKVEKD----------YSYLKEICDHQAEQLSR 582
Cdd:pfam15294 206 KT---------LNASTALQKSLEEDLASTKHELLK-------VQEQLEMAEKElekkfqqtaaYRNMKEMLTKKNEQIKE 269
|
....*.
gi 987976900 583 TSLKLQ 588
Cdd:pfam15294 270 LRKRLS 275
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
330-713 |
4.05e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 330 ELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENE------KLINLLQERVK--KEEPGTQEG 401
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDsgtpggKKYLLLQKQLEqlQEENFRLET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 402 KVLELEQKCtEILEQgrcereKLLSIQQQltcslrkaEEENQGAAEMIQRLKEENEKLnglleleRQNS---GVMAQTLE 478
Cdd:pfam05622 81 ARDDYRIKC-EELEK------EVLELQHR--------NEELTSLAEEAQALKDEMDIL-------RESSdkvKKLEATVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 479 ECTVTLEGLkienGSLKayleneKQ-KAIVTSSMGQTAEGCEIQEMLKVARAEKDQLELscteLKQELLKAHGEIKHVSS 557
Cdd:pfam05622 139 TYKKKLEDL----GDLR------RQvKLLEERNAEYMQRTLQLEEELKKANALRGQLET----YKRQVQELHGKLSEESK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 558 LLAKVEKDYSYLKEicDHQAEQLSRTSLklqekASESDAeikdMKETIFELE-DQVEQHRAVKLHNNQLITELESSVMKL 636
Cdd:pfam05622 205 KADKLEFEYKKLEE--KLEALQKEKERL-----IIERDT----LRETNEELRcAQLQQAELSQADALLSPSSDPGDNLAA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 637 EGQKADLERQLKTL---TKQIKEETEE-WRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDMQG 712
Cdd:pfam05622 274 EIMPAEIREKLIRLqheNKMLRLGQEGsYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGS 353
|
.
gi 987976900 713 H 713
Cdd:pfam05622 354 K 354
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
311-490 |
4.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 311 ASLTEKIQKMEENHHSTAEELQATLQELSDQQQMVQEltaENEKLVDEKtiLETSFHQHRERAEQLSHENEKLINLLQER 390
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA---EEEKKKVEQ--LKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 391 VKKEEPGTQEG----KVLELEQKCTEILEQGRCEREKLLSIQQQL------TCSLRKAEEENQGAAEMIQRLKEENEKLN 460
Cdd:PTZ00121 1667 AKKAEEDKKKAeeakKAEEDEKKAAEALKKEAEEAKKAEELKKKEaeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
170 180 190
....*....|....*....|....*....|
gi 987976900 461 GLLELERQNSGVMAQTLEECTVTLEGLKIE 490
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
519-706 |
4.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 519 EIQEMLKVARAEKDQLElsctELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEIcdHQAEQLSRTSLKLQEKASESDAEI 598
Cdd:COG4717 75 ELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 599 KDMKETIFELEDQVEQhravklhnnqlITELESSVMKLEGQKADLERQLKTLT-KQIKEETEEWRRFQADLQTAvvvaND 677
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAEL----EE 213
|
170 180
....*....|....*....|....*....
gi 987976900 678 IKCEAQQELRTVKRRLLEEEEKNARLQKE 706
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
173-713 |
5.89e-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: 40.80 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 173 EEKNKNFQKELSDLEEENRALKEKLRYFEHSEAGSSHTADSSCPTSLTQESSFGSptgNQVSGEVDEYKRHAPQNIlptS 252
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSER---Q 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 253 GSSSSDVTKASLSPDASDFEHLTADTPSRPLSSTSNPFK-SSKCSTTGSSPNNASELSLASLTEKIQKMEENHHSTA--- 328
Cdd:TIGR00606 392 IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGssd 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 329 ------EELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKeepgtqe 400
Cdd:TIGR00606 472 rileldQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK------- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 401 gkvLELEQKCTEILEQGRCEREKLLSI---QQQLTCSLRKAEEENQGAAEMIQRLKEENEKL--------NGLLELERQN 469
Cdd:TIGR00606 545 ---MDKDEQIRKIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLeqnknhinNELESKEEQL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 470 SGVMAQTLEECTVTLEGLKIENgsLKAYLEN-EKQKAI-----------VTSSMGQTAEGCEIQEmlKVARAEKDQLELS 537
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLER--LKEEIEKsSKQRAMlagatavysqfITQLTDENQSCCPVCQ--RVFQTEAELQEFI 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 538 cTELKQELLKAHGEIKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQ 614
Cdd:TIGR00606 698 -SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnKLQKVNRDIQRLKNDIEEQETLLGT 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 615 HRAVKLHNNQLITELeSSVMKLEGQKADLERQLKTLTKQIKeeteewrrfQADLQTAVVVANDIKCEAQQELRTV----- 689
Cdd:TIGR00606 777 IMPEEESAKVCLTDV-TIMERFQMELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVvskie 846
|
570 580
....*....|....*....|....*.
gi 987976900 690 -KRRLLEEEEKNAR-LQKELGDMQGH 713
Cdd:TIGR00606 847 lNRKLIQDQQEQIQhLKSKTNELKSE 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
326-505 |
7.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 326 STAEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSHENEKLINLLQERVKK--EEPGTQEGKV 403
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELAEleKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 404 LELEQKCTEIL----EQGRCEREKLLSIQQQLTCSLRKAE------EENQGAAEMIQRLKEENEKLNGLLELERQNSGVM 473
Cdd:COG4942 100 EAQKEELAELLralyRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|..
gi 987976900 474 AQTLEECTVTLEGLKIENGSLKAYLENEKQKA 505
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
105-457 |
7.41e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 7.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 105 EKAVLESQVRELLAEAKAKDSEINRLRSELKKCRekrtlntAGTDTSDPKTDGTSVSAADSEPLIQALEEKNKNFQKELS 184
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLR-------KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 185 DLEEENRALKEKLryfehseagsshtadsscpTSLTQESSFGSPTGNQVSGEVDEYKRHAPQNILptsgssssdvTKASL 264
Cdd:TIGR02168 758 ELEAEIEELEERL-------------------EEAEEELAEAEAEIEELEAQIEQLKEELKALRE----------ALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 265 SPDASDFEHLTADTPSRPLSSTSNpfksskcsttgsspnnaselsLASLTEKIQKMEENHHSTAEELQATLQELSDQQQM 344
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERR---------------------IAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 345 VQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLinllqervkkeepgtqEGKVLELEQKCTEILEQGRCEREKL 424
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELREL----------------ESKRSELRRELEELREKLAQLELRL 931
|
330 340 350
....*....|....*....|....*....|...
gi 987976900 425 LSIQQQLTCSLRKAEEENQGAAEMIQRLKEENE 457
Cdd:TIGR02168 932 EGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
310-685 |
7.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 310 LASLTEKIQKMEENHHSTAEELQATLQELS-DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQ 388
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 389 ERVKKEEPGTQE------GKVLELEQKCTEILEQGRCEREKLLSIQQQLTC---SLRKAEEENQGAAEMIQRLKE----E 455
Cdd:COG4717 238 AAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflLLAREKASLGKEAEELQALPAleelE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 456 NEKLNGLLELERQNSGVMAQTLEECTVTLEGLKIENGSLKAYLENEKQKAIVTssmgqtaegcEIQEMLKVARAEKDQLE 535
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ----------EIAALLAEAGVEDEEEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 536 LSCTELKQELLKAHGEIKHVSSLLAkvEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQh 615
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLE--ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ- 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 616 ravklhnnqlitelessvMKLEGQKADLERQLKTLTKQIKEETEEWRRfqadLQTAVVVANDIKCEAQQE 685
Cdd:COG4717 465 ------------------LEEDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAREEYREE 512
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
313-495 |
8.20e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 313 LTEKIQKMEENHHSTAEELQATLQeLSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVK 392
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 393 KEEP-GTQEGKVLELEQKCTEILEQGRCEREKllSIQQQLTCSL-RKAEEEnqgAAEMIQRLKEENEklnglLELERQNS 470
Cdd:PRK12705 110 REKAlSARELELEELEKQLDNELYRVAGLTPE--QARKLLLKLLdAELEEE---KAQRVKKIEEEAD-----LEAERKAQ 179
|
170 180 190
....*....|....*....|....*....|.
gi 987976900 471 GVMAQTLEECT------VTLEGLKIENGSLK 495
Cdd:PRK12705 180 NILAQAMQRIAsetasdLSVSVVPIPSDAMK 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
109-468 |
9.54e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 109 LESQVRELLAEAKAKDSEINRLRSELKKCREKrtLNTAGTDTSDPKTDgtsvsAADSEPL---IQALEEKNKNFQKELSD 185
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK--LQKVNRDIQRLKND-----IEEQETLlgtIMPEEESAKVCLTDVTI 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 186 LEEENRALKEKLRYFEHSEAGSshtadsscptsltqESSFGSPTGNQVSGEVDEyKRHAPQNIlptsgSSSSDVTKASLS 265
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQAAKL--------------QGSDLDRTVQQVNQEKQE-KQHELDTV-----VSKIELNRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 266 PDASDFEHLtadtpsrplSSTSNPFKSSKcsttgsspnnaseLSLASLTEKIQKMEENHHSTAEELQATLQELSDQQQMV 345
Cdd:TIGR00606 854 DQQEQIQHL---------KSKTNELKSEK-------------LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 346 QELTAENEKLVDEKTILETSFHQHRERAEQLSHENEKLINLLQERVKKEEPGTQEGKVLELEQKCTEI------LEQGRC 419
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELntvnaqLEECEK 991
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 987976900 420 EREKLLSIQQQLTCSLRKAEEENQGAAEMIQRLKEENEklngLLELERQ 468
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE----LKEVEEE 1036
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
523-711 |
9.58e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.88 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 523 MLKVARAEKDQLELS-CTELKQELLKAHgeiKHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKASESDAEIKDM 601
Cdd:pfam07888 23 LLVVPRAELLQNRLEeCLQERAELLQAQ---EAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 602 KETIFELEDQVEQHR-------AVKLHNNQLITELESSVMKLEGQKADLERQL-------KTLTKQIKEETEEWRRFQAD 667
Cdd:pfam07888 100 EEKYKELSASSEELSeekdallAQRAAHEARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 987976900 668 LQTAVVVAndikCEAQQELRTVKRRLLEEEEKNARLQKELGDMQ 711
Cdd:pfam07888 180 LQQTEEEL----RSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
324-706 |
9.70e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 39.89 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 324 HHSTAEeLQATLQELSDQQQMVQELTAENEKL------------VDEKTILETSFHQHRERAEQLS---HENEKLI--NL 386
Cdd:pfam15964 124 HHLEAE-VKFCKEELSEMKQRVQVVVLENEKLqqelksqtqeetLREQTLLDSSGNMQNSWCTPEDsrvHQTSKRPasHN 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 387 LQERVKKEEPGTQEGKVLELEQKCTEILEQGRCEREKLLSIQQQLTCSLRKAEeenqgaaEMIQRLKEE--------NEK 458
Cdd:pfam15964 203 LAERLKSATTGEDEKWRLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCE-------DLKERLKHKeslvaastSSR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 459 LNGLLELERQNSGVMAQTLEECTV-TLEGLKIENGSLKAYLENEKQKAIVTSSMGQTA--EGCEIQEMLKVARAEKDQLE 535
Cdd:pfam15964 276 VGGLCLKCAQHEAVLAQTHTNVHMqTIERLTKERDDLMSALVSVRSSLAEAQQRESSAyeQVKQAVQMTEEANFEKTKAL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 536 LSCTELKQELLKAHGEI-KHVSSLLAKVEKDYSYLKEICDHQAEQLSRTSLKLQEKasesdaeikdmketIFELEDQVEQ 614
Cdd:pfam15964 356 IQCEQLKSELERQKERLeKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQN--------------VAQLEAQVEK 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 987976900 615 hraVKLHNNQLITELESSVMKLEGQKADLE------RQLKTLTKQIKEETE-EWRRFQADLQTAVVVANDIKCEAQQELR 687
Cdd:pfam15964 422 ---VTREKNSLVSQLEEAQKQLASQEMDVTkvcgemRYQLNQTKMKKDEAEkEHREYRTKTGRQLEIKDQEIEKLGLELS 498
|
410
....*....|....*....
gi 987976900 688 TVKRRLLEEEEKNARLQKE 706
Cdd:pfam15964 499 ESKQRLEQAQQDAARAREE 517
|
|
| |
