|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
866-977 |
2.55e-78 |
|
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: 250.33 E-value: 2.55e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 866 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGI 945
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 71979930 946 NPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
866-977 |
2.98e-75 |
|
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: 241.88 E-value: 2.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 866 LAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGI 945
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 71979930 946 NPSLELSEMLYTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
860-978 |
1.75e-66 |
|
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: 218.40 E-value: 1.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 860 RDPLAALAREYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEA 939
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 71979930 940 AQSVGINPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET 978
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
873-976 |
2.01e-33 |
|
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: 124.78 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEL 951
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
875-976 |
2.42e-32 |
|
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: 121.30 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 875 RNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLELSE 953
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAeELADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 71979930 954 MLY-TDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21200 83 MVRmGNRPDWKCVFTYVQSLYRHL 106
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
876-976 |
9.13e-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: 116.62 E-value: 9.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 876 NALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLELSEM 954
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDvAEQELGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 71979930 955 LYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
878-976 |
1.87e-30 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 115.60 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 878 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLELSEMLYT 957
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 71979930 958 DRPDWQSVMQYVAQIYKYF 976
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
873-976 |
9.38e-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: 113.66 E-value: 9.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGInPSLEL 951
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDvAEQELGI-AKLLD 80
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
869-976 |
2.09e-29 |
|
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: 113.01 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 869 EYGGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINP 947
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 71979930 948 SLELSEMLYTDRPDWQSVMQYVAQIYKYF 976
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 ... |
873-976 |
3.16e-28 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 109.41 E-value: 3.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 951
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAeQKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
873-974 |
6.36e-28 |
|
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: 108.92 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPS-LEL 951
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQlLDV 80
|
90 100
....*....|....*....|...
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYK 974
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
873-976 |
1.60e-27 |
|
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: 107.78 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 951
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAeRQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
875-974 |
2.58e-26 |
|
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: 104.40 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 875 RNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLELSE 953
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAeKHADCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 71979930 954 MLYTDRPDWQSVMQYVAQIYK 974
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
873-976 |
2.94e-26 |
|
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: 103.97 E-value: 2.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 951
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 71979930 952 SEMLYT-DRPDWQSVMQYVAQIYKYF 976
Cdd:cd21258 81 EDMMIMgKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
878-976 |
6.14e-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: 103.01 E-value: 6.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 878 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLELSEMLYT 957
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 71979930 958 DRPDWQSVMQYVAQIYKYF 976
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
877-977 |
9.14e-26 |
|
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: 102.43 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 877 ALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLELSEML 955
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 71979930 956 YTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
873-976 |
2.42e-25 |
|
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: 101.48 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 951
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAeQELGISQLLD- 82
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
873-977 |
3.18e-25 |
|
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: 101.02 E-value: 3.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLELS 952
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 71979930 953 EMLYTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
874-976 |
1.88e-24 |
|
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: 98.76 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 874 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLELS 952
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 71979930 953 EMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
873-976 |
2.63e-24 |
|
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: 98.50 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSV-GINPSLEL 951
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 71979930 952 SEMLYTDR-PDWQSVMQYVAQIYKYF 976
Cdd:cd21261 81 EDMMVMGRkPDPMCVFTYVQSLYNHL 106
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
871-977 |
3.19e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 98.19 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 871 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSL 949
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 71979930 950 ELSEMLYTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
873-977 |
7.11e-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: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEL 951
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
873-976 |
6.43e-23 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 94.38 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEl 951
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLD- 79
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21189 80 PEDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
874-976 |
6.88e-23 |
|
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: 94.56 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 874 KRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLELS 952
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDvAEREFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 71979930 953 EMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
875-978 |
4.17e-22 |
|
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: 91.96 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 875 RNALLKWCQKKTEGY-ANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKR--NLLLAFEAAQ-SVGINPSLE 950
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDKleNINLALDVAEkKLGVPKVLI 83
|
90 100
....*....|....*....|....*...
gi 71979930 951 LSEMLYTdrPDWQSVMQYVAQIYKYFET 978
Cdd:pfam00307 84 EPEDLVE--GDNKSVLTYLASLFRRFQA 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
872-977 |
5.54e-22 |
|
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: 91.72 E-value: 5.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 872 GSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLE 950
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRiAEQHLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 71979930 951 LSEMLyTDRPDWQSVMQYVAQIYKYFE 977
Cdd:cd21192 82 VEDVL-VDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
875-976 |
1.68e-21 |
|
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: 90.31 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 875 RNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLELSE 953
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 71979930 954 MLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
878-974 |
1.03e-20 |
|
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: 87.87 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 878 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLElSEMLY 956
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEhLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 71979930 957 TDRPDWQSVMQYVAQIYK 974
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
873-976 |
1.76e-20 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 87.40 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLElS 952
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLD-A 82
|
90 100
....*....|....*....|....
gi 71979930 953 EMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
873-976 |
2.10e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 87.81 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 951
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAeKELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
873-976 |
1.27e-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: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 951
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
873-976 |
1.38e-19 |
|
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: 85.52 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 951
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
873-976 |
2.28e-19 |
|
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: 84.78 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 951
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
873-976 |
2.40e-19 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 84.38 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLEl 951
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNlAEQHLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
876-972 |
5.04e-19 |
|
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: 83.13 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 876 NALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPY----QELNSQEKKRNLLLAFEAAQSVGINPSLEL 951
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQI 972
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
873-976 |
6.16e-19 |
|
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: 83.95 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAA-QSVGINPSLEl 951
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAeQHLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
873-976 |
4.39e-18 |
|
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: 81.29 E-value: 4.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLEL 951
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
871-976 |
5.52e-18 |
|
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: 80.44 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 871 GGSKRnALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGInPSL 949
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI-PRL 81
|
90 100
....*....|....*....|....*..
gi 71979930 950 ELSEMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21243 82 LDPEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
877-976 |
1.90e-17 |
|
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: 78.66 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 877 ALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLELSEmL 955
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 71979930 956 YTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
875-974 |
5.70e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 77.38 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 875 RNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPY---QELNSQEKKRNLLLAFEAAQSVGInPSLEL 951
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGL-PELDL 79
|
90 100
....*....|....*....|....*
gi 71979930 952 --SEMLYtDRPDWQSVMQYVAQIYK 974
Cdd:cd00014 80 fePEDLY-EKGNLKKVLGTLWALAL 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
873-976 |
5.21e-16 |
|
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: 74.64 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQSVGINPSLElS 952
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 71979930 953 EMLYTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
860-978 |
7.86e-16 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 81.91 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 860 RDPLAALAREYGGSKRNALLKWCQKKTEGYAN-IDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQ--EKKRNLLLA 936
Cdd:COG5069 112 RLTIATINEEGELTKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQA 191
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71979930 937 FEAAQ-SVGINPSLELSEMLYTDRPDWQSVMQYVAQIYKYFET 978
Cdd:COG5069 192 FENANkVIGIARLIGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
873-971 |
8.47e-15 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 71.11 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYAnidITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQS-VGINPSLE 950
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|.
gi 71979930 951 LSEMLYTDrPDWQSVMQYVAQ 971
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 ... |
873-976 |
2.36e-14 |
|
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: 69.86 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFE-AAQSVGINPSLEL 951
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRiAEQELKIPRLLEP 84
|
90 100
....*....|....*....|....*
gi 71979930 952 SEMLYTDrPDWQSVMQYVAQIYKYF 976
Cdd:cd21244 85 EDVDVVN-PDEKSIMTYVAQFLQYS 108
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
877-976 |
2.77e-14 |
|
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: 69.82 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 877 ALLKWCQKKTEGYAnIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLElSEML 955
Cdd:cd21245 7 ALLNWVQRRTRKYG-VAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQeSLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 71979930 956 YTDRPDWQSVMQYVAQIYKYF 976
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-646 |
4.49e-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: 77.02 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 278 GSSPNNASELS----LASLTEKIQKMEENqhstAEELQATLQELSDQQqmvQELTAENEKLVDEKTILETSFHQHRERAE 353
Cdd:TIGR02168 664 GSAKTNSSILErrreIEELEEKIEELEEK----IAELEKALAELRKEL---EELEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 354 QLSQENEKLINLLQERvkNEEPSAQGGKVLELEQKctdiLEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKE 433
Cdd:TIGR02168 737 RLEAEVEQLEERIAQL--SKELTELEAEIEELEER----LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 434 ENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLE------ADKQKAIEASST--VGQTAENFEVQEMLK 505
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeiEELEELIEELESelEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 506 VARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLS-RTSLKLQ---EKASESDAEIKDM 581
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEeaeALENKIEDDEEEA 970
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71979930 582 KETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWR-RFQA 646
Cdd:TIGR02168 971 RRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREAReRFKD 1036
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
871-977 |
5.01e-14 |
|
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: 68.92 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 871 GGSKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSL 949
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90 100
....*....|....*....|....*...
gi 71979930 950 ELSEMLYTDRPdwQSVMQYVAQIYKYFE 977
Cdd:cd21196 81 SAQAVVAGSDP--LGLIAYLSHFHSAFK 106
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
876-971 |
1.53e-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: 67.33 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 876 NALLKWCQKKTegyANIDITNFSSSWSDGLALCALLHTyLPAHIP-YQELNSQEKKRNLLLAFEAAQSVGINPSLELSEM 954
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 71979930 955 lyTDrPDWQS--VMQYVAQ 971
Cdd:cd21185 80 --AD-PEVEHlgIMAYAAQ 95
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
876-970 |
1.91e-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: 65.40 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 876 NALLKWCQKKTEGYaNIDITNFSSSWSDGLALCALLHTYLPAHIP----------------------------------- 920
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPldairqpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 71979930 921 -YQELNSQEkKRNLLLAFEAAQSVGINPS-LELSEMLYTdRPDWQSVMQYVA 970
Cdd:cd21224 82 lSSELLANE-KRNFKLVQQAVAELGGVPAlLRASDMSNT-IPDEKVVILFLS 131
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
878-974 |
2.02e-12 |
|
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: 64.56 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 878 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKK-RNLLLAFEAA-QSVGINPSLElSEML 955
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIArQHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 71979930 956 YTDRPDWQSVMQYVAQIYK 974
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
873-973 |
1.68e-10 |
|
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: 58.88 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQ-SVGINPSLEl 951
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 71979930 952 SEMLYTDRPDWQSVMQYVAQIY 973
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
878-974 |
2.91e-10 |
|
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: 58.05 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 878 LLKWCQKKTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQEKKRNLLLAFEAAQS-VGINPSLElSEMLY 956
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 71979930 957 TDRPDWQSVMQYVAQIYK 974
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
381-706 |
6.63e-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: 63.54 E-value: 6.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 381 KVLELEQKCTDILEKSRFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECR 460
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELE-QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 461 VTLEGLKMENGSLKALLEADKQkaieasstvgqtaenfEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLA 540
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIE----------------ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 541 KMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQK 620
Cdd:TIGR02168 828 SLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 621 SDLERQLKTLTKQIKEETEEWRRFQADLQtavvvandikcEAQQELRTVKRRLLEEEeknarlQKELGDIQGHSRPVNEE 700
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-----------GLEVRIDNLQERLSEEY------SLTLEEAEALENKIEDD 966
|
....*.
gi 71979930 701 PEPSEA 706
Cdd:TIGR02168 967 EEEARR 972
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-636 |
1.42e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 295 KIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsFHQHRERAEQLSQENEKlinlLQERVKNEE 374
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELER----LKKRLTGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 375 PSAQGGKVLELEQKCTDI-------------LEKSRFEREKLL-----------------------NIQQQLTCSLRKVE 418
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIeeeiskitarigeLKKEIKELKKAIeelkkakgkcpvcgrelteehrkELLEEYTAELKRIE 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 419 EENQGAIDMIKHLKEENEKLNGFLEHER--CNNSVMAKTLEECRVTLEGLKMENGSLKA-LLEADKQKAIEASSTVGQTA 495
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLK 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 496 ENFEVQEMLKVARAE----KDQLQLSCTELRQELLKANGE-IKHVSSLLAKMEKDYSYLKEVCD--HQAEQLSRTSLKLQ 568
Cdd:PRK03918 546 KELEKLEELKKKLAElekkLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDaeKELEREEKELKKLE 625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71979930 569 EKASESDAEIKDMKETIFELEDQVEQHRavKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKE 636
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-699 |
2.12e-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: 61.61 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 393 LEKSRFEREKLLN-IQQQLTCSLR----KVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVM---AKTLEECRVTLE 464
Cdd:TIGR02168 191 LEDILNELERQLKsLERQAEKAERykelKAELRELELALLVLRLEELREELEELQEELKEAEEELeelTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 465 GLKMENGSLKALLEaDKQKAIEAsstvgQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEK 544
Cdd:TIGR02168 271 ELRLEVSELEEEIE-ELQKELYA-----LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 545 DYSYLKEVCDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKS 621
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 622 DLERQLKTLTKQ--------IKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGH 693
Cdd:TIGR02168 425 ELLKKLEEAELKelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
....*.
gi 71979930 694 SRPVNE 699
Cdd:TIGR02168 505 SEGVKA 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-687 |
3.66e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 473 LKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEv 552
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 553 cdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTK 632
Cdd:COG1196 310 ---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71979930 633 QIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKEL 687
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALL-ERLERLEEELEELEEALAELEEEEEEE 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-558 |
4.79e-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: 60.46 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELSD-------QQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEK 361
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEElrlevseLEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 362 ----LINLLQERVKNEEPSAQGGKVLELEQKCTDILEKsrfEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 437
Cdd:TIGR02168 321 leaqLEELESKLDELAEELAELEEKLEELKEELESLEA---ELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 438 LNGFLEhercnnsVMAKTLEECRVTLEGLKMENGSL-KALLEADKQKAIEASSTVGQTAENFE-----VQEMLKVARAEK 511
Cdd:TIGR02168 398 LNNEIE-------RLEARLERLEDRRERLQQEIEELlKKLEEAELKELQAELEELEEELEELQeelerLEEALEELREEL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 71979930 512 DQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAE 558
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
283-687 |
5.23e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEENQH---STAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQEN 359
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREqarETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 360 EKLINLLQERVKNEEPSAQGGKVLELEQkctDILEKSRFEREKLLniqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLn 439
Cdd:PRK02224 289 EELEEERDDLLAEAGLDDADAEAVEARR---EELEDRDEELRDRL---EECRVAAQAHNEEAESLREDADDLEERAEEL- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 440 gfleheRCNNSVMAKTLEECRVTLEGLKMENGSLKALLEadkqkaiEASSTVGQTAENFE-VQEMLKVARAEKDQLQLSC 518
Cdd:PRK02224 362 ------REEAAELESELEEAREAVEDRREEIEELEEEIE-------ELRERFGDAPVDLGnAEDFLEELREERDELRERE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 519 TELRQELLKANGEIKHVSSLLAKmEKDYSYLKEVCDhqAEQLSRTSLKlQEKASESDAEIKDMKETIFELEDQVEqhRAV 598
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEA-GKCPECGQPVEG--SPHVETIEED-RERVEELEAELEDLEEEVEEVEERLE--RAE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 599 KLhnnqliSELEGSVIKLEEQKSDLERQLKTLTKQIKEETE---EWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLE 675
Cdd:PRK02224 503 DL------VEAEDRIERLEERREDLEELIAERRETIEEKREraeELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410
....*....|..
gi 71979930 676 EEEKNARLQKEL 687
Cdd:PRK02224 577 LNSKLAELKERI 588
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
873-971 |
9.52e-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: 53.93 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTEGyanIDITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQS-VGINPSLE 950
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|.
gi 71979930 951 LSEMLYTDrPDWQSVMQYVAQ 971
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 ... |
285-699 |
9.73e-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: 59.42 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 285 SELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL-- 362
Cdd:pfam01576 24 AESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMqq 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 363 -INLLQERVKNEEPSAQGgkvLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGaiDMIKHLKEENEKLNGf 441
Cdd:pfam01576 104 hIQDLEEQLDEEEAARQK---LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERIS--EFTSNLAEEEEKAKS- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 442 LEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEAdkqkaiEASSTVGQTAENFEVQEMLKVARAEK-DQLQLSCTE 520
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEG------ESTDLQEQIAELQAQIAELRAQLAKKeEELQAALAR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 521 LRQELLKANGEIKHVSSL---LAKMEKDYSyLKEVCDHQAEQLSR----------------------------------T 563
Cdd:pfam01576 252 LEEETAQKNNALKKIRELeaqISELQEDLE-SERAARNKAEKQRRdlgeelealkteledtldttaaqqelrskreqevT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 564 SLK--LQEKASESDAEIKDMKE----TIFELEDQVEQHRAVKlhnnqliSELEGSVIKLEEQKSDLERQLKTLTkQIKEE 637
Cdd:pfam01576 331 ELKkaLEEETRSHEAQLQEMRQkhtqALEELTEQLEQAKRNK-------ANLEKAKQALESENAELQAELRTLQ-QAKQD 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71979930 638 TEEWRRFQ----ADLQTAVVVANDIKCEA-------QQELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNE 699
Cdd:pfam01576 403 SEHKRKKLegqlQELQARLSESERQRAELaeklsklQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE 475
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-640 |
1.35e-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: 58.88 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEEnqhstaeeLQATLQELSDQQQMVQE-LTAENEKLVDEKTILETSfhqhRERAEQLSQENEK 361
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKS--------LESQISELKKQNNQLKDnIEKKQQEINEKTTEISNT----QTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 362 LINLLQErvKNEEPSAQGGKVLELEQKCTDI-LEKSRFEREKLLNIQQQLTCSLRKVEEENQGA-------IDMIKHLKE 433
Cdd:TIGR04523 265 IKKQLSE--KQKELEQNNKKIKELEKQLNQLkSEISDLNNQKEQDWNKELKSELKNQEKKLEEIqnqisqnNKIISQLNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 434 ENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTV-GQTAENFEVQEMLKVARAEKD 512
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKLNQQKDEQIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 513 QLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTS------------------------LKLQ 568
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLN 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 569 EKASESDAEIKDMKETIFELEDQVEQHRA------------------------------VKLHNNQLISELEGSVIKLEE 618
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdledelnkddfelkkenlekEIDEKNKEIEELKQTQKSLKK 582
|
410 420
....*....|....*....|..
gi 71979930 619 QKSDLERQLKTLTKQIKEETEE 640
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKE 604
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-691 |
2.23e-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: 58.11 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILE-----------TSFHQHRER 351
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEkeklniqknidKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 352 AEQLS------QENEKL---INLLQERV---------KNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS 413
Cdd:TIGR04523 200 ELLLSnlkkkiQKNKSLesqISELKKQNnqlkdniekKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 414 LRKVEE---------------ENQGAIDMIKHLKEE------------------NEKLNGF----------LEHERCNNS 450
Cdd:TIGR04523 280 NKKIKElekqlnqlkseisdlNNQKEQDWNKELKSElknqekkleeiqnqisqnNKIISQLneqisqlkkeLTNSESENS 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 451 VMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTV-GQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKAN 529
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 530 GEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTS------------------------LKLQEKASESDAEIKDMKETI 585
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskekelKKLNEEKKELEEKVKDLTKKI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 586 FELEDQVEQHRAVKLHNNQLISELEGsviKLEEQKSDLER-QLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQ 664
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLED---ELNKDDFELKKeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK 596
|
490 500
....*....|....*....|....*..
gi 71979930 665 ELRTVKRRLLEEEEKNARLQKELGDIQ 691
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
282-686 |
3.16e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 282 NNASELSLasLTEKIQKmeenQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTiletsfhQHRERAEQLSQENEK 361
Cdd:pfam05483 374 KNEDQLKI--ITMELQK----KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK-------QFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 362 LINLLQERVKN-EEPSAQGGKVLELEQKCTDILE--KSRFEREKLLNIQQQLTCSLRKVEEEN--QGAIDMIKHLKEENE 436
Cdd:pfam05483 441 LIFLLQAREKEiHDLEIQLTAIKTSEEHYLKEVEdlKTELEKEKLKNIELTAHCDKLLLENKEltQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 437 KLNGFLEHERcnnsVMAKTLEECRVTLEGLKMEngsLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQ-LQ 515
Cdd:pfam05483 521 DIINCKKQEE----RMLKQIENLEEKEMNLRDE---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKiLE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 516 LSCTELR----------QELLKANGEIKHVSSLLAKMEKDYsylkEVCDHQAE-QLSRTSLKLQEKASESDAEIKDMKET 584
Cdd:pfam05483 594 NKCNNLKkqienknkniEELHQENKALKKKGSAENKQLNAY----EIKVNKLElELASAKQKFEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 585 IFELEDQVEQHRAVKLHNNQLISELEGSVI-KLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCE-- 661
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAVKLQKEIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIEls 749
|
410 420
....*....|....*....|....*.
gi 71979930 662 -AQQELRTVKRRLLEEEEKNARLQKE 686
Cdd:pfam05483 750 nIKAELLSLKKQLEIEKEEKEKLKME 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
293-688 |
4.36e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 293 TEKIQKMEENQHstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhQHRERAEQLSQENEKL---INLLQER 369
Cdd:PRK03918 188 TENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEELEKELESLegsKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 370 VKN------------EEPSAQGGKVLELEQKCTDILEKSRFeREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 437
Cdd:PRK03918 261 IREleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 438 LNGFLEHErcnnsvmaKTLEECRVTLEGLKMENGSLKALL-EADKQKAIEASSTVGqtaenfEVQEMLKVARAEKdqlql 516
Cdd:PRK03918 340 LEELKKKL--------KELEKRLEELEERHELYEEAKAKKeELERLKKRLTGLTPE------KLEKELEELEKAK----- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 517 scTELRQELLKANGEIKHVSSLLAKMEKDYSYLKE------VCDHQAEQLSRTSLKlqekaSESDAEIKDMKETIFELED 590
Cdd:PRK03918 401 --EEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpVCGRELTEEHRKELL-----EEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 591 QVEQHRAVKLHNNQLISElEGSVIKLE---EQKSDLERQLKTLT-KQIKEETEEWRRFQADLQT----AVVVANDIK--C 660
Cdd:PRK03918 474 KERKLRKELRELEKVLKK-ESELIKLKelaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKlkgeIKSLKKELEklE 552
|
410 420
....*....|....*....|....*...
gi 71979930 661 EAQQELRTVKRRLLEEEEKNARLQKELG 688
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELE 580
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
283-687 |
7.48e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQE----LTAENEKLvDEKTILETSFHQHRERAEQLSQE 358
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQshayLTQKREAQ-EEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 359 nEKLINLLQERV----KNEEPSAQGGKVLELEQKCTDI---LEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIK-- 429
Cdd:TIGR00618 276 -EAVLEETQERInrarKAAPLAAHIKAVTQIEQQAQRIhteLQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqe 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 430 -HLKEENEKLNGFLEHeRCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQkaiEASSTVGQTAENFEVQEMLKVAR 508
Cdd:TIGR00618 355 iHIRDAHEVATSIREI-SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR---EQATIDTRTSAFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 509 AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFEL 588
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ----QLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 589 EDQvEQHRAVKLH-------NNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCE 661
Cdd:TIGR00618 507 CGS-CIHPNPARQdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
410 420
....*....|....*....|....*.
gi 71979930 662 AQQeLRTVKRRLLEEEEKNARLQKEL 687
Cdd:TIGR00618 586 IPN-LQNITVRLQDLTEKLSEAEDML 610
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
275-691 |
7.66e-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: 56.61 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 275 SPTGSSPNNASEL-SLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAE 353
Cdd:TIGR02169 661 APRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 354 Q----LSQENEKLINLLQERVKNE-EPSAQGGKVLELEQKCTDIleKSRFEREKLLNIQQQltcsLRKVEEENQgaiDMI 428
Cdd:TIGR02169 741 EleedLSSLEQEIENVKSELKELEaRIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAE----LSKLEEEVS---RIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 429 KHLKEENEKLNgflehercnnsvmaktleecRVTLEglkmengslKALLEADKQKAIEasstvgqtaENFEVQEMLKVAR 508
Cdd:TIGR02169 812 ARLREIEQKLN--------------------RLTLE---------KEYLEKEIQELQE---------QRIDLKEQIKSIE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 509 AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSylkevcdhqaeqlsrtslKLQEKASESDAEIKDMKETIFEL 588
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD------------------ELEAQLRELERKIEELEAQIEKK 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 589 EDQVEQHRAVKLHNNQLISELEGSVIKLEEQkSDLERQLKTLTKQIKEETEEWRRFQadlqtavvvanDIKCEAQQELRT 668
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIRALE-----------PVNMLAIQEYEE 983
|
410 420
....*....|....*....|...
gi 71979930 669 VKRRLLEEEEKNARLQKELGDIQ 691
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAIL 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
283-547 |
1.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL 362
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 363 INLLQERVKNEEpsAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLtcsLRKVEEENQGAIDMIKHLKEENEKLNGFL 442
Cdd:COG1196 329 EEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 443 EHERcNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENfevQEMLKVARAEKDQLQLSCTELR 522
Cdd:COG1196 404 ELEE-AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE---EEALLELLAELLEEAALLEAAL 479
|
250 260
....*....|....*....|....*
gi 71979930 523 QELLKANGEIKHVSSLLAKMEKDYS 547
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYE 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
283-676 |
2.05e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.12 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 283 NASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAEneklvdektiletsfHQHRERAEQLSQENekl 362
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTAS---------------LQEKERAIEATNAE--- 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 363 INLLQERVKneepsaqggkvLELEQkctdiLEKSRFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGfl 442
Cdd:pfam15921 519 ITKLRSRVD-----------LKLQE-----LQHLKNEGDHLRNVQTECE-ALKLQMAEKDKVIEILRQQIENMTQLVG-- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 443 EHERCNNSVMAKTlEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVgqtaENFEVqEMLKVARAEKDQLQlSCTELR 522
Cdd:pfam15921 580 QHGRTAGAMQVEK-AQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLEL-EKVKLVNAGSERLR-AVKDIK 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 523 QELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN 602
Cdd:pfam15921 653 QERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71979930 603 NQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQeLRTVKRRLLEE 676
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEK 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
391-678 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 391 DILEKS-------RFEREKLLNiQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTL 463
Cdd:TIGR02169 647 ELFEKSgamtggsRAPRGGILF-SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 464 EGLKMENGSLKALLE--ADKQKAIEASSTvgqtaenfEVQEMLKVARAEKDQLQLSCTELRQELLK-----ANGEIKHVS 536
Cdd:TIGR02169 726 EQLEQEEEKLKERLEelEEDLSSLEQEIE--------NVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQ 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 537 SLLAKMEKDYSYLKEVCDHQAEQLSRTSLK---LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSV 613
Cdd:TIGR02169 798 AELSKLEEEVSRIEARLREIEQKLNRLTLEkeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71979930 614 IKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKC---EAQQELRTVKRRLLEEEE 678
Cdd:TIGR02169 878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAkleALEEELSEIEDPKGEDEE 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-691 |
4.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTA--ENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLL 366
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 367 QERVKNEEpsaqggKVLELEQKCTDILEKSRFEREKLLniqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGflEHER 446
Cdd:COG4717 163 EELEELEA------ELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQRLAELEEELEEAQEELEELEE--ELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 447 CNNSVMAKTLEECRVTLEGLKMENGSLkALLEADKQKAIEASSTVGQTAenFEVQEMLKVARAEKDQLQLSCTELRQELL 526
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAAL-LALLGLGGSLLSLILTIAGVL--FLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 527 KANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKEtifeleDQVEQHRAVKLHNNQLI 606
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------EELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 607 SELE-GSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvvandikcEAQQELRTVKRRLLEEEEKNARLQK 685
Cdd:COG4717 383 DEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---------ELEEELEELEEELEELEEELEELRE 453
|
....*.
gi 71979930 686 ELGDIQ 691
Cdd:COG4717 454 ELAELE 459
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
286-686 |
4.72e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.04 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 286 ELSLASLTEKIQKMEENQHSTA----EELQATLQE---LSDQQQmvQELTAENEKLVDEKTILETSFHQHRERAEQLSQE 358
Cdd:PRK10246 175 ELTGTEIYGQISAMVFEQHKSArtelEKLQAQASGvalLTPEQV--QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 359 NEklinLLQERVKNEEPSAQGGKVLELEQKCTDILE---KSRFEREKLLNIQQQ---LTCSLRKVEEEN----------- 421
Cdd:PRK10246 253 DE----LQQEASRRQQALQQALAAEEKAQPQLAALSlaqPARQLRPHWERIQEQsaaLAHTRQQIEEVNtrlqstmalra 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 422 ---QGAIDMIKHLKEENEKLNGFL-EHERCNnsVMAKTLEECRVTLEGLKMENGSLKAL---LEADKQK-AIEASSTVGQ 493
Cdd:PRK10246 329 rirHHAAKQSAELQAQQQSLNTWLaEHDRFR--QWNNELAGWRAQFSQQTSDREQLRQWqqqLTHAEQKlNALPAITLTL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 494 TAENfevqemLKVARAEKDQLQlsctELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKAS- 572
Cdd:PRK10246 407 TADE------VAAALAQHAEQR----PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQq 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 573 --------ESDAEIKDMKETIFELED-------------QVEQHRAVKLHNNQL-ISELEGSVIKLEEQKSDLERQLKTL 630
Cdd:PRK10246 477 ladvkticEQEARIKDLEAQRAQLQAgqpcplcgstshpAVEAYQALEPGVNQSrLDALEKEVKKLGEEGAALRGQLDAL 556
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71979930 631 TKQIKEE--------------TEEWRRFQADLQTAVVVANDI------KCEAQQELRTVKRRLLEEEEKNARLQKE 686
Cdd:PRK10246 557 TKQLQRDeseaqslrqeeqalTQQWQAVCASLNITLQPQDDIqpwldaQEEHERQLRLLSQRHELQGQIAAHNQQI 632
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
496-698 |
6.59e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 6.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 496 ENF----EVQEMLKVARAEKDQLQLSCtELRQELLKANGEIKHVSSLLAKM-----EKDYSYLKEVCDHQAEQLSRtslk 566
Cdd:COG4913 232 EHFddleRAHEALEDAREQIELLEPIR-ELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELAR---- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 567 LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHN-NQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQ 645
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQlEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 71979930 646 ADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQghSRPVN 698
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE--RRKSN 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
308-658 |
1.08e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 308 EELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhQHRERAEQLSQENEKLINLLQERVKNEEpsaqggKVLELEQ 387
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQ------EIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 388 KCTDIleKSRFEREKLLNiqQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVT----- 462
Cdd:TIGR04523 392 QINDL--ESKIQNQEKLN--QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTresle 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 463 --LEGLKMENGSLKALLEADKQKAIEASSTVGQ-TAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLL 539
Cdd:TIGR04523 468 tqLKVLSRSINKIKQNLEQKQKELKSKEKELKKlNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 540 AKM--EKDYSYLKEVCDHQAEQLSR-----TSLK-----LQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLIS 607
Cdd:TIGR04523 548 NKDdfELKKENLEKEIDEKNKEIEElkqtqKSLKkkqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71979930 608 ELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDI 658
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDI 678
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
289-684 |
1.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLL 366
Cdd:COG4717 90 YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 367 QERVKNEEpsaqggkvlELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHER 446
Cdd:COG4717 170 AELAELQE---------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 447 CNNSV------------------MAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVAR 508
Cdd:COG4717 241 LEERLkearlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 509 --AEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKdysyLKEVCDHQAEQLSRTSLkLQEKASESDAEI-------- 578
Cdd:COG4717 321 leELLAALGLPPDLSPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL-LAEAGVEDEEELraaleqae 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 579 --KDMKETIFELEDQVEQHRAVKLHNNQLISELEgsvikLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvVAN 656
Cdd:COG4717 396 eyQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEELEELEEELEELEEELEELREELAELEAELEQL--EED 468
|
410 420
....*....|....*....|....*...
gi 71979930 657 DIKCEAQQELRTVKRRLLEEEEKNARLQ 684
Cdd:COG4717 469 GELAELLQELEELKAELRELAEEWAALK 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
428-691 |
3.20e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 428 IKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEV-QEMLKV 506
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARlEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 507 ARAEKDQLQLSCTELRQELLKANGEIkhvssllakmekdysylkevcdhqaEQLSRTSLKLQEKASESDAEIKDMKETIF 586
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEEL-------------------------EELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 587 ELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANdikcEAQQEL 666
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----EEEEAL 444
|
250 260
....*....|....*....|....*
gi 71979930 667 RTVKRRLLEEEEKNARLQKELGDIQ 691
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELL 469
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
499-789 |
3.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 499 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEK-ASESDAE 577
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSgGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 578 IKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEwrrfQADLQTAVVVAND 657
Cdd:COG3883 107 VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA----KAELEAQQAEQEA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 658 IKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNEEPEPSEADAAGRWRGVYVNRTSPAPSDSATTVKSLIKS 737
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 71979930 738 FDLGHSGGTGQSISVhkTPRSPLSGIPVRTAPAAAVSPMQRHSTYSSMKPAS 789
Cdd:COG3883 263 GAAGAAAGAAGAGAA--AASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGG 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-659 |
3.51e-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: 50.53 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 454 KTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEM-LKVARAEKDQLQLSCTELRQEL------L 526
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIAELRAELEAQKEELaellraL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 527 KANGEIKHVSSLL-----AKMEKDYSYLKEVCDH---QAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAV 598
Cdd:COG4942 114 YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71979930 599 KLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIK 659
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
878-950 |
3.59e-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: 3.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71979930 878 LLKWCQK--KTEGYANIDITNFSSSWSDGLALCALLHTYLPAHIP----YQELNSQEKKRNLLLAFEAAQSVGINPSLE 950
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLT 93
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-713 |
4.65e-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: 50.15 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 499 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEI 578
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA----ELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 579 KDM------------------KETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEE 640
Cdd:COG4942 107 AELlralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71979930 641 wrrfQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNEEPEPSE-ADAAGRWR 713
Cdd:COG4942 187 ----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGfAALKGKLP 256
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
308-690 |
8.77e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 308 EELQATLQELsdqqQMVQELTAENEKLVDEKtiletsfhqhRERAEQLSQENEKLINL--LQERVKNEEPSAQGGKVLEL 385
Cdd:TIGR02169 170 RKKEKALEEL----EEVEENIERLDLIIDEK----------RQQLERLRREREKAERYqaLLKEKREYEGYELLKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 386 EQkctdilEKSRFEREkLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCNnsvMAKTLEECRVTLEG 465
Cdd:TIGR02169 236 ER------QKEAIERQ-LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 466 LKmenGSLKAL------LEADKQKAIEASSTVGQTAENFEvqEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLL 539
Cdd:TIGR02169 306 LE---RSIAEKereledAEERLAKLEAEIDKLLAEIEELE--REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 540 AKMEKDYSYLKEVCD---HQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKL 616
Cdd:TIGR02169 381 AETRDELKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71979930 617 EEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAvvvandiKCEAQQELRTVKRRLLEEEEKNARLQKELGDI 690
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-------EAQARASEERVRGGRAVEEVLKASIQGVHGTV 527
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
894-956 |
1.25e-05 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 44.21 E-value: 1.25e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71979930 894 ITNFSSSWSDGLALCALLHTYLPAHIPYQELNSQE------KKRNLLLAFEAAQS-VGINPS-LELSEMLY 956
Cdd:pfam11971 13 VEDLLRDLSDGCALAALIHFYCPQLIDLEDICLKEsmsladSLYNIQLLQEFCQRhLGNRCChLTLEDLLY 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-709 |
1.44e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 456 LEECRVTLEGLKMEngSLKALLEADKQKAIEASSTVgqtaenFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHV 535
Cdd:TIGR02168 222 LRELELALLVLRLE--ELREELEELQEELKEAEEEL------EELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 536 SSLLAKMEKDYSYLKE----------VCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQL 605
Cdd:TIGR02168 294 ANEISRLEQQKQILRErlanlerqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 606 ISELEGSVIKLEEQKSDLERQLKTLTKQI----------KEETEEWRRFQADLQTAVVVANdiKCEAQQELRTVKRRLLE 675
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNEIerlearlerlEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEE 451
|
250 260 270
....*....|....*....|....*....|....
gi 71979930 676 EEEKNARLQKELGDIQGHSRPVNEEPEPSEADAA 709
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELA 485
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
894-956 |
3.57e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 43.53 E-value: 3.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71979930 894 ITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQSV-GI----------NPSL-ELSEMLY 956
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAKREfNIpmvlspedlsSPHLdELSGMTY 96
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
871-971 |
3.66e-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: 44.00 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 871 GGSKRNALLKWCQKKTegyANIDITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQSVGINPSL 949
Cdd:cd21315 14 GPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAEDWLDVPQL 90
|
90 100
....*....|....*....|..
gi 71979930 950 ELSEMLYTDRPDWQSVMQYVAQ 971
Cdd:cd21315 91 IKPEEMVNPKVDELSMMTYLSQ 112
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
873-974 |
4.26e-05 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 43.54 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQS-VGINPSLE 950
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCPdWESWDPQKPVDNAREAMQQADDwLGVPQVIT 84
|
90 100
....*....|....*....|....
gi 71979930 951 LSEMLYTDrPDWQSVMQYVAQIYK 974
Cdd:cd21313 85 PEEIIHPD-VDEHSVMTYLSQFPK 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-675 |
4.85e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 284 ASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKL- 362
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAa 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 363 --INLLQERVKNEEPSAQGGKVLELEQK------CTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQgAIDMIKHLKEE 434
Cdd:COG1196 491 arLLLLLEAEADYEGFLEGVKAALLLAGlrglagAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV-AAAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 435 NEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQL 514
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 515 QLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQ 594
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 595 HRAVKLHNNQLISELEGSVIKLEEQK-------SDLERQLKTLTKQIK-------------EETEEWRRF----QADLQT 650
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEalgpvnllaieeyEELEERYDFlseqREDLEE 809
|
410 420
....*....|....*....|....*.
gi 71979930 651 AVvvaNDIKcEAQQEL-RTVKRRLLE 675
Cdd:COG1196 810 AR---ETLE-EAIEEIdRETRERFLE 831
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
452-702 |
6.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 452 MAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAEnfEVQEMLKVARAEKDQLQLSCTELRQELLKANGE 531
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELE--QLREELEQAREELEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 532 IKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEG 611
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQE----ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 612 SVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 691
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250
....*....|.
gi 71979930 692 GHSRPVNEEPE 702
Cdd:COG4372 238 LLDALELEEDK 248
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
873-974 |
7.18e-05 |
|
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: 43.14 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKTegyANIDITNFSSSWSDGLALCALLHTYLPAHIP-YQELNSQEKKRNLLLAFEAAQS-VGInPSLE 950
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPdWESWDPNQPVQNAREAMQQADDwLGV-PQVI 86
|
90 100
....*....|....*....|....
gi 71979930 951 LSEMLYTDRPDWQSVMQYVAQIYK 974
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQFPK 110
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
496-674 |
7.30e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 496 ENFEVQEMLKVARAEKDQL-----QLSCTELRQELLKANGEIKHVSSLlakMEKDYSYLKEVcDHQAEQLSRTSLKLQEK 570
Cdd:PRK04778 250 DHLDIEKEIQDLKEQIDENlalleELDLDEAEEKNEEIQERIDQLYDI---LEREVKARKYV-EKNSDTLPDFLEHAKEQ 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 571 ASESDAEIKDMKETiFEL-EDQVEQHRAVKLHNNQLISELEGSVIKLEEQK---SDLERQLKTLTKQIKEETEEWRRFQA 646
Cdd:PRK04778 326 NKELKEEIDRVKQS-YTLnESELESVRQLEKQLESLEKQYDEITERIAEQEiaySELQEELEEILKQLEEIEKEQEKLSE 404
|
170 180 190
....*....|....*....|....*....|.
gi 71979930 647 DLQT---AVVVANDIKCEAQQELRTVKRRLL 674
Cdd:PRK04778 405 MLQGlrkDELEAREKLERYRNKLHEIKRYLE 435
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
294-687 |
8.42e-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: 46.64 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 294 EKIQKMEENQHSTAEELQATLQE----LSDQQQMVQELTAENEKLvdektiletsfhqhRERAEQLSQENEKLInllqer 369
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKV--------------SLKLEEEIQENKDLI------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 370 vknEEPSAQGGKVLELEQKCTDILEK-SRFEREKllniqqqltcslrkvEEENQGAIDMIKHLKEeneklngflehercn 448
Cdd:pfam05483 148 ---KENNATRHLCNLLKETCARSAEKtKKYEYER---------------EETRQVYMDLNNNIEK--------------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 449 nsvMAKTLEECRVTLEGLKMEngsLKALLEADKQKAIEASSTVGQTAENFEVQ-EMLKVARAEKDQLQLSCTELRQELLK 527
Cdd:pfam05483 195 ---MILAFEELRVQAENARLE---MHFKLKEDHEKIQHLEEEYKKEINDKEKQvSLLLIQITEKENKMKDLTFLLEESRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 528 ANGEIKHVSSLlakMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMK---ETIFEL----EDQVEQHRAVKL 600
Cdd:pfam05483 269 KANQLEEKTKL---QDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatKTICQLteekEAQMEELNKAKA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 601 HNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAqQELRTV---KRRLLEEE 677
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-EELKKIlaeDEKLLDEK 424
|
410
....*....|
gi 71979930 678 EKNARLQKEL 687
Cdd:pfam05483 425 KQFEKIAEEL 434
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
479-785 |
8.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 479 ADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAE 558
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 559 QLSRTS---------------------LKLQEKASESDAE-IKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKL 616
Cdd:COG3883 94 ALYRSGgsvsyldvllgsesfsdfldrLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 617 EEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKELGDIQGHSRP 696
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA-AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 697 VNEEPEPSEADAAGRWRGVYVNRTSPAPSDSATTVKSLIKSFDLGHSGGTGQSISVHKTPRSPLSGIPVRTAPAAAVSPM 776
Cdd:COG3883 253 GAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGG 332
|
....*....
gi 71979930 777 QRHSTYSSM 785
Cdd:COG3883 333 GSGGGGGSS 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
297-720 |
8.77e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 297 QKMEENQhsTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILEtsfhqHRERAEQLSQENEKLINLLQERVKNEEP- 375
Cdd:PTZ00121 1385 KKAEEKK--KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE-----EKKKADEAKKKAEEAKKADEAKKKAEEAk 1457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 376 SAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS------LRKVEEENQGAIDMIKhlKEENEKLNGFLEHERCNN 449
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAkkkadeAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKK 1535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 450 SVMAKTLEECRVTLEGLKMEngSLKALLEA----DKQKAIEASSTVGQTAEnfEVQEMLKVARAEKDQLQLSCTELRQEL 525
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAE--ELKKAEEKkkaeEAKKAEEDKNMALRKAE--EAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 526 LKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSlklQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQl 605
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE---ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE- 1687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 606 iSELEGSVIKLEEQKsdleRQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKN--ARL 683
Cdd:PTZ00121 1688 -KKAAEALKKEAEEA----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHL 1762
|
410 420 430
....*....|....*....|....*....|....*..
gi 71979930 684 QKELGDIQGHSRPVNEEPEPSEADAAGRWRGVYVNRT 720
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
520-689 |
1.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 520 ELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRtslklQEKASESDAEIKDMKETIFELEDQVEQHRAvk 599
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQE----RREALQR-----LAEYSWDEIDVASAEREIAELEAELERLDA-- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 600 lhNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTV---KRRLLEE 676
Cdd:COG4913 683 --SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleeRFAAALG 760
|
170
....*....|...
gi 71979930 677 EEKNARLQKELGD 689
Cdd:COG4913 761 DAVERELRENLEE 773
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
294-633 |
1.32e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 294 EKIQKMEENQhstaEELQATLQELSDQQQMVQELTAENEKLVDEKTILETS-------------FHQHRERAEQLSqENE 360
Cdd:pfam05557 146 AKASEAEQLR----QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSkselaripelekeLERLREHNKHLN-ENI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 361 KLINLLQERVKNEEpsaqggKVLELEQKCTDILEKSRFEREKLL-------NIQQQLTCSLR-------KVEEENQGAID 426
Cdd:pfam05557 221 ENKLLLKEEVEDLK------RKLEREEKYREEAATLELEKEKLEqelqswvKLAQDTGLNLRspedlsrRIEQLQQREIV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 427 mikhLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEAsstvgqTAENFEVQEMLKV 506
Cdd:pfam05557 295 ----LKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLL------TKERDGYRAILES 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 507 ARAEkdqlqLSCTELRQELLKANGEikhvsslLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETif 586
Cdd:pfam05557 365 YDKE-----LTMSNYSPQLLERIEE-------AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ-- 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 71979930 587 elEDQVEQHRAVKLHNN--QLISELEGSVIKLEEQKSDLERQLKTLTKQ 633
Cdd:pfam05557 431 --ESLADPSYSKEEVDSlrRKLETLELERQRLREQKNELEMELERRCLQ 477
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
69-693 |
1.57e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 69 TPAKPKQEHEgaEKAVLESQVRELLAEAKTKDSEINRLRSELKKCKER--------WALSTEDANASDPSAEGTASPESD 140
Cdd:TIGR00618 210 TPCMPDTYHE--RKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqllkQLRARIEELRAQEAVLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 141 AQPLIRTLEEKNKTFQKELADLEEENRALKEKLTYLEQSpnSEGAASHTGDSScptsithESSFGSPVGNELSSETDEYR 220
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL--LMKRAAHVKQQS-------SIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 221 RTTHGSALRTSGSSSSDVTKASLSPDASDFEHITADTPS--------RPLSATSNPFKSSKGSPTGsspnnasELSLASL 292
Cdd:TIGR00618 359 DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSlckeldilQREQATIDTRTSAFRDLQG-------QLAHAKK 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 293 TEKIQK--MEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTIL--ETSFHQHRERAEQLSQENE-----KLI 363
Cdd:TIGR00618 432 QQELQQryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHlqETRKKAVVLARLLELQEEPcplcgSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 364 NLLQERVKNEEPS-------------AQGGKVLE-LEQKCTDILEKSRFEREKLLNIQQ----------QLTCSLRKVEE 419
Cdd:TIGR00618 512 HPNPARQDIDNPGpltrrmqrgeqtyAQLETSEEdVYHQLTSERKQRASLKEQMQEIQQsfsiltqcdnRSKEDIPNLQN 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 420 ENQGAIDMIKHLKEENEKLNGFLE------HERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQ 493
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHallrklQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLP 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 494 TAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLlakmekdysylkevcDHQAEQLSRTSLKLQEKASE 573
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY---------------DREFNEIENASSSLGSDLAA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 574 SDAEIKDMKETIFELEDQVEQHRAVKLHNNqliSELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVV 653
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNN---NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 71979930 654 VANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGH 693
Cdd:TIGR00618 814 SDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
74-688 |
2.88e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 74 KQEHEGAEKAVLESQVRELLAEAKTKdseINRLRSELKKCKERWALSTE--DANASDPSAEGTASPESDAQPLirtleEK 151
Cdd:pfam12128 277 RQEERQETSAELNQLLRTLDDQWKEK---RDELNGELSAADAAVAKDRSelEALEDQHGAFLDADIETAAADQ-----EQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 152 NKTFQKELADLEEENRALKEKLTYLEQSPNSEGAAShtgDSSCPTSIThessfGSPVGNELSSETDEYRRT---THGSAL 228
Cdd:pfam12128 349 LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI---KEQNNRDIA-----GIKDKLAKIREARDRQLAvaeDDLQAL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 229 RTSGSSSSDVTKASLSPDASDFEHITADTPSRPLSATSNPfksskgsptgsspnnASELSLASLTEKIQKMEENQ-HSTA 307
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATP---------------ELLLQLENFDERIERAREEQeAANA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 308 EELQATLQE-----LSDQQqmvqeltaeNEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQERVKNEEPSAqgGKV 382
Cdd:pfam12128 486 EVERLQSELrqarkRRDQA---------SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSI--GKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 383 LELEQKC-TDI-------------------LEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLNGFL 442
Cdd:pfam12128 555 ISPELLHrTDLdpevwdgsvggelnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 443 EHERCNNSVMAKTLEECRVTLEGLKMENGSLK----ALLEADKQKAIEASSTVG--QTAENFEVQEMLKvarAEKDQLQL 516
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKdkknKALAERKDSANERLNSLEaqLKQLDKKHQAWLE---EQKEQKRE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 517 SCTELRQELLKANGEIK-HVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKL---QEKASESDAEIKDMKETIFELEdqV 592
Cdd:pfam12128 712 ARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIERIA--V 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 593 EQHRAVKLH---NNQLISELEgsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTV 669
Cdd:pfam12128 790 RRQEVLRYFdwyQETWLQRRP----RLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGL 865
|
650 660
....*....|....*....|....
gi 71979930 670 KRRL-----LEEEEKNARLQKELG 688
Cdd:pfam12128 866 RCEMsklatLKEDANSEQAQGSIG 889
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-709 |
3.34e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKME---ENQHSTAEELQATLQEL-SDQQQMVQELTAENEKLVdektILETSFHQHRERAEQLSQENEKLIN 364
Cdd:TIGR02168 353 LESLEAELEELEaelEELESRLEELEEQLETLrSKVAQLELQIASLNNEIE----RLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 365 LLQERVKNEepsaQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLtcslRKVEEENQGAIDMIKHLKEENEKLNGFLEH 444
Cdd:TIGR02168 429 KLEEAELKE----LQAELEELEEELEELQEELERLEEALEELREEL----EEAEQALDAAERELAQLQARLDSLERLQEN 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 445 ERcNNSVMAKTLEECRVTLEGLKmenGSLKALLEADK--QKAIEAssTVGQTAENFEV---------QEMLKVARAEK-- 511
Cdd:TIGR02168 501 LE-GFSEGVKALLKNQSGLSGIL---GVLSELISVDEgyEAAIEA--ALGGRLQAVVVenlnaakkaIAFLKQNELGRvt 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 512 ---------DQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLkevcdhqaeqLSRTSLKLQEKASESDAEIKDMK 582
Cdd:TIGR02168 575 flpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL----------LGGVLVVDDLDNALELAKKLRPG 644
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 583 ETIFELEDQV-----------EQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTa 651
Cdd:TIGR02168 645 YRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE- 723
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71979930 652 vvvANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNEEPEPSEADAA 709
Cdd:TIGR02168 724 ---LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
278-686 |
4.16e-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: 44.58 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 278 GSSPNNASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETsfhqhRERAEQLSQ 357
Cdd:pfam02463 129 GISPEAYNFLVQGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEE-----LKLQELKLK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 358 ENEKLINLLQERVKNEEPSAQGGKVLELEQkctdILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEK 437
Cdd:pfam02463 204 EQAKKALEYYQLKEKLELEEEYLLYLDYLK----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 438 LNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLS 517
Cdd:pfam02463 280 EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 518 CTELRQELLKangeikhvssllakmekdysylkevcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIF---ELEDQVEQ 594
Cdd:pfam02463 360 ELEKLQEKLE----------------------------QLEEELLAKKKLESERLSSAAKLKEEELELKseeEKEAQLLL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 595 HRAVKLHNNQLISELEGSVIKLEEQKSdLERQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRLL 674
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEES-IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
410
....*....|..
gi 71979930 675 EEEEKNARLQKE 686
Cdd:pfam02463 491 SRQKLEERSQKE 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-513 |
4.23e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQE 368
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 369 RVKNEEPSAQGGKVLELeqkctdileksrFEREKLLNIQQQLTcSLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCN 448
Cdd:COG4942 109 LLRALYRLGRQPPLALL------------LSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71979930 449 NSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAENFEvQEMLKVARAEKDQ 513
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-ALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
288-640 |
4.45e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 288 SLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQ 367
Cdd:TIGR00618 543 SEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 368 ERVKNEEPSAQGGKVLELEQkctdiLEKSRFEREKLLNIQQQLTCSLRKVEEENqgaidmiKHLKEENEKLNGFLEHERC 447
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELA-----LKLTALHALQLTLTQERVREHALSIRVLP-------KELLASRQLALQKMQSEKE 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 448 NNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQkaieASSTVGQT--AENFEVQEMLKVARAEKDqlqlsctelrqEL 525
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN----ASSSLGSDlaAREDALNQSLKELMHQAR-----------TV 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 526 LKANGEIKHVSSLLAKME----KDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDmKETIFELEDQVEQHRAVKLH 601
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVQEEEQFL 834
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 71979930 602 NN-QLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEE 640
Cdd:TIGR00618 835 SRlEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
501-691 |
4.62e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 501 QEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKdysylkevcdhQAEQLSRTSLKLQEKASESDAEIKD 580
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-----------RIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 581 MKETIFELEDQVEQHRA------VKLHNNQLISELE--------GSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQA 646
Cdd:COG4942 88 LEKEIAELRAELEAQKEelaellRALYRLGRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 71979930 647 DLQTAVVVANDIKCEAQQELRTVKRRLLEEEEKNARLQKELGDIQ 691
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
282-612 |
6.25e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 282 NNASELSLASLTEKIQKMEENQHST--AEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQEN 359
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRlkKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 360 EKLInlLQERVKNEEPSAQGGKVLELEQKCTDILEKsrFEREKLLNIQQQLTCSLRKVEEENQgaidmikhLKEENEKLN 439
Cdd:pfam02463 812 EEAE--LLEEEQLLIEQEEKIKEEELEELALELKEE--QKLEKLAEEELERLEEEITKEELLQ--------ELLLKEEEL 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 440 GFLEHERcnnsvmAKTLEECRVTLEGLKMENGSLKALLEADKQKAIE---ASSTVGQTAENFEVQEMLKVARAEKDQLQL 516
Cdd:pfam02463 880 EEQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEeriKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 517 SCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHR 596
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEE----RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
330
....*....|....*.
gi 71979930 597 AVKLHNNQLISELEGS 612
Cdd:pfam02463 1030 NKGWNKVFFYLELGGS 1045
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
289-623 |
6.37e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLvdEKTILETSfHQHRERAEQLsqeNEKLINLLQE 368
Cdd:PRK04778 107 INEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYREL--RKSLLANR-FSFGPALDEL---EKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 369 RVKNEEPSAQGGKVleleqKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKH----LKEENEKLNGF--- 441
Cdd:PRK04778 181 FSQFVELTESGDYV-----EAREILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreLVEEGYHLDHLdie 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 442 -----LEHERCNNSVMAKTLE--ECRVTLEGLKMENGSLKALLEadkqKAIEASSTVGQTAEnfEVQEMLKVARAEKDQL 514
Cdd:PRK04778 256 keiqdLKEQIDENLALLEELDldEAEEKNEEIQERIDQLYDILE----REVKARKYVEKNSD--TLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 515 QLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLkLQEKASESDAEIKDMKETIFELEDQVEQ 594
Cdd:PRK04778 330 KEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSE-LQEELEEILKQLEEIEKEQEKLSEMLQG 408
|
330 340 350
....*....|....*....|....*....|.
gi 71979930 595 HRAVKLHNNQLISELEG--SVIKLEEQKSDL 623
Cdd:PRK04778 409 LRKDELEAREKLERYRNklHEIKRYLEKSNL 439
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
290-691 |
6.47e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 290 ASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQER 369
Cdd:TIGR00606 691 AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 370 VKneepsaQGGKVLELEQKCTDILEKsrfereklLNIQQQLTCSLRKVEEEnqgaidmIKHLKEENEKLNGFLEHERCNN 449
Cdd:TIGR00606 771 ET------LLGTIMPEEESAKVCLTD--------VTIMERFQMELKDVERK-------IAQQAAKLQGSDLDRTVQQVNQ 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 450 SVMAKTLEECRVTLEGLKMEngslKALLEADKQKAIEASSTVGQTAENFEVQEMLKVARAEKDQLQLSCTELrQELLKAN 529
Cdd:TIGR00606 830 EKQEKQHELDTVVSKIELNR----KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV-QSLIREI 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 530 GEIKHVSSLLAKMEKDYSYLKEVCDHQAEqlsrtslklqEKASESDAEIKDMKETIfeleDQVEQHRAVKLHNNQlisel 609
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKE----------TSNKKAQDKVNDIKEKV----KNIHGYMKDIENKIQ----- 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 610 EGSviklEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTavvVANDIKCEAQQE--------LRTVKRRLLEEEEKNA 681
Cdd:TIGR00606 966 DGK----DDYLKQKETELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELK 1038
|
410
....*....|
gi 71979930 682 RLQKELGDIQ 691
Cdd:TIGR00606 1039 QHLKEMGQMQ 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
289-692 |
9.94e-04 |
|
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: 43.13 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQH---STAEELQATLQELSDQQQMVQEltaENEKLVDEKTILETSFHQHRERAEQLSQENEKL--- 362
Cdd:TIGR02169 352 RDKLTEEYAELKEELEdlrAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEELADLnaa 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 363 -------INLLQERV--KNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCS-------------------- 413
Cdd:TIGR02169 429 iagieakINELEEEKedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqrelaeaeaqaraseervrg 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 414 ---------------------LRKVEEENQGAIDM--------------------IKHLKEENE---------------- 436
Cdd:TIGR02169 509 graveevlkasiqgvhgtvaqLGSVGERYATAIEVaagnrlnnvvveddavakeaIELLKRRKAgratflplnkmrderr 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 437 -----KLNGFL-------EHER---------CNNSVMAKTLEECR--------VTLEGL------KMENGSLKALLEADK 481
Cdd:TIGR02169 589 dlsilSEDGVIgfavdlvEFDPkyepafkyvFGDTLVVEDIEAARrlmgkyrmVTLEGElfeksgAMTGGSRAPRGGILF 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 482 QKAIEASSTVGQtAENFEVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLS 561
Cdd:TIGR02169 669 SRSEPAELQRLR-ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 562 RTSLKLQEKASESD---AEIKDMKETIFELEDQVEQHRAVKLHnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEET 638
Cdd:TIGR02169 748 SLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71979930 639 EEWRRFQADLQTAVVVANDIK------CEAQQELRTVKRRLLEEEEKNA----RLQKELGDIQG 692
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKeqiksiEKEIENLNGKKEELEEELEELEaalrDLESRLGDLKK 889
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
309-708 |
1.19e-03 |
|
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: 42.85 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 309 ELQATLQELSDQ-QQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQERVKNEEPSAQGGKVLE-LE 386
Cdd:pfam01576 226 ELQAQIAELRAQlAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEaLK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 387 QKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEEN----EKLNGFLEHERCNNSVMAKTleecrvt 462
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHtqalEELTEQLEQAKRNKANLEKA------- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 463 leglkmengslKALLEADKQKAIEASSTVGQTAEnfEVQEMLKVARAEKDQLQLSCTE---LRQELL----KANGEIKHV 535
Cdd:pfam01576 379 -----------KQALESENAELQAELRTLQQAKQ--DSEHKRKKLEGQLQELQARLSEserQRAELAeklsKLQSELESV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 536 SSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQE------KASESDAEIKDMKETIFE-LEDQVEQHRAVKLH----NNQ 604
Cdd:pfam01576 446 SSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEetrqklNLSTRLRQLEDERNSLQEqLEEEEEAKRNVERQlstlQAQ 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 605 L------ISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEW-------RRFQADLQTAVVvandikceAQQELRTVKR 671
Cdd:pfam01576 526 LsdmkkkLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLV--------DLDHQRQLVS 597
|
410 420 430
....*....|....*....|....*....|....*..
gi 71979930 672 RLleeEEKNARLQKELGDIQGHSRPVNEEPEPSEADA 708
Cdd:pfam01576 598 NL---EKKQKKFDQMLAEEKAISARYAEERDRAEAEA 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
499-686 |
1.38e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 499 EVQEMLKVARAEKDQLQlsctELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVcdHQAEQLSRTSLKLQEKASESDAEI 578
Cdd:COG4717 75 ELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKL--LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 579 KDMKETIFELEDQVEQhravklhnnqlISELEGSVIKLEEQKSDLERQLKTLT-KQIKEETEEWRRFQADLQTAvvvaND 657
Cdd:COG4717 149 EELEERLEELRELEEE-----------LEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAEL----EE 213
|
170 180
....*....|....*....|....*....
gi 71979930 658 IKCEAQQELRTVKRRLLEEEEKNARLQKE 686
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
499-648 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 499 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDysyLKEVCDH-QAEQLSR--TSLKLqekasesd 575
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNkEYEALQKeiESLKR-------- 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71979930 576 aEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADL 648
Cdd:COG1579 104 -RISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
296-636 |
1.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 296 IQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQERVKN--- 372
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEiee 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 373 -----EEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKVEEEnqgaidmikhlKEENEKLngfLEHERC 447
Cdd:PRK02224 389 leeeiEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER-----------VEEAEAL---LEAGKC 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 448 -------NNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQK------AIEASSTVGQTAENFE-VQEMLKVARAEKDQ 513
Cdd:PRK02224 455 pecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERleraedLVEAEDRIERLEERREdLEELIAERRETIEE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 514 LQLSCTELRQEL--LKANGEIKH------------VSSLLAKMEKDYSYLKEV----------------CDHQAEQLSRT 563
Cdd:PRK02224 535 KRERAEELRERAaeLEAEAEEKReaaaeaeeeaeeAREEVAELNSKLAELKERieslerirtllaaiadAEDEIERLREK 614
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71979930 564 SLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNN-----QLISELEGSVIKLEEQKSDLERQLKTLTKQIKE 636
Cdd:PRK02224 615 REALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDkeraeEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
282-685 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 282 NNASELSLASLTEKIQKMEENQHSTAEELQATLQELSDQqqmVQELTAENEKLVdektilETSFHQHRERAEQLSQENEK 361
Cdd:pfam15921 208 DSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQ---LEALKSESQNKI------ELLLQQHQDRIEQLISEHEV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 362 LINLLQERVKNEEPSAQggkvlELEQKCTDILEKSRFER-------EKLLNIQQQLTCSLR--------KVEEENQGAID 426
Cdd:pfam15921 279 EITGLTEKASSARSQAN-----SIQSQLEIIQEQARNQNsmymrqlSDLESTVSQLRSELReakrmyedKIEELEKQLVL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 427 MIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVGQTAE-NFEVQEMLK 505
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 506 VARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDH------QAEQLSRT------SLKLQEKASE 573
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltakkmTLESSERTvsdltaSLQEKERAIE 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 574 -SDAEIKDMKETIfELEDQVEQH-RAVKLHNNQLISELEGSVIKLEEQKSDLE---RQLKTLTKQIKEETEEWRRFQADL 648
Cdd:pfam15921 514 aTNAEITKLRSRV-DLKLQELQHlKNEGDHLRNVQTECEALKLQMAEKDKVIEilrQQIENMTQLVGQHGRTAGAMQVEK 592
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 71979930 649 QTAVVVANDIKCEAQQ-----ELRTVKRRLLEEEEKNARLQK 685
Cdd:pfam15921 593 AQLEKEINDRRLELQEfkilkDKKDAKIRELEARVSDLELEK 634
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
873-974 |
1.79e-03 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (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 anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A 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: 409161 Cd Length: 114 Bit Score: 39.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 873 SKRNALLKWCQKKtegYANIDITNFSSSWSDGLALCALLHTYLPAHIPyqELNSQEKKRNLLLAFEAAQS----VGInPS 948
Cdd:cd21312 12 TPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCP--DWDSWDASKPVTNAREAMQQaddwLGI-PQ 85
|
90 100
....*....|....*....|....*.
gi 71979930 949 LELSEMLYTDRPDWQSVMQYVAQIYK 974
Cdd:cd21312 86 VITPEEIVDPNVDEHSVMTYLSQFPK 111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
518-686 |
1.99e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 518 CTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEvcdhQAEQLSRtslkLQEKASESDAEIKDMKETIFELEDQVEQHRA 597
Cdd:PRK04863 899 IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQS----DPEQFEQ----LKQDYQQAQQTQRDAKQQAFALTEVVQRRAH 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 598 VKLHNNQ-LISELEGSVIKLEEQKSDLE---RQLKTLTKQIKEETEEWRRFQADLQTAVVVANDIKCEAQQELRTVKRRL 673
Cdd:PRK04863 971 FSYEDAAeMLAKNSDLNEKLRQRLEQAEqerTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
170
....*....|...
gi 71979930 674 LEEEEKNARLQKE 686
Cdd:PRK04863 1051 DSGAEERARARRD 1063
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
282-467 |
2.06e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 282 NNASELsLASLTEKIQKM------EENQHSTAEELQATLQElsdqqqMVQELTAENEKLVDEKTILETSFH-QHRE--RA 352
Cdd:pfam06160 259 DEAEEA-LEEIEERIDQLydllekEVDAKKYVEKNLPEIED------YLEHAEEQNKELKEELERVQQSYTlNENEleRV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 353 EQLSQENEKLI---NLLQERVKNEEP--SAQGGKVLELEQKCTDI-------------LEKSRFE-REKLLNIQQQLTCS 413
Cdd:pfam06160 332 RGLEKQLEELEkryDEIVERLEEKEVaySELQEELEEILEQLEEIeeeqeefkeslqsLRKDELEaREKLDEFKLELREI 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 71979930 414 LRKVEEEN-----QGAIDMIKHLKEENEKLNGFLEHERCNNSVMAKTLEECRVTLEGLK 467
Cdd:pfam06160 412 KRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLY 470
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
74-693 |
2.34e-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: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 74 KQEHEGAEKAVLESQVREL------LAEAKTKDSEINRLRSELK----KCKERWALSTEDANASDPSAEGTASP----ES 139
Cdd:TIGR00606 229 KEAQLESSREIVKSYENELdplknrLKEIEHNLSKIMKLDNEIKalksRKKQMEKDNSELELKMEKVFQGTDEQlndlYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 140 DAQPLIRTLEEKNKTFQKELADLEEENRALKEKLTYLEqspNSEGAASHTGDSSCPTSITHESSFGSpvgNELSSETDEY 219
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL---VEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 220 RrttHGSALRTSGSSSSDVTKASLSPDASDFEHITADTPSRPLSATSNPFK-SSKGSPTGSSPNNASELSLASLTEKIQK 298
Cdd:TIGR00606 383 E---RGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEiRDEKKGLGRTIELKKEILEKKQEELKFV 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 299 MEENQHSTA---------EELQATLQELS--DQQQMVQELTAENEKLVDEKTILETSFHQHRERAEQLSQENEKLINLLQ 367
Cdd:TIGR00606 460 IKELQQLEGssdrileldQELRKAERELSkaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEM 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 368 ERVKNEEPSAQGGKV-----LELEQKCTDILEKSRFER--EKLLNIQQQLTCSLRKVEEENQGAIDMIKHLKEENEKLng 440
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIksrhsDELTSLLGYFPNKKQLEDwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK-- 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 441 flehERCNNSVMAKTLEECRVTLEGLKMENGSlKALLEADKQKAIEASST-------VGQTAENFEVQEMLKVARAEKDQ 513
Cdd:TIGR00606 618 ----EEQLSSYEDKLFDVCGSQDEESDLERLK-EEIEKSSKQRAMLAGATavysqfiTQLTDENQSCCPVCQRVFQTEAE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 514 LQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQE---KASESDAEIKDMKETIFELED 590
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnKLQKVNRDIQRLKNDIEEQET 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 591 QVEQHRAvKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKeeteewrrfQADLQTAVVVANDIKCEAQQELRTV- 669
Cdd:TIGR00606 773 LLGTIMP-EEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVv 842
|
650 660 670
....*....|....*....|....*....|
gi 71979930 670 -----KRRLLEEEEKNAR-LQKELGDIQGH 693
Cdd:TIGR00606 843 skielNRKLIQDQQEQIQhLKSKTNELKSE 872
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
523-685 |
2.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 523 QELLKANGEIKhvsSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLqEKASESDAEIKDMKETIFELEDQVEqhravklhn 602
Cdd:PRK03918 182 EKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELE--------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 603 nqlisELEGSVIKLEEQKSDLERQLKTLTKQIKE-------------ETEEWRRFQADLQTAVVVANDIKCEA---QQEL 666
Cdd:PRK03918 249 -----SLEGSKRKLEEKIRELEERIEELKKEIEEleekvkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLsrlEEEI 323
|
170
....*....|....*....
gi 71979930 667 RTVKRRLLEEEEKNARLQK 685
Cdd:PRK03918 324 NGIEERIKELEEKEERLEE 342
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
289-699 |
2.78e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENqHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTILETSFHQHRERAEQLSQENEklinllQE 368
Cdd:PRK01156 314 LSNIDAEINKYHAI-IKKLSVLQKDYNDYIKKKSRYDDL----NNQILELEGYEMDYNSYLKSIESLKKKIE------EY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 369 RVKNEEPSAQGGKVLELEQKCTDILEKSRFE-REKLLNIQQQLTC------SLRKVEEENQGAIDMIK----------HL 431
Cdd:PRK01156 383 SKNIERMSAFISEILKIQEIDPDAIKKELNEiNVKLQDISSKVSSlnqrirALRENLDELSRNMEMLNgqsvcpvcgtTL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 432 KEEneKLNGFLEHERCNNSVMAKTLEECRVTLEGLKMENGSLKALLEADKQKAIEASSTVgqtaenfevQEMLKVARAEK 511
Cdd:PRK01156 463 GEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADL 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 512 DQLQLSCTELRQELLKANGEIKHVSSL-LAKMEKDY-SYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMKETIFELE 589
Cdd:PRK01156 532 EDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRtSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFP 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 590 DqveqhraVKLHNNQLISELEGSVIKLEEQKS---DLERQLKTLTKQI---KEETEEWRRFQADLQTAVVVANDIKCEAQ 663
Cdd:PRK01156 612 D-------DKSYIDKSIREIENEANNLNNKYNeiqENKILIEKLRGKIdnyKKQIAEIDSIIPDLKEITSRINDIEDNLK 684
|
410 420 430
....*....|....*....|....*....|....*.
gi 71979930 664 QELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNE 699
Cdd:PRK01156 685 KSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
499-700 |
3.09e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 499 EVQEMLKVARAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRT---SLKLQEKAS--- 572
Cdd:COG5022 786 LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKfgrSLKAKKRFSllk 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 573 ------ESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELegsVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQA 646
Cdd:COG5022 866 ketiylQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEI---IELKKSLSSDLIENLEFKTELIARLKKLLNNIDL 942
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 71979930 647 DLQTAV-VVANDIKceaqQELRTVKRRLLEEEEKNARLQKELGDIQGHSRPVNEE 700
Cdd:COG5022 943 EEGPSIeYVKLPEL----NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSE 993
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
569-687 |
3.98e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 569 EKASESDAEIKDMKETIFELEDQVEQHRavklhnnQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADL 648
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEE-------EEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*....
gi 71979930 649 QTAVVVANDIKcEAQQELRTVKRRLLEEEEKNARLQKEL 687
Cdd:COG2433 458 RREIRKDREIS-RLDREIERLERELEEERERIEELKRKL 495
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
292-500 |
3.99e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 292 LTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEKTILETSFHQHRE---RAEQLSQENEKLINLLQE 368
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEE 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 369 RVKNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQltcsLRKVEEENQGAIDMIKHLKEENEKLNGFLEHERCN 448
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE----LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 71979930 449 NSVMAKTLEECRVTLEGLKMENGSL--KALLEADKQKAIEASSTVGQTAENFEV 500
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
560-650 |
4.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 560 LSRTSLKLQEKASESDAEIKDMKETIFELEDQVEQHRAVKLHNNQLISELEGSVIKLEEQKSDLERQLKTLTKQIKEETE 639
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90
....*....|.
gi 71979930 640 EWRRFQADLQT 650
Cdd:COG4942 91 EIAELRAELEA 101
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
355-647 |
4.67e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 355 LSQENEKLINLLQERVKNEEPSAQGGKVLELEQKCTDiLEKSRFEREKLLniqQQLTCSLRKVEEENQGAIDMIKHLKEE 434
Cdd:pfam15905 48 STPATARKVKSLELKKKSQKNLKESKDQKELEKEIRA-LVQERGEQDKRL---QALEEELEKVEAKLNAAVREKTSLSAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 435 NEKLNGFL-EHERCNNSVMAKTLEE-CRVTLEGLKMENGSLKALLEAdKQKAIEASSTvGQTAENFEVQEMLKVARAEKD 512
Cdd:pfam15905 124 VASLEKQLlELTRVNELLKAKFSEDgTQKKMSSLSMELMKLRNKLEA-KMKEVMAKQE-GMEGKLQVTQKNLEHSKGKVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 513 QLQ--LSCTELR--------QELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKLQEKASESDAEIKDMK 582
Cdd:pfam15905 202 QLEekLVSTEKEkieeksetEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLN 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71979930 583 ETIFELEdqveqhravklhnnqliSELEGSVIKLEEQKSDLERQLKTLTKQIKEETEEWRRFQAD 647
Cdd:pfam15905 282 EKCKLLE-----------------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
264-656 |
5.04e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.71 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 264 ATSNPFKSSKGSPTGSSPNNASE--LSLASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELtaenEKLVDEKTIL 341
Cdd:COG5185 190 KGISELKKAEPSGTVNSIKESETgnLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKL----EKLVEQNTDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 342 ETS-FHQHRERAEQLSQENEKLINL---LQERVKNEEPSAQGGKVLELEQKCTDILEKSRFEREKLLNIQQQLTCSLRKV 417
Cdd:COG5185 266 RLEkLGENAESSKRLNENANNLIKQfenTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 418 EEENQGAIDMIKHLKEENEKLNGFLEHERcnnsvMAKTLEECRVTLEGLKMENGSLKAlleADKQKAIEASSTVGQTAEN 497
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSK-----SSEELDSFKDTIESTKESLDEIPQ---NQRGYAQEILATLEDTLKA 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 498 FEVQEmlkvaraekdqlqlscTELRQELLKANGEIKHVSSLLAKMEKDYSylKEVCDHQAEQLSRTSLKLQEKASESDAE 577
Cdd:COG5185 418 ADRQI----------------EELQRQIEQATSSNEEVSKLLNELISELN--KVMREADEESQSRLEEAYDEINRSVRSK 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71979930 578 IKDMKETIFELEDQVEQHRAvklhnnqliselegsviKLEEQKSDLERQLKTLTKQIKEETEEWRRFQADLQTAVVVAN 656
Cdd:COG5185 480 KEDLNEELTQIESRVSTLKA-----------------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
488-688 |
6.03e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 488 SSTVGQTAENFEVQEMLkvaRAEKDQLQLSCTELRQELLKANGEIKHVSSLLAKMEKDYSYLKEVCDHQAEQLSRTSLKL 567
Cdd:PRK04863 974 EDAAEMLAKNSDLNEKL---RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPA 1050
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 568 QEKASESDAEIKDmketifELEDQVEQHRAVKlhnNQLiselegsviklEEQKSDLERQLKTLTKQIKEETEEWRrfqaD 647
Cdd:PRK04863 1051 DSGAEERARARRD------ELHARLSANRSRR---NQL-----------EKQLTFCEAEMDNLTKKLRKLERDYH----E 1106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 71979930 648 LQTAVVVANDIKCEAQQELRT--VKRRLLEEE-------EKNARLQKELG 688
Cdd:PRK04863 1107 MREQVVNAKAGWCAVLRLVKDngVERRLHRRElaylsadELRSMSDKALG 1156
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
275-600 |
8.49e-03 |
|
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: 39.66 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 275 SPTGSSPNNASELSLAsLTEKIQKMEENQHSTAEELQATLQE---LS----DQQQMVQEL--TAE--NEKLVDEKTILET 343
Cdd:pfam15070 71 AEEEQPPAGPSEEEQR-LQEEAEQLQKELEALAGQLQAQVQDneqLSrlnqEQEQRLLELerAAErwGEQAEDRKQILED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 344 ----------SFHQHRERAEQL----------SQENEKLINLLQ--ERVKNE---------EPSAQGGKVLEL-EQKCTD 391
Cdd:pfam15070 150 mqsdratisrALSQNRELKEQLaelqngfvklTNENMELTSALQseQHVKKElakklgqlqEELGELKETLELkSQEAQS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 392 ILEksrfEREKLLNIQQQLTCSLRKVEEENqgaiDMIKHLKEENEKLNGFLEHERCNNSVMAKT----LEECRVTLEGLK 467
Cdd:pfam15070 230 LQE----QRDQYLAHLQQYVAAYQQLASEK----EELHKQYLLQTQLMDRLQHEEVQGKVAAEMarqeLQETQERLEALT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 468 MENGSLKALL-------EAD----KQKAIEASSTVGQTAENFEVQEMLK------VARAEKDQLQLS---------CTEL 521
Cdd:pfam15070 302 QQNQQLQAQLsllanpgEGDglesEEEEEEAPRPSLSIPEDFESREAMVaffnsaLAQAEEERAELRrqlkeqkrrCRRL 381
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71979930 522 RQELLKANGEIKHVSSllAKMEKDYSYLKEVcdHQAEQLSRTslKLQEKASESDAEIKDMKETIFELEdqveqHRAVKL 600
Cdd:pfam15070 382 AQQAAPAQEEPEHEAH--APGTGGDSVPVEV--HQALQVAME--KLQSRFTELMQEKADLKERVEELE-----HRCIQL 449
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
289-378 |
9.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 9.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71979930 289 LASLTEKIQKMEENQHSTAEELQATLQELSDQQQMVQELTAENEKLVDEktiLETSFHQHRERAEQLSQENEKLINLLQE 368
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIAR 231
|
90
....*....|
gi 71979930 369 RVKNEEPSAQ 378
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| |
