|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1005-1116 |
1.53e-81 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 260.76 E-value: 1.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 50949456 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
999-1117 |
9.58e-80 |
|
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: 256.15 E-value: 9.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 999 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQA 1078
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 50949456 1079 AESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET 1117
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1005-1116 |
6.81e-73 |
|
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: 236.85 E-value: 6.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1005 LAREYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGI 1084
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 50949456 1085 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1014-1115 |
3.09e-36 |
|
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: 132.47 E-value: 3.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINE 1092
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 50949456 1093 MVRTE-RPDWQNVMLYVTAIYKYF 1115
Cdd:cd21200 83 MVRMGnRPDWKCVFTYVQSLYRHL 106
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1012-1115 |
7.91e-35 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 128.63 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1012-1113 |
1.74e-32 |
|
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: 122.02 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKhADCPQLLDV 80
|
90 100
....*....|....*....|...
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYK 1113
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1017-1115 |
1.06e-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: 116.76 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRT 1096
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 50949456 1097 ERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1008-1115 |
1.61e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 116.47 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1008 EYGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQ-AAESVGIKS 1086
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 50949456 1087 TLDINEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1012-1115 |
1.20e-29 |
|
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: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGIAKLLD- 80
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
1014-1113 |
3.02e-29 |
|
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: 112.87 E-value: 3.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVG-IKSTLDINE 1092
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHAdCAPLLEVED 82
|
90 100
....*....|....*....|.
gi 50949456 1093 MVRTERPDWQNVMLYVTAIYK 1113
Cdd:cd21260 83 MVRMSVPDSKCVYTYIQELYR 103
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1012-1115 |
5.58e-29 |
|
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: 112.02 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
1015-1115 |
9.22e-29 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.22 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1015 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEM 1093
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGIPPVMTGQEM 82
|
90 100
....*....|....*....|..
gi 50949456 1094 VRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1016-1116 |
1.03e-28 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 110.90 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1016 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEMV 1094
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 50949456 1095 RTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
1012-1115 |
1.21e-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: 110.95 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEqKLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21248 81 PEDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
1012-1115 |
1.75e-28 |
|
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: 110.52 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMlADCVPLVEV 80
|
90 100
....*....|....*....|....*.
gi 50949456 1091 NE-MVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21258 81 EDmMIMGKKPDSKCVFTYVQSLYNHL 106
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1013-1115 |
8.44e-27 |
|
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: 105.70 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1013 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDIN 1091
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 50949456 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
1012-1116 |
1.93e-26 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 104.48 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDIN 1091
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGVPRLLEPA 80
|
90 100
....*....|....*....|....*
gi 50949456 1092 EMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21255 81 DMVLLPIPDKLIVMTYLCQLRAHFT 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1012-1115 |
1.97e-26 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 104.56 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQeLGISQLLDP 83
|
90 100
....*....|....*....|....*
gi 50949456 1091 nEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21249 84 -EDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
1012-1115 |
3.34e-26 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 103.89 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESV-GIKSTLDI 1090
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLaNCDRLIEV 80
|
90 100
....*....|....*....|....*.
gi 50949456 1091 NEM-VRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21261 81 EDMmVMGRKPDPMCVFTYVQSLYNHL 106
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
1017-1115 |
1.96e-25 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 101.85 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMVRT 1096
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGISRLLEPSDMVLL 85
|
90
....*....|....*....
gi 50949456 1097 ERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21254 86 AVPDKLTVMTYLYQIRAHF 104
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
1012-1115 |
3.82e-24 |
|
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: 97.85 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEkEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 50949456 1091 nEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21189 81 -EDVDVPEPDEKSIITYVSSLYDVF 104
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1014-1115 |
5.73e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 97.63 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINE 1092
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAEReLGIPALLDPED 81
|
90 100
....*....|....*....|...
gi 50949456 1093 MVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21252 82 MVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
1013-1115 |
6.16e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 97.64 E-value: 6.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1013 KRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDIN 1091
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAErEFGIPPVTTGK 84
|
90 100
....*....|....*....|....
gi 50949456 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21250 85 EMASAEEPDKLSMVMYLSKFYELF 108
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
1010-1116 |
1.86e-23 |
|
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: 96.26 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1010 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTL 1088
Cdd:cd21195 2 GDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAErEFGIPPVT 81
|
90 100
....*....|....*....|....*...
gi 50949456 1089 DINEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21195 82 TGKEMASAQEPDKLSMVMYLSKFYELFR 109
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
1017-1113 |
7.71e-23 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 94.03 E-value: 7.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAA-ESVGIKSTLDiNEMVR 1095
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGIEKLLD-PEDVN 83
|
90
....*....|....*...
gi 50949456 1096 TERPDWQNVMLYVTAIYK 1113
Cdd:cd21187 84 VEQPDKKSILMYVTSLFQ 101
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
1012-1115 |
1.44e-22 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 94.38 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21287 90 EDIVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
1012-1116 |
3.83e-22 |
|
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: 92.32 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDI 1090
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEkEFGISPIMTG 84
|
90 100
....*....|....*....|....*.
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21251 85 KEMASVGEPDKLSMVMYLTQFYEMFK 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1012-1115 |
1.92e-21 |
|
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: 90.89 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21321 5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEkELGLTKLLD- 83
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21321 84 PEDVNVDQPDEKSIITYVATYYHYF 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
1012-1115 |
2.99e-21 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 90.52 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKhLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21288 90 EDIVNTPKPDERAIMTYVSCFYHAF 114
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1012-1115 |
4.68e-21 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 90.11 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQhLGLTKLLD- 95
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21322 96 PEDVNMEAPDEKSIITYVVSFYHYF 120
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
1012-1115 |
5.27e-21 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 89.78 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKyLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21289 90 EDIVNTPKPDEKAIMTYVSCFYHAF 114
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1012-1115 |
7.01e-21 |
|
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: 88.95 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDIn 1091
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGVTRLLDA- 82
|
90 100
....*....|....*....|....
gi 50949456 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
1012-1115 |
1.43e-20 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 88.60 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDI 1090
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKyLDIPKMLDA 92
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21290 93 EDIVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
1011-1116 |
2.51e-20 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 87.09 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1011 GSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQhLNIPRLLE 81
|
90 100
....*....|....*....|....*..
gi 50949456 1090 InEMVRTERPDWQNVMLYVTAIYKYFE 1116
Cdd:cd21192 82 V-EDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1012-1115 |
7.22e-20 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 85.92 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQhLGLTKLLD- 80
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21320 81 PEDISVDHPDEKSIITYVVTYYHYF 105
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
1014-1117 |
3.91e-19 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 83.88 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1014 RNALLKWCQKKTEGY-QNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKSTL- 1088
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEkKLGVPKVLi 83
|
90 100 110
....*....|....*....|....*....|..
gi 50949456 1089 ---DINEmvrterPDWQNVMLYVTAIYKYFET 1117
Cdd:pfam00307 84 epeDLVE------GDNKSVLTYLASLFRRFQA 109
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
1016-1115 |
2.89e-18 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 80.97 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1016 ALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDINEmV 1094
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKkLGIPKLLEAED-V 82
|
90 100
....*....|....*....|.
gi 50949456 1095 RTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
1012-1115 |
2.91e-18 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 81.19 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDiN 1091
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLLD-P 79
|
90 100
....*....|....*....|....
gi 50949456 1092 EMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVF 103
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
1015-1108 |
2.38e-17 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 78.51 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1015 NALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY----QELNSQDKRRNFMLAFQAAESVGIKSTL-- 1088
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvaASLSRFKKIENINLALSFAEKLGGKVVLfe 80
|
90 100
....*....|....*....|..
gi 50949456 1089 --DINEMvrteRPDWQNVMLYV 1108
Cdd:smart00033 81 peDLVEG----PKLILGVIWTL 98
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
1014-1113 |
6.49e-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: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1014 RNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPY---QELNSQDKRRNFMLAFQAAESVGIKST--L 1088
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKinkKPKSPFKKRENINLFLNACKKLGLPELdlF 80
|
90 100
....*....|....*....|....*
gi 50949456 1089 DINEMVrtERPDWQNVMLYVTAIYK 1113
Cdd:cd00014 81 EPEDLY--EKGNLKKVLGTLWALAL 103
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
1010-1115 |
2.00e-16 |
|
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: 76.20 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1010 GGSKRnALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTL 1088
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGIPRLL 82
|
90 100
....*....|....*....|....*..
gi 50949456 1089 DiNEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21243 83 D-PEDVDVDKPDEKSIMTYVAQFLKKY 108
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
1012-1117 |
1.74e-15 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 81.14 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQN-IDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQ--DKRRNFMLAFQAAE-SVGIKST 1087
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLDLQkkNKALNNFQAFENANkVIGIARL 204
|
90 100 110
....*....|....*....|....*....|
gi 50949456 1088 LDINEMVRTERPDWQNVMLYVTAIYKYFET 1117
Cdd:COG5069 205 IGVEDIVNVSIPDERSIMTYVSWYIIRFGL 234
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
1012-1115 |
4.98e-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: 71.88 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQnidITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGIPKIIT 77
|
90 100
....*....|....*....|....*.
gi 50949456 1090 INEMVRTErPDWQNVMLYVTaiykYF 1115
Cdd:cd21184 78 PEDMVSPN-VDELSVMTYLS----YF 98
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
1017-1113 |
1.08e-14 |
|
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: 71.11 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKR-RNFMLAFQAAE-SVGIKSTLDiNEMV 1094
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARqHLGIEKLLD-PEDV 83
|
90
....*....|....*....
gi 50949456 1095 RTERPDWQNVMLYVTAIYK 1113
Cdd:cd21233 84 ATAHPDKKSILMYVTSLFQ 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-801 |
1.85e-13 |
|
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: 75.09 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 500 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 580 KAQLENEKQKVAELySIHNSGDKSDIQDLLESVRLDKEKAETL----------ASSLQEDLAHTRNDANRLQDAIAKVED 649
Cdd:TIGR02168 760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALrealdelraeLTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 650 EYRAFQEEAKK----------QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVK 719
Cdd:TIGR02168 839 RLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 720 KLQDQKHDMER-------EIKTLHRRLREEsaewrqFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:TIGR02168 919 ELREKLAQLELrleglevRIDNLQERLSEE------YSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAI 992
|
330
....*....|..
gi 50949456 790 KELEEIKSRKQE 801
Cdd:TIGR02168 993 EEYEELKERYDF 1004
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
1012-1112 |
3.03e-13 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 66.97 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAE-SVGIKSTLDi 1090
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLD- 80
|
90 100
....*....|....*....|..
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIY 1112
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-804 |
4.03e-13 |
|
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: 73.94 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 202 LRNELRDMRAQLGINEDHSEGDEKSEKETI---MAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGfSL 278
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEElkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-NE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 279 EQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSApgsvEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTS 358
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 359 SDDALDAPSSSESEGI---------LSIERSRKGSSGNASEVSVACLTERIHQMEENQHSTseELQATLQELADLQQITQ 429
Cdd:TIGR02168 373 RLEELEEQLETLRSKVaqlelqiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 430 ELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvidedvksgrYMELEQRYMDLAENARF---ER 506
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS---------------LERLQENLEGFSEGVKAllkNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGA-----LKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKA 581
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 582 QLENEKQKVAELYSIHNSGDKSdIQDLLESVR-----------LDKEKAETLASSLQEDLAH------------------ 632
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKA-LSYLLGGVLvvddldnalelAKKLRPGYRIVTLDGDLVRpggvitggsaktnssile 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 633 TRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNL 709
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 710 IISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEEAANLRERLESLE 830
|
650
....*....|....*
gi 50949456 790 KELEEIKSRKQEEER 804
Cdd:TIGR02168 831 RRIAATERRLEDLEE 845
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
528-803 |
9.21e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 528 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdksdiqd 607
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 608 lLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMK 687
Cdd:COG1196 304 -IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 688 ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEA 767
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 50949456 768 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
1010-1099 |
1.19e-12 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 65.45 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1010 GGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTL 1088
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENeLGITPVV 80
|
90
....*....|.
gi 50949456 1089 DINEMVRTERP 1099
Cdd:cd21196 81 SAQAVVAGSDP 91
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
604-799 |
1.49e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 604 DIQDLLESVRLDKEKAETLA--SSLQEDLAHTRNDANRLQDAIAKVEDeYRAFQ--EEAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRL-WFAQRrlELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 680 ETERSDMKETIFELEDEVEQHravklhDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLR-------EESAEWRQFQAD 752
Cdd:COG4913 315 EARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50949456 753 LQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
1012-1115 |
1.66e-12 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 64.86 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDi 1090
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQeLKIPRLLE- 83
|
90 100
....*....|....*....|....*
gi 50949456 1091 NEMVRTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVAQFLQYS 108
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
1017-1113 |
1.92e-12 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 64.59 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAES-VGIKSTLDiNEMVR 1095
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNhLGIEKLLD-PEDVA 83
|
90
....*....|....*...
gi 50949456 1096 TERPDWQNVMLYVTAIYK 1113
Cdd:cd21234 84 VQLPDKKSIIMYLTSLFE 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
505-815 |
3.41e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 505 EREQLLGVQQHLSNTLKMAEQDNKEAQEMIG--------------ALKERSHHMERIIESEQKGKAA-------LAATLE 563
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieqleqeeeKLKERLEELEEDLSSLEQEIENvkselkeLEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 564 EYKATVASDQIEMNRLKA--------QLENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEArlshsripEIQAELSKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 636 DANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnLIIS 712
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEEleaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-------KRLS 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 713 DLENTVKKLQDQkhdmEREIKTLHRRLREESAEW---RQFQADLQ---TAVVIANDIKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:TIGR02169 921 ELKAKLEALEEE----LSEIEDPKGEDEEIPEEElslEDVQAELQrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
330 340
....*....|....*....|....*....
gi 50949456 787 KLTKELEEIKSRKQEEERGRVYNYMNAVE 815
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREVFMEAFE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-804 |
4.71e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 551 EQKGKA----ALAATLEEYKATVASDQIEmnRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:COG1196 207 RQAEKAeryrELKEELKELEAELLLLKLR--ELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 627 QE---DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAv 703
Cdd:COG1196 277 EElelELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 704 klhdnliisDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQE 783
Cdd:COG1196 352 ---------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260
....*....|....*....|.
gi 50949456 784 KNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEA 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-821 |
5.25e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 567 ATVASDQIEMNRLKAQLENEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQD 642
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIID--EKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 643 AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDM--------KETIFELEDEVEQHRAVKLHDNLIISDL 714
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 715 ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|....*....
gi 50949456 792 LEEIK---------SRKQEEERGRVYNYMNAVERDLAAL 821
Cdd:TIGR02169 401 INELKreldrlqeeLQRLSEELADLNAAIAGIEAKINEL 439
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
1015-1108 |
1.16e-11 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 63.47 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1015 NALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQ--------------------------------E 1062
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDairqpttqtvdraqdeaedfwvaefspstgdsG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 50949456 1063 LNSQDK---RRNFMLAFQAAESVGikstlDINEMVRTE-----RPDWQNVMLYV 1108
Cdd:cd21224 82 LSSELLaneKRNFKLVQQAVAELG-----GVPALLRASdmsntIPDEKVVILFL 130
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
1016-1115 |
1.37e-11 |
|
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: 62.12 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1016 ALLKWCQKKTEGYqNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAA-ESVGIKSTLDiNEMV 1094
Cdd:cd21245 7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGIPPLLE-PEDV 84
|
90 100
....*....|....*....|.
gi 50949456 1095 RTERPDWQNVMLYVTAIYKYF 1115
Cdd:cd21245 85 MVDSPDEQSIMTYVAQFLEHF 105
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1015-1110 |
5.49e-11 |
|
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: 60.01 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1015 NALLKWCQKKTegyQNIDITNFSSSWNDGLAFCALLHTyLPAHIP-YQELNSQDKRRNFMLAFQAAESVGIKSTLDINEM 1093
Cdd:cd21185 4 KATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVLTAEEM 79
|
90
....*....|....*....
gi 50949456 1094 VrteRPDWQN--VMLYVTA 1110
Cdd:cd21185 80 A---DPEVEHlgIMAYAAQ 95
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
398-825 |
2.24e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 398 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHhiSY 477
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 478 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 553
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 554 GKAALAATLEEYKatvasdqiEMNRLKAQLENEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:PRK03918 353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 634 RNDANRLQDAIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERS------- 684
Cdd:PRK03918 418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 685 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:PRK03918 498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 738 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 799
Cdd:PRK03918 578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
|
490 500
....*....|....*....|....*.
gi 50949456 800 QEEERGRVYNYMNAVERDLAALRQGM 825
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAEL 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
529-804 |
4.11e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 529 EAQEMIGALK-ERSHHMERIIESEQKGKAALAAtLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSihnsgDKSDIQD 607
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-----DLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 608 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIA-----KVEDEYRAFQEEAKKQ----------IEDLNMTLEKL 672
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 673 RSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQAD 752
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 753 LQTAVVIANDIK---SEAQEEIGDLKRRLHEAQEKNEKlTKELEEIKSRKQEEER 804
Cdd:TIGR02169 912 IEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-822 |
5.37e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhi 475
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 476 syviDEDVKSGrymELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALK--------ERSHHMERI 547
Cdd:PRK02224 402 ----DAPVDLG---NAEDFLEELRE----ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 548 IESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaelysihnsgdksdiqdlLESVRLDKEKAETLASSLQ 627
Cdd:PRK02224 471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------------------IERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 628 EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLnmtlEKLRSDLDEKETERSDMKETIFELEDEVEQHRAvklhd 707
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA----- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 708 nliISDLENTVKKLQDQKHDMErEIKTLHR-RLREESAEWRQFQADLQTAvviandikseaqeeigdlkrRLHEAQEKNE 786
Cdd:PRK02224 601 ---IADAEDEIERLREKREALA-ELNDERReRLAEKRERKRELEAEFDEA--------------------RIEEAREDKE 656
|
410 420 430
....*....|....*....|....*....|....*...
gi 50949456 787 KLTKELEEI--KSRKQEEERGRVYNYMNAVERDLAALR 822
Cdd:PRK02224 657 RAEEYLEQVeeKLDELREERDDLQAEIGAVENELEELE 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
613-823 |
6.50e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 613 RLDKEKAETLasslqEDLAHTRNDANRLQDAIAKVED-------------EYRAFQEEAKK--------QIEDLNMTLEK 671
Cdd:COG1196 169 KYKERKEEAE-----RKLEATEENLERLEDILGELERqleplerqaekaeRYRELKEELKEleaellllKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 672 LRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQA 751
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50949456 752 DLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQ 823
Cdd:COG1196 324 ELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAE 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-804 |
1.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 609 LESVRLDKEKAE---TLASSLQE--------DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLD 677
Cdd:COG1196 202 LEPLERQAEKAEryrELKEELKEleaellllKLRELEAELEELEAELEELEAE----LEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 678 EKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50949456 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
669-806 |
1.33e-09 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 62.18 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQ 748
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEE---------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949456 749 FQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:COG2433 453 ARSEERREIRKDREISRL-DREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-824 |
1.39e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQITQELNSENERLGEEKvilmeslcqqsdklehfsRQIEYFRSLLDEHhisyvidEDVksgRYMEL 491
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRER------------------EKAERYQALLKEK-------REY---EGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 492 EQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQkgkAALAATLEEYKATVAS 571
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 572 --DQIEMNRLKAQ-LENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:TIGR02169 306 leRSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 649 DEYRAFQEEakkqiedlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDM 728
Cdd:TIGR02169 385 DELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 729 EREIKTLHRRLREESAewrqfqadlqtavviandIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVY 808
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAA------------------DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410
....*....|....*.
gi 50949456 809 NYmnAVERDLAALRQG 824
Cdd:TIGR02169 509 GR--AVEEVLKASIQG 522
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
387-797 |
2.00e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVIL---MESLCQQSDKLEHFSRQI 463
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 464 EYFRSLLDehhiSYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHH 543
Cdd:TIGR04523 200 ELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 544 MERI---IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYS-IHNSGDK-SDIQDLLESVRLDKEK 618
Cdd:TIGR04523 276 LEQNnkkIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNqISQNNKIiSQLNEQISQLKKELTN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 619 AETLASSLQEDLahtrndaNRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELED 695
Cdd:TIGR04523 354 SESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 696 EVEQHRAVKLHDNLIISDLEN-------TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQ 768
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430
....*....|....*....|....*....|..
gi 50949456 769 ---EEIGDLKRRLHEAQEKNEKLTKELEEIKS 797
Cdd:TIGR04523 507 eleEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
387-822 |
2.34e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 387 NASEVSVACLTERIHQMEENQhstsEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYF 466
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 467 RSLLDEHhisyvidEDVKSGRYMELEQRYMDlAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 546
Cdd:PRK02224 285 RERLEEL-------EEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 547 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-----PVDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 627 QEDLAHTRND---ANRLQDA--------------IAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLD------EKETER 683
Cdd:PRK02224 432 EATLRTARERveeAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 684 SDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQADLQTAVVIA 760
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeeAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 761 NDIKS------EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE--------------EERGRVYNYMNAVERDLAA 820
Cdd:PRK02224 592 ERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKREleaefdearieearEDKERAEEYLEQVEEKLDE 671
|
..
gi 50949456 821 LR 822
Cdd:PRK02224 672 LR 673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
387-700 |
2.82e-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: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYF 466
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 467 RSLLDEHHISY---VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSntlKMAEQDNKEAQEMIGALKERSHH 543
Cdd:TIGR02168 809 RAELTLLNEEAanlRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE---ELEELIEELESELEALLNERASL 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 544 mERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVR----LDKEKA 619
Cdd:TIGR02168 886 -EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL--------EVRIDNLQERLSeeysLTLEEA 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 620 ETLASSLQEDLAHTRNDANRLQDAIAK-------VEDEYRAFQE---EAKKQIEDLNMTLEKLRSDLDEKETErsdMKET 689
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKErydFLTAQKEDLTEAKETLEEAIEEIDRE---ARER 1033
|
330
....*....|.
gi 50949456 690 IFELEDEVEQH 700
Cdd:TIGR02168 1034 FKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-829 |
4.93e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 630 LAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---------------------QIEDLNMTLEKLRSDLDEKETERSDMKE 688
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 689 TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTA---VVIANDIKS 765
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELA 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50949456 766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGrvynyMNAVERDLAALRQGMGLSR 829
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLN 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
405-803 |
9.32e-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: 59.69 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 405 ENQHSTSEELQATLQELADLQQITQELNSEnerlgeekvilMESLCQQSDKLEHFsrqIEYfRSLLDEHHISYVIDedvk 484
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERY---KEL-KAELRELELALLVL---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 485 sgRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:TIGR02168 233 --RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 565 YKATVASDQIEMNRLKAQLENEKQKvaelysihnsgdksdiqdllesvrldKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESK--------------------------LDELAEELAELEEKLEELKEELESLEAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 645 akveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQhravklhdnliisdLENTVKKLQDQ 724
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--------------LEDRRERLQQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 725 KHDMEREIKTLHRR-LREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR02168 423 IEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-808 |
9.51e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEdvKSGRYMEL 491
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE--LPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 492 EQRYMDLAEnARFEREQLLGVQQHLSNTLKMAEQDNKEA--QEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATV 569
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEE-LEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 570 asDQIEMNRLKAQLENEKQKVAELYSIHN-----SGDKSDIQDLLESV--------------RLDKEKAETLASSLQEDL 630
Cdd:COG4717 230 --EQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 631 AHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKEtifeleDEVEQHRAVKLHDNLI 710
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL------EELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 711 IS--DLENTVKKLQdQKHDMEREIKTLHRRLREESAEWRQFQADLQtavviandiKSEAQEEIGDLKRRLHEAQEKNEKL 788
Cdd:COG4717 382 EDeeELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
|
410 420
....*....|....*....|
gi 50949456 789 TKELEEIKSRKQEEERGRVY 808
Cdd:COG4717 452 REELAELEAELEQLEEDGEL 471
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
390-816 |
1.43e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 390 EVSVACLTERIHQMEENQHSTSEELQATLQELADLQQItQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSL 469
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 470 LDEhhisyvIDEDVK-----SGRYMELEQRYMDLAENAR-FEREQLLGVQ-------------QHLSNTLKMAEQDNKEA 530
Cdd:PRK03918 330 IKE------LEEKEErleelKKKLKELEKRLEELEERHElYEEAKAKKEElerlkkrltgltpEKLEKELEELEKAKEEI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 531 QEMIGALKERSHHMERIIES---------EQKGKAAL----------AATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:PRK03918 404 EEEISKITARIGELKKEIKElkkaieelkKAKGKCPVcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 592 ELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqIEDLNMTLEK 671
Cdd:PRK03918 484 ELEKVLK--KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 672 LRSDLDEKETERSDMKETI----FELEDEVEQ---------HRAVKLHDnlIISDLENTVKKLQDQKHDMEREIKTL--- 735
Cdd:PRK03918 561 LEKKLDELEEELAELLKELeelgFESVEELEErlkelepfyNEYLELKD--AEKELEREEKELKKLEEELDKAFEELaet 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 736 ----------------------HRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLtkELE 793
Cdd:PRK03918 639 ekrleelrkeleelekkyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL--EKL 716
|
490 500
....*....|....*....|...
gi 50949456 794 EIKSRKQEEERGRVYNYMNAVER 816
Cdd:PRK03918 717 EKALERVEELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-699 |
1.64e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESlcqqsdKLEHFSRQIEYF 466
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE------KIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 467 RSLLDehhisyvidedvksgrymELEQRYMDLAENARfereqllgvqqhlsntlkmaeqdnkEAQEMIGALKERSHHMER 546
Cdd:TIGR02169 307 ERSIA------------------EKERELEDAEERLA-------------------------KLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 547 IIESEQKGKAALaatleeyKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDK--SDIQDLLESVRLDKEKAETLAS 624
Cdd:TIGR02169 344 EIEEERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQ 699
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-823 |
2.29e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLENEKQKVAELYSIHNSGD--KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAkvedEYR 652
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 653 AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEV---------------EQHRAVKLHDNLI------I 711
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleaeleeleaeleELESRLEELEEQLetlrskV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 712 SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 50949456 792 LEEIKSRKQEEERGRVynymnAVERDLAALRQ 823
Cdd:TIGR02168 463 LEELREELEEAEQALD-----AAERELAQLQA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
620-823 |
2.53e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 620 ETLASSLQEDLAH---TRNDANRLQDAIAKVEDEYRAFQEEakkqIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE 696
Cdd:PRK02224 212 ESELAELDEEIERyeeQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 697 VEQHRAvKLHDNLIISDLEN-TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE------ 769
Cdd:PRK02224 288 LEELEE-ERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaa 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 770 ----EIGDLKRRLHEAQEKNEKLTKELEEIKSR--KQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:PRK02224 367 elesELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRE 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
399-778 |
2.57e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 399 RIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmeslcqqsdKLEHFSRQIEYfrslldehhisyv 478
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----------------RLELEELELEL------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 479 ideDVKSGRYMELEQRYMDLAENARFEREQLlgvqQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAAL 558
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 559 AATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN 638
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 639 RLQDAIA--KVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE- 715
Cdd:COG1196 426 LEEALAEleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEg 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 716 -NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVV-IANDIKSEAQEEIGDLKRRL 778
Cdd:COG1196 506 fLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnIVVEDDEVAAAAIEYLKAAK 570
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
1012-1109 |
6.25e-08 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 51.61 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1012 SKRNALLKWCQKKTEGyqnIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAES-VGIKSTLD 1089
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAEDwLGVPQLIT 77
|
90 100
....*....|....*....|
gi 50949456 1090 INEMVrTERPDWQNVMLYVT 1109
Cdd:cd21230 78 PEEII-NPNVDEMSVMTYLS 96
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
649-803 |
6.68e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 649 DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQK--H 726
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVRNNKeyE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 727 DMEREIKTLHRRlreesaewrqfQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1579 93 ALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-802 |
2.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 397 TERIHQMEENQHSTSEELQATLQELADLQQITQELN--SENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhh 474
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 475 iSYVIDEDVKSGRYmELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKG 554
Cdd:COG4717 165 -LEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 555 K-----------AALAATLEEYKATVASDQIE------------------MNRLKAQLENEKQKVAELYSIHNsGDKSDI 605
Cdd:COG4717 243 ErlkearlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEE-LEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSD 685
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 686 MKETIFELEDEVEQHR--AVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADlqtavvianDI 763
Cdd:COG4717 400 LKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED---------GE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 50949456 764 KSEAQEEIGDLKRRLHEAQEKN-------EKLTKELEEIKSRKQEE 802
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPP 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-696 |
3.80e-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: 54.69 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 399 RIHQMEENQHSTSEE-------LQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL-EHFSRQIEYFRSLL 470
Cdd:TIGR02169 724 EIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 471 DEHHISYvidedvkSGRYMELEQRymdlaENARFEREQLLgvqqhlsntlkmaEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:TIGR02169 804 EEEVSRI-------EARLREIEQK-----LNRLTLEKEYL-------------EKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 551 EQKGKAALAATLEEYKATV-------ASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLA 623
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALrdlesrlGDLKKERDELEAQLRELERKIEEL--------EAQIEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 624 SSLQEDLAHTRN---------DANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLrSDLDEK----ETERSDMKETI 690
Cdd:TIGR02169 931 EELSEIEDPKGEdeeipeeelSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKraklEEERKAILERI 1009
|
....*.
gi 50949456 691 FELEDE 696
Cdd:TIGR02169 1010 EEYEKK 1015
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
575-809 |
4.60e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKaqleneKQKVAELYSihnsgdksDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI---AKVEDEY 651
Cdd:PHA02562 167 EMDKLN------KDKIRELNQ--------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYdelVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 652 RAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR----------AVKLHDNLI------ISDLE 715
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqQISEGPDRItkikdkLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 716 NTVKKLQDQKHDMER---EIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSE---AQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:PHA02562 313 HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 50949456 790 KELEEIKsrKQEEERGRVYN 809
Cdd:PHA02562 393 KTKSELV--KEKYHRGIVTD 410
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
396-801 |
5.28e-07 |
|
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: 53.96 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 457
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 458 HFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 524
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 525 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLENEKQKVAELYSIHNsgdksd 604
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 605 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKEte 682
Cdd:pfam05483 496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-- 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 683 rSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:pfam05483 573 -ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
410 420 430
....*....|....*....|....*....|....*....
gi 50949456 763 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-804 |
5.36e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 521 KMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATvASDQIEMNRLKAQLENEKQKVAELYSIHNSG 600
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 601 DKSDIQDLLESVRLDKE--KAETLASSLQEDLAHTRNDANRLQDA--IAKVEDEYRAfqEEAKKQIEDLNMTLEKlRSDL 676
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKA--EEAKKAEEDKNMALRK-AEEA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 677 DEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADL 753
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50949456 754 QTAVVIANDIKSEAQEEIGDlKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
396-838 |
6.65e-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: 53.97 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSE--ELQATL-----QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRS 468
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNEsnELHEKQkfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 469 LldehhisyviDEDVKSGRYMELEQ-RYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMiGALKERSHHMERI 547
Cdd:pfam15921 160 L----------KEDMLEDSNTQIEQlRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHF-RSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 548 IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYSIHnsgdKSDIQDLLESVRLDKEKAETLASSLQ 627
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEALKSES--QNKIELLLQQHQDRIEQLISEH----EVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 628 EDLAHTRND-------ANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQH 700
Cdd:pfam15921 303 IIQEQARNQnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 701 RAvKLHDNLIISDLENTV-KKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviandIKSEAQeeiGDLKRRLH 779
Cdd:pfam15921 383 LA-DLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA-------MKSECQ---GQMERQMA 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 780 EAQEKNE------KLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGMGLSRRS--STSSEPT 838
Cdd:pfam15921 452 AIQGKNEslekvsSLTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAieATNAEIT 520
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-895 |
7.63e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 699 QH-RAVKLHDNLI-----------ISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI 763
Cdd:COG3883 90 ERaRALYRSGGSVsyldvllgsesFSDFldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynymNAVERDLAALRQGMGLSRRSSTSSEPTPTVKT 843
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA-------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 50949456 844 LIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-764 |
7.98e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 499 AENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKErshhMERIIESEQKGKAALAATLEEYKATVASDQIEMNR 578
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 579 LKAQLENEKQKVAE-LYSIHNSGDKSDIQDLLEsvrldkekaetlasslQEDLahtrNDANRLQDAiakvedeYRAFQEE 657
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLS----------------PEDF----LDAVRRLQY-------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|....*..
gi 50949456 738 RLREESAEWRQFQADLQTAVVIANDIK 764
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-791 |
1.04e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 359 SDDALDAPSSSESEGILSIERSRKgssgnASEVSVACLTERIHQMEENQHSTSEEL----QATLQELADLQQITQELNSE 434
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKK-----AEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 435 NERLGEEKVILMESLcqqsDKLEHFSRQIEYFRSLLDEHHISYvidEDVKSgrymELEQRYMDLAENARFEREQllgvqQ 514
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKA---EELKK----AEEENKIKAAEEAKKAEED-----K 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 515 HLSNTLKMAEQDNKEAQEMIGALKERSHHMERI--IESEQKGKAalaatlEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkKEAEEKKKA------EELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 593 LYSihNSGDKSDIQDLLE-----SVRLDKEKAETLASSLQEDLAHTRNDANRlqdAIAKVEDEYRAFQEEAKKQIEDLNm 667
Cdd:PTZ00121 1749 AKK--DEEEKKKIAHLKKeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIN- 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 668 tleklrsdlDEKETERSDMKE------TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIktlhrrlrE 741
Cdd:PTZ00121 1823 ---------DSKEMEDSAIKEvadsknMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI--------E 1885
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 742 ESAEWRQFQADLQTAVVIANDIKSEAQEEIGD-------LKRRLHEAQEKNEKLTKE 791
Cdd:PTZ00121 1886 EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDkldkdeyIKRDAEETREEIIKISKK 1942
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
1017-1094 |
1.09e-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: 48.45 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWCQK--KTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIP----YQELNSQDKRRNFMLAFQAAESVGIKSTLDI 1090
Cdd:cd21218 15 LLRWVNYhlKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLGCKYFLTP 94
|
....
gi 50949456 1091 NEMV 1094
Cdd:cd21218 95 EDIV 98
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
602-803 |
1.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 602 KSDIQDLLESVRLDK--EKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEeAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4717 36 KSTLLAFIRAMLLERleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 680 ETERSDMKETI--FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4717 115 REELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50949456 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
378-690 |
1.16e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.82 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 378 ERSRKGSSGNASEVsvacltERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLG-EEKVILMESLCQQSDKL 456
Cdd:pfam17380 299 ERLRQEKEEKAREV------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 457 EhFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaENARFEREQLLGVQQhlsntlKMAEQDNKEAQEMIGA 536
Cdd:pfam17380 373 E-ISRMRELERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQ------IRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 537 LKERSHHMERIIESEQKGKAALaatleeykATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDK 616
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 617 EKAETLASSLQEdlahtRNDANRLQDAIAKVEDEYRAFQE-EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam17380 513 RKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-823 |
1.34e-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: 52.07 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 699 QHRavklhdnliisdlentvKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIA---NDIKSEAQEEIGDLK 775
Cdd:COG4942 94 ELR-----------------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylKYLAPARREQAEELR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 50949456 776 RRLHEAQEKNEKLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:COG4942 157 ADLAELAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEK 206
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
504-836 |
1.61e-06 |
|
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: 52.27 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 504 FEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMERIIESEQKGKAaLAATLEEYKATV-ASDQIEMNRLK 580
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIinIEEALKGFQDPESELED-LAQTSDKLEKLVeQNTDLRLEKLG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 581 AQLENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQ-EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK 659
Cdd:COG5185 272 ENAESSKRLNEN-----ANNLIKQFENTKEKIAEYTKSIDIKKATESlEEQLAAAEAEQELEESKRETETGIQNLTAEIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 660 KQIEDLNMTLEKLRSDLDEKETER--SDMKETIFELEDEVE--------QHRAVKLHDNLIISDLENTVKKLQDQKHDME 729
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVelSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 730 REIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRlhEAQEKNEKLTKELEEIKSRKQeEERGRVYN 809
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR--SVRSKKEDLNEELTQIESRVS-TLKATLEK 503
|
330 340
....*....|....*....|....*..
gi 50949456 810 YMNAVERDLAALRQGMGLSRRSSTSSE 836
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFM 530
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
415-792 |
1.65e-06 |
|
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: 52.28 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 415 QATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDE---------DVKS 485
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 486 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHM---ERIIESEQKGKAALAATL 562
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkEQIHLQETRKKAVVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 563 EEYK---------------ATVASDQIEMN-RLKAQLENEKQKVAElysihnSGDKSD--IQDLLESVRLDKEKAETLAS 624
Cdd:TIGR00618 497 LELQeepcplcgscihpnpARQDIDNPGPLtRRMQRGEQTYAQLET------SEEDVYhqLTSERKQRASLKEQMQEIQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 625 SLQ----------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKE------ 688
Cdd:TIGR00618 571 SFSiltqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalha 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 689 TIFEL--EDEVEQHRAVKLHDNLIISDLENTVKKLQDQK-----------------HDMEREIKTLHRRLREESAEWRQF 749
Cdd:TIGR00618 651 LQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtllRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 50949456 750 QADLQTAVVIANDIKSEAQEEIGD-LKRRLHEAQEKNEKLTKEL 792
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAAL 774
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
570-798 |
2.85e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 570 ASDQIEmnRLKAQLENEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLahtrnDANRLQDAIAKVED 649
Cdd:COG4913 608 NRAKLA--ALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 650 EYRAFQ------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV-----------------KLH 706
Cdd:COG4913 676 ELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelralleERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 707 DNLIISDLENTVKK-LQDQKHDMEREIKTLHRRLREE----SAEWRQFQADLQTAV-----------VIANDIKSEAQEE 770
Cdd:COG4913 756 AAALGDAVERELREnLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLeslpeylalldRLEEDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 50949456 771 igdLKRRLHEAQEK-----NEKLTKELEEIKSR 798
Cdd:COG4913 836 ---FKELLNENSIEfvadlLSKLRRAIREIKER 865
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
375-822 |
3.47e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 375 LSIERSRKGSSGNASEVSVACLTERIHQM-EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQS 453
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 454 DKLEHFSRQIEYFRSLLDEHHISYVIDEDVksgrYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEM 533
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 534 IGALKERSHHMERI---IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaELYSIHNsgDKSDIQDLLE 610
Cdd:TIGR02169 412 QEELQRLSEELADLnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE--EYDRVEKELS 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 611 SVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI----------AKVEDEYRAFQE----------------EAKKQIED 664
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlGSVGERYATAIEvaagnrlnnvvveddaVAKEAIEL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 665 LN------MT---LEKLRSDldEKETERSDMKETIFELEDEVE---QHRAV---KLHDNLIISDLENT------------ 717
Cdd:TIGR02169 567 LKrrkagrATflpLNKMRDE--RRDLSILSEDGVIGFAVDLVEfdpKYEPAfkyVFGDTLVVEDIEAArrlmgkyrmvtl 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 718 -------------------------------VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLqtavviandikSE 766
Cdd:TIGR02169 645 egelfeksgamtggsraprggilfsrsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-----------SD 713
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 50949456 767 AQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALR 822
Cdd:TIGR02169 714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-----ENVKSELKELE 764
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-804 |
4.62e-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: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 601 DKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLD 677
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 678 EKETERSDMKETIFELEdeveQHRAVKLHdnLIISDLENTVKKLQDQKHdMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4942 101 AQKEELAELLRALYRLG----RQPPLALL--LSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 50949456 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
202-822 |
7.80e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.22 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 202 LRNELRDMRAQLGINEDHSEGDEKSEKETIMA--HQPTDVESTLLQLQ----EQNTAIREELNQLKNENRMLKDRLNALg 275
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAADAAVAKdrSELEALEDQHGAFLdadiETAAADQEQLPSWQSELENLEERLKAL- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 276 fsLEQRLDNSEKlfgYQSLSPEITPGNQSDGGGT---LTSSVEGSAPG--SVEDLLSQDENTLmDHQHSNSMDNLDSECS 350
Cdd:pfam12128 367 --TGKHQDVTAK---YNRRRSKIKEQNNRDIAGIkdkLAKIREARDRQlaVAEDDLQALESEL-REQLEAGKLEFNEEEY 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 351 EVYQPLTSSDDALDAPSSSEsEGILSIERSrkgssgnasevsvaclTERIHQMEENQHS--------TSEELQA-TLQEL 421
Cdd:pfam12128 441 RLKSRLGELKLRLNQATATP-ELLLQLENF----------------DERIERAREEQEAanaeverlQSELRQArKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 422 AD--LQQITQELNSENERLGEekviLMESLCQQSDKLEHFSRQieyfRSLLDEHHISYVIDEdvksgrymELEQRyMDLa 499
Cdd:pfam12128 504 ASeaLRQASRRLEERQSALDE----LELQLFPQAGTLLHFLRK----EAPDWEQSIGKVISP--------ELLHR-TDL- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 500 eNARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:pfam12128 566 -DPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 580 KAQLENEKQKVAELYSIHNSgdksdiqdllESVRLDKEKAETLASSLQE--DLAHTRNdanrlqdaiaKVEDEYRAFQEE 657
Cdd:pfam12128 645 RTALKNARLDLRRLFDEKQS----------EKDKKNKALAERKDSANERlnSLEAQLK----------QLDKKHQAWLEE 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 658 AKKQIEDLNMT-LEKLRSDLDEKETERSDMKETIFELEdevEQHRAvklHDNLIISDLENTVKKL---QDQKHDMEREIK 733
Cdd:pfam12128 705 QKEQKREARTEkQAYWQVVEGALDAQLALLKAAIAARR---SGAKA---ELKALETWYKRDLASLgvdPDVIAKLKREIR 778
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 734 TLHRRL------REESAEWRQFQADL-----QTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEeiKSRKQEE 802
Cdd:pfam12128 779 TLERKIeriavrRQEVLRYFDWYQETwlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERK--ASEKQQV 856
|
650 660
....*....|....*....|
gi 50949456 803 ERGRVYNYMNAVERDLAALR 822
Cdd:pfam12128 857 RLSENLRGLRCEMSKLATLK 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
412-681 |
8.60e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQAtlqELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHHISyvIDEDvkSGRYMEL 491
Cdd:PRK02224 478 EELEA---ELEDLEEEVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRET--IEEK--RERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 492 EQRYMDLAENARFEREQLlgvqqhlsntlKMAEQDNKEAQEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATVAS 571
Cdd:PRK02224 543 RERAAELEAEAEEKREAA-----------AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIER 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 572 ------DQIEMNRL-KAQLENEKQKVAELYSIHNsgdksdiQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:PRK02224 611 lrekreALAELNDErRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
250 260 270
....*....|....*....|....*....|....*..
gi 50949456 645 AKVEDEYRAFqEEAKKQIEDLNMTLEKLRSDLDEKET 681
Cdd:PRK02224 684 GAVENELEEL-EELRERREALENRVEALEALYDEAEE 719
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-801 |
1.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI 475
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 476 SY------VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 549
Cdd:COG1196 387 ELlealraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 550 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAET-----LAS 624
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 625 SLQEDLAHTRNDA------------------------------------------NRLQDAIAKVEDEYRAFQE------ 656
Cdd:COG1196 547 ALQNIVVEDDEVAaaaieylkaakagratflpldkiraraalaaalargaigaavDLVASDLREADARYYVLGDtllgrt 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 657 ---------------------EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE 715
Cdd:COG1196 627 lvaarleaalrravtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 716 NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTK----- 790
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlla 786
|
490
....*....|...
gi 50949456 791 --ELEEIKSRKQE 801
Cdd:COG1196 787 ieEYEELEERYDF 799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-678 |
1.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 538 KERSHHMERIIESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE----LYSIHNSGDKSDIQDLLESVR 613
Cdd:COG1579 24 HRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqLGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDE 678
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-804 |
2.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLENEKQKVAElysihnsgDKSDIQDLLESVRLDKEKAETLASSLQE----------DLAHTRNDANRLQDAI 644
Cdd:TIGR04523 163 DLKKQKEELENELNLLEK--------EKLNIQKNIDKIKNKLLKLELLLSNLKKkiqknkslesQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 645 AKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENtvKKL 721
Cdd:TIGR04523 235 EKKQQEINEKTTEisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-------ISDLNN--QKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 722 QDQKHDMEREIKTLHRRLREesaewrqfqadLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEE-----------IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
...
gi 50949456 802 EER 804
Cdd:TIGR04523 375 LKK 377
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
1010-1110 |
3.72e-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: 44.39 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1010 GGSKRNALLKWCQKKTEgyqNIDITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAEsvgikSTL 1088
Cdd:cd21315 14 GPTPKQRLLGWIQSKVP---DLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEAMDLAE-----DWL 85
|
90 100
....*....|....*....|....*..
gi 50949456 1089 DINEMVRTE-----RPDWQNVMLYVTA 1110
Cdd:cd21315 86 DVPQLIKPEemvnpKVDELSMMTYLSQ 112
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-819 |
4.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLENEKQKVAELYS--------IHNSGDKSDIQDLLESVRLDKEKAE-TLASSLQEDLAHTRNDANRLQDAIA 645
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKnlnkdeekINNSNNKIKILEQQIKDLNDKLKKNkDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 646 KVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE--------------VEQHRAVKLHDN 708
Cdd:TIGR04523 121 KLEVELNKLEKQKKenkKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnllekeklniqknIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 709 LIISDLENTVKK---LQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKN 785
Cdd:TIGR04523 201 LLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270
....*....|....*....|....*....|....*..
gi 50949456 786 EK---LTKELEEIKSRKQEEERGRVYNYMNAVERDLA 819
Cdd:TIGR04523 281 KKikeLEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
604-737 |
4.62e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 604 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDlDEKE 680
Cdd:cd22656 99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 681 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:cd22656 176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
172-802 |
4.72e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 172 DNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQ-- 249
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQar 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 250 --NTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK--LFGYQSLSPEITPGNQ-SDGGGTLTSSVEGSAPG---- 320
Cdd:pfam15921 310 nqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQfSQESGNLDDQLQKLLADlhkr 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 321 SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGilSIERSRKGSSG-NASEVSVACL 396
Cdd:pfam15921 390 EKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNESLEKVSSL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 397 TERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFSRQIEYFRSLldehhis 476
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR------- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 477 yvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIESEQKGKA 556
Cdd:pfam15921 526 --VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVGQHGRTAG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---------SL 626
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdikqerdQL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 627 QEDLAHTRNDANRLQdaiakveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLH 706
Cdd:pfam15921 659 LNEVKTSRNELNSLS-------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 707 DNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQfqaDLQTAVVIANDIKSEAqEEIGDLKRRLHE--- 780
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQ---ELSTVATEKNKMAGEL-EVLRSQERRLKEkva 807
|
650 660
....*....|....*....|....*.
gi 50949456 781 ----AQEKNEKLTKELEEIKSRKQEE 802
Cdd:pfam15921 808 nmevALDKASLQFAECQDIIQRQEQE 833
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
604-807 |
5.11e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 604 DIQDLLESVRLDKEKAETLASSLQedlahtrndanRLQDAIAKVEDEYRAFQEEAKKqiedlnmtLEKLRSDLDEKETER 683
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQ-----------QHGNALAQLEPIVSVLQSDPEQ--------FEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 684 SDMKETIFELEDEVEQHRAVKLHDNLII----SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVI 759
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDAAEMlaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949456 760 ANDIKSEAQEEIGDLKRRLHE-----AQEKNEKLTKELEEIKSRKQEEERGRV 807
Cdd:PRK04863 1032 KRQMLQELKQELQDLGVPADSgaeerARARRDELHARLSANRSRRNQLEKQLT 1084
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
602-801 |
5.71e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 602 KSDIQDLLesvrldKEKAETLASSLQEdLAHTRNDANRLQDAIAKVEDEYRAFQE------EAKKQIEDLNMTLEKLRSD 675
Cdd:PRK03918 188 TENIEELI------KEKEKELEEVLRE-INEISSELPELREELEKLEKEVKELEElkeeieELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 676 LDEKETERSDMKETIFELEDEV-----------EQHRAVKLHDNLI---------ISDLENTVKKLQDQKHDME------ 729
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVkelkelkekaeEYIKLSEFYEEYLdelreiekrLSRLEEEINGIEERIKELEekeerl 340
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949456 730 REIKTLHRRLREESAEWRQFQADLQTAVVIANDI----KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
491-968 |
5.99e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.38 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 491 LEQRYMDLAENARFEReQLLGVQQHLSNTLKmAEQDNKEAQEMIGALKERSHHmERIIESEQKGKAALaatLEEYKATVA 570
Cdd:COG5022 798 KLQPLLSLLGSRKEYR-SYLACIIKLQKTIK-REKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFS---LLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 571 SDQIEMNRLKAQLENEKQKVAELYSIHNSGDKsdiqdlLESVRLdkEKAETLASSLQEDLAHTRNDANRLQDAIAKVE-D 649
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKSISSLKLVNLE------LESEII--ELKKSLSSDLIENLEFKTELIARLKKLLNNIDlE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 650 EYRAFQEEAKKQIEDLNMtleklrsdldeketERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQ---DQKH 726
Cdd:COG5022 944 EGPSIEYVKLPELNKLHE--------------VESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYG 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 727 DMEREIKTLHRRLREesaewrqfQADLQTAVVIANDIKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSR-----K 799
Cdd:COG5022 1010 ALQESTKQLKELPVE--------VAELQSASKIISSESTELSilKPLQKLKGLLLLENNQLQARYKALKLRRENsllddK 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 800 QEEERGRVYNYMNAVERD--LAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNpaaaaiprtPLSPSPMKTPPA 877
Cdd:COG5022 1082 QLYQLESTENLLKTINVKdlEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVN---------TLEPVFQKLSVL 1152
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 878 -AAVSPMQRHSISGPISTSKPLTALSDKRpnygeiPVQEHLLRTSSASRPASLPrvpaMESAKTLSVSRRSSEEMKRDIS 956
Cdd:COG5022 1153 qLELDGLFWEANLEALPSPPPFAALSEKR------LYQSALYDEKSKLSSSEVN----DLKNELIALFSKIFSGWPRGDK 1222
|
490
....*....|..
gi 50949456 957 AQEGASPASLMA 968
Cdd:COG5022 1223 LKKLISEGWVPT 1234
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
398-804 |
6.25e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 398 ERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISY 477
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 478 VIDE-------DVKSGRYMELEQRYM------------DLAENARFEREQL-------LGVQQHLSNTLKMAEQDNKEAQ 531
Cdd:TIGR00606 378 ELDGfergpfsERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQAdeirdekKGLGRTIELKKEILEKKQEELK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 532 EMIGALKERSHHMERIIESEQKGKAALA--------ATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS 603
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERelskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 604 -----DIQDLLESVRLDKEKAETLASSLQEDLAHT----------RNDANRLQDAIAKVEDEYrAFQEEAKKQIEDLNMT 668
Cdd:TIGR00606 538 emltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKkqledwlhskSKEINQTRDRLAKLNKEL-ASLEQNKNHINNELES 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 669 LEKLRSDLDEK-------ETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTlhrrlre 741
Cdd:TIGR00606 617 KEEQLSSYEDKlfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT------- 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 742 eSAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRR---------------------LHEAQEKNEKLTKELEEIKSRKQ 800
Cdd:TIGR00606 690 -EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlglapgrqsiidlkekeIPELRNKLQKVNRDIQRLKNDIE 768
|
....
gi 50949456 801 EEER 804
Cdd:TIGR00606 769 EQET 772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-678 |
7.22e-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: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 476 sYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERshhmERIIESEQKGK 555
Cdd:COG1196 321 -LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL----AEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 556 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 50949456 636 DANRLQDAIAKVEDEyrafqEEAKKQIEDLNMTLEKLRSDLDE 678
Cdd:COG1196 471 EAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLE 508
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
618-833 |
7.71e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 618 KAETLASSLQEDLaHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam07888 28 RAELLQNRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEeky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 695 -------DEVEQHRAVKLHDN----LIISDLENTVKKLQDQKHDMEREI-------KTLHRRLREESAEWRQFQADLQTA 756
Cdd:pfam07888 104 kelsassEELSEEKDALLAQRaaheARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 757 VVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynyMNAVERDLAALRQGMGLSRRSST 833
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKVE 254
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-702 |
8.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 464 EYFRSL-LDEHHISYVIDEDVKS-GRYMELEQRymdlAENARFEREQLLGVQQHLSntlkmAEQDNKEAQEMIGALKERS 541
Cdd:COG4913 211 DFVREYmLEEPDTFEAADALVEHfDDLERAHEA----LEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 542 HHMERiieseQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS---GDKSDIQDLLESVRLDKEK 618
Cdd:COG4913 282 RLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 619 AETLASSLQ--------------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtlekLRSDLDEKETERS 684
Cdd:COG4913 357 RERRRARLEallaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-------LRRELRELEAEIA 429
|
250
....*....|....*...
gi 50949456 685 DMKETIFELEDEVEQHRA 702
Cdd:COG4913 430 SLERRKSNIPARLLALRD 447
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
614-823 |
9.29e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 46.25 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYR--AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF 691
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRqnAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 692 ELEDEVEqhravklhdnliiSDLENTVKKLQDQKHDMEREIK-TLHRRLREESAEWRQFqadlqtavviandiKSEAQEE 770
Cdd:pfam03528 93 EAIDEVK-------------SQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQY--------------RESAERE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 50949456 771 IGDLKRRLHEAQEKnEKLTKELeeiksRKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:pfam03528 146 IADLRRRLSEGQEE-ENLEDEM-----KKAQEDAEKLRSVVMPMEKEIAALKA 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
606-895 |
1.16e-04 |
|
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: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE---- 678
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 679 --KETERSDMKETIF------ELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLhrrlreesaewRQFQ 750
Cdd:COG3883 95 lyRSGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-----------EALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQGMGLSRR 830
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA-----AAAAAAAAAAAAAAAAAAA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 831 SSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
396-822 |
1.19e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.43 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNS-ENERLGEEKVILMESLCQQSDkLEHFSRQIEYFRSLLDEHH 474
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiINDPVYKNRNYINDYFKYKND-IENKKQILSNIDAEINKYH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 475 ISYVIDEDVKSGR--YMELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQ 552
Cdd:PRK01156 326 AIIKKLSVLQKDYndYIKKKSRYDDLNN----QILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 553 KGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdkSDIQDLLESVRLDKEKAETLASSLQEDLA- 631
Cdd:PRK01156 402 IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL---------SRNMEMLNGQSVCPVCGTTLGEEKSNHIIn 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 632 HTRNDANRLQDAIAKVEDEYRAFQEEAKKQI--------EDLNMT------LEKLRSDLDEKETERSDMKETIFELEDEV 697
Cdd:PRK01156 473 HYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeylesEEINKSineynkIESARADLEDIKIKINELKDKHDKYEEIK 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 698 EQHRAVKLHD-----------NLIISDLEntVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV-VIANDIKS 765
Cdd:PRK01156 553 NRYKSLKLEDldskrtswlnaLAVISLID--IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIrEIENEANN 630
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 766 --EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRkqEEERGRVYNYMNAVERDLAALR 822
Cdd:PRK01156 631 lnNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI--IPDLKEITSRINDIEDNLKKSR 687
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
625-803 |
1.37e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR 701
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaeKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 702 AVKlhdNLIISDLENtVKKLQDQKHDMEREIKTLHRRLREEsaEWRQfqadlQTAVVianDIKSEAQ--EEIGDLKRRLH 779
Cdd:COG1340 85 EKL---NELREELDE-LRKELAELNKAGGSIDKLRKEIERL--EWRQ-----QTEVL---SPEEEKElvEKIKELEKELE 150
|
170 180
....*....|....*....|....*...
gi 50949456 780 EAQ---EKNEKLTKELEEIKS-RKQEEE 803
Cdd:COG1340 151 KAKkalEKNEKLKELRAELKElRKEAEE 178
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
556-801 |
1.59e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 556 AALAATLEEYKATVASDQIEMNRLKAQLENEK-QKVAELYSIHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETaQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 634 RNDANRLQDAIAkVEDEYRAFQE----EAKKQIEDLNMTLEKLRSDLDEKETErsdmkeTIFELEDEVEQHRAVKlhdnl 709
Cdd:pfam01576 305 KTELEDTLDTTA-AQQELRSKREqevtELKKALEEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKRNK----- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 710 iiSDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND---IKSEAQE-------EIGDLKRRLH 779
Cdd:pfam01576 373 --ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEklsklqsELESVSSLLN 450
|
250 260
....*....|....*....|..
gi 50949456 780 EAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQD 472
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
134-817 |
1.74e-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: 45.81 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 134 QSKKLPSAGQGANDMALAKRSRSRTATECDVRMS------KSKSDNQISDRAALEAKVKDLLTLAKTKDvEILHLRNELR 207
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtiELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 208 DMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK 287
Cdd:TIGR00606 482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDE 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 288 LFGYQSLSPeitpgNQSDGGGTLtSSVEGSAPGSVEDLLSQDENTLMDHQHSNSMDNLDSECSEvyQPLTSSDDALDAPS 367
Cdd:TIGR00606 562 LTSLLGYFP-----NKKQLEDWL-HSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE--QLSSYEDKLFDVCG 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 368 SSESEGILS-----IERSRKGSSGNASEVSVacLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENeRLGEEK 442
Cdd:TIGR00606 634 SQDEESDLErlkeeIEKSSKQRAMLAGATAV--YSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKL-RLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 443 VILMESLCQQSDKlehfsrqieyfrslldehhisyvidedvksgrymeleqrymdlaenarfEREQLLGVQQHLSNTLKM 522
Cdd:TIGR00606 711 LKSTESELKKKEK-------------------------------------------------RRDEMLGLAPGRQSIIDL 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 523 AEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKaTVASDQIEMNRLKAQLENEKQKVAELYSIHNSGD- 601
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDl 820
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 602 ----------KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD---AIAKVEDEYRAFQEeakkQIEDLNMT 668
Cdd:TIGR00606 821 drtvqqvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE----QLVELSTE 896
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKH-------------------DME 729
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqdgkddylkQKE 976
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 730 REIKTLHRRLREESAEWRQFQADLQTavvIANDIKSEAQEE------IGDLKRR--LHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnLTLRKREneLKEVEEELKQHLKEMGQMQVLQMK 1053
|
730
....*....|....*.
gi 50949456 802 EERGRVYNYMNAVERD 817
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRN 1069
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
1033-1097 |
1.75e-04 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 41.99 E-value: 1.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949456 1033 ITNFSSSWNDGLAFCALLHTYLPAHIP-YQELNSQDKRRNFMLAFQAAesvgiKSTLDINEMVRTE 1097
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLA-----KREFNIPMVLSPE 81
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
513-806 |
1.78e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 513 QQH---LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQK-------GKAALAATLEEYKATVASDQIEMNRLKAQ 582
Cdd:pfam10174 323 KQHievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKqlqdlteEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 583 LENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI 662
Cdd:pfam10174 403 IENLQEQLRD-----KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 663 EDLNMTLEKLRSDLDEKETERSDMKE--------------TIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQ---- 724
Cdd:pfam10174 478 KDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEE-------CSKLENQLKKAHNAeeav 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 725 --KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI---KSEAQEEIGDLKRRlheAQEKNEKLTKELEEIKSRK 799
Cdd:pfam10174 551 rtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVeneKNDKDKKIAELESL---TLRQMKEQNKKVANIKHGQ 627
|
....*..
gi 50949456 800 QEEERGR 806
Cdd:pfam10174 628 QEMKKKG 634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-659 |
2.00e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 408 HSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvIDEDVKsgr 487
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 488 ymELEQRYMDLAENARFEREQLlgvQQHLSNTLKMAEQDNKE---AQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 565 YKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEdlahtrnDANRLQDAI 644
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQ-------EAEELEALI 229
|
250
....*....|....*
gi 50949456 645 AKVEDEYRAFQEEAK 659
Cdd:COG4942 230 ARLEAEAAAAAERTP 244
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
635-802 |
2.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 635 NDANRLQDAIAKVEDEYRAfQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF-ELEDEVEQH-RAVKLHDNLIIS 712
Cdd:PRK00409 513 EDKEKLNELIASLEELERE-LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAiKEAKKEADEIIK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 713 DLENTVKKLQ-DQKhdmEREIKTLHRRLRE-----------ESAEWRQFQA--------DLQTAVVIANDIKSEAQEEIG 772
Cdd:PRK00409 592 ELRQLQKGGYaSVK---AHELIEARKRLNKanekkekkkkkQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAG 668
|
170 180 190
....*....|....*....|....*....|
gi 50949456 773 DLKRRLHEAQEknEKLTKELEEIKSRKQEE 802
Cdd:PRK00409 669 IMKMKVPLSDL--EKIQKPKKKKKKKPKTV 696
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-804 |
2.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLII--SDLENTVKKLQDQKHDMEREIKTL 735
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 736 hRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4913 688 -AALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-825 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 655 QEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDMEREIKT 734
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 735 LHRRLREesaeWRQFQADLQTAvviANDIKsEAQEEIGDLKRRLHEAQEKN-EKLTKELEEIKSRKQ--EEERGRVYNYM 811
Cdd:COG4717 151 LEERLEE----LRELEEELEEL---EAELA-ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAelEEELEEAQEEL 222
|
170
....*....|....
gi 50949456 812 NAVERDLAALRQGM 825
Cdd:COG4717 223 EELEEELEQLENEL 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-801 |
2.50e-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: 45.43 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 651 YRAFQEEAKKQIEDLNMTLEK-------LRSDLD------EKETERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENT 717
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRledilneLERQLKslerqaEKAERYKELKAELRELELALLVLRLEELREEL--EELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 718 VKKLQDQKHDMEREIKTLH---RRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
....*..
gi 50949456 795 IKSRKQE 801
Cdd:TIGR02168 328 LESKLDE 334
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
520-803 |
2.65e-04 |
|
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: 44.84 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 520 LKMAEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAATLEEYKAtvASDQIEMNR---------LKAQLENE 586
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQIleelDELLESEEKNREEVEELKDKYRE--LRKTLLANRfsygpaideLEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 587 KQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDanrLQDAIAKVEDEYRAFQEE--------- 657
Cdd:pfam06160 159 EEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE---LPDQLEELKEGYREMEEEgyalehlnv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 658 ------AKKQIEDLNMTLEKLrsDLDEKETERSDMKETIFEL----EDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHD 727
Cdd:pfam06160 236 dkeiqqLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 728 MEREIKTLHrrLRE-ESAEWRQFQADLQTAV----VIANDIK------SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIk 796
Cdd:pfam06160 314 LERVQQSYT--LNEnELERVRGLEKQLEELEkrydEIVERLEekevaySELQEELEEILEQLEEIEEEQEEFKESLQSL- 390
|
....*..
gi 50949456 797 sRKQEEE 803
Cdd:pfam06160 391 -RKDELE 396
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
538-804 |
2.87e-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: 45.12 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 538 KERSHHMERIiESEQKGkAALAATLEEYKATVASDQIEMNRLKAQlENEKQKVaelysihnsgdksdIQDLLESVRLDKE 617
Cdd:pfam05557 21 MELEHKRARI-ELEKKA-SALKRQLDRESDRNQELQKRIRLLEKR-EAEAEEA--------------LREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 618 KAETLASSLQEDLAhTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam05557 84 YLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 695 ----------DEVEQHRAVKLHDNLIIsdleNTVKKLQDQKHDMEREIKtlhrRLREESAEWRQFQADlqtavviandiK 764
Cdd:pfam05557 163 sslaeaeqriKELEFEIQSQEQDSEIV----KNSKSELARIPELEKELE----RLREHNKHLNENIEN-----------K 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 50949456 765 SEAQEEIGDLKRRLH---EAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05557 224 LLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVK 266
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
575-725 |
2.97e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYraf 654
Cdd:smart00787 155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949456 655 qEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 725
Cdd:smart00787 221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
827-992 |
3.14e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 827 LSRRSSTSSEPT---------------PTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGP 891
Cdd:PHA03247 2663 RPRRARRLGRAAqassppqrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 892 ISTSKPLTALSDKRPNYGEIPvqehllrtSSASRPASlPRVPAMESAKTLSVSRRSSEEMKRDiSAQEGASPASLMAMGT 971
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTT--------AGPPAPAP-PAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPPAAVL 2812
|
170 180
....*....|....*....|.
gi 50949456 972 TSPQLSLSSSPTASVTPTTRS 992
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTS 2833
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
412-801 |
3.58e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.81 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQitqELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHhisyvideDVKSGRYMEL 491
Cdd:pfam10174 331 ESLTAKEQRAAILQT---EVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML--------DVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 492 EQRYMDLAENARFEREQLLGvqqhLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKA----ALAATLEEYKA 567
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREredrERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 568 TVASDQIEMNRLKAQLENEKQKVAEL----YSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANR---- 639
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLkehaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpe 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 640 LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRsdldEKETERSDMKETIFELEDEVEQHravklhdnliISDLENTVK 719
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAELESLTLRQ----------MKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 720 KLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSeaQEEIGDLKRRLHEAQ----EKNEKLT------ 789
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQqslaEKDGHLTnlraer 699
|
410
....*....|...
gi 50949456 790 -KELEEIKSRKQE 801
Cdd:pfam10174 700 rKQLEEILEMKQE 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
484-823 |
3.88e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 484 KSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIEseqkgKAALAATLE 563
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 564 EYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdKSDIQDLLEsvRLDKEKAETLASSLQEdLAHTRNDANRLQDA 643
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEEL-----EAELAELQE--ELEELLEQLSLATEEE-LQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 644 IAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDL-DEKETERSDMKETIFELEDEVEQHRAVKLHDN-------------- 708
Cdd:COG4717 208 LAELEEEL----EEAQEELEELEEELEQLENELeAAALEERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 709 -LIISDLENTVKKLQDQKHDMErEIKTLHRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEK 787
Cdd:COG4717 284 gLLALLFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALGLP-------PDLSPEELLELLDRIEELQELLRE 355
|
330 340 350
....*....|....*....|....*....|....*.
gi 50949456 788 LTKELEEIKSRKQEEERGRVYNYMNAveRDLAALRQ 823
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGV--EDEEELRA 389
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
575-676 |
4.50e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLenekQKVAELYSIHNSGdKSDIQDLLESVRLDKEKAETLASSLQ---EDLAHTRNDANRLQDAIAKVEDEY 651
Cdd:PRK09039 54 ALDRLNSQI----AELADLLSLERQG-NQDLQDSVANLRASLSAAEAERSRLQallAELAGAGAAAEGRAGELAQELDSE 128
|
90 100
....*....|....*....|....*
gi 50949456 652 RAFQEEAKKQIEDLNMTLEKLRSDL 676
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQL 153
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
505-792 |
5.28e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 505 EREQLLGVQQHlSNTLKMAEQdnkEAQEMIGALKErshhMERIIESEQKgkaALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:pfam12128 239 IRPEFTKLQQE-FNTLESAEL---RLSHLHFGYKS----DETLIASRQE---ERQETSAELNQLLRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 585 NEKQKVAELYSihnsGDKSDIqDLLES--VRLDKEKAETLASSlQEDLAHTRNDANR-------LQDAIAKVEDEYRAFQ 655
Cdd:pfam12128 308 GELSAADAAVA----KDRSEL-EALEDqhGAFLDADIETAAAD-QEQLPSWQSELENleerlkaLTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 656 ----EEAKKQIEDLNMTLEKLRSDLD-EKETERSDMKETIFELEDEVEQH-RAVKLHDNLIISDLE------NTVKKLQD 723
Cdd:pfam12128 382 skikEQNNRDIAGIKDKLAKIREARDrQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGelklrlNQATATPE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 724 QKHDMEREIKTLHRrLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL 792
Cdd:pfam12128 462 LLLQLENFDERIER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
396-803 |
5.68e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQ---QITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDE 472
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALqqtQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 473 -----------HHISYVIDEDVKSGRYMELEQRYMDLAENARFER------EQLLGVQQHLSNTLKMAEQDNKEAQE--- 532
Cdd:TIGR00618 286 inrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEvat 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 533 MIGALKERSHHMERIIESEQKGKAALAATLEEYKAtvasdqiemnrLKAQLENEKQKVAELYSIHNSgDKSDIQDLLESV 612
Cdd:TIGR00618 366 SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK-----------ELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 613 RLDKEKAETLASSLQedlahtrndaNRLQDAIAKVEDEYRAFQeeAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFE 692
Cdd:TIGR00618 434 ELQQRYAELCAAAIT----------CTAQCEKLEKIHLQESAQ--SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 693 LEDEVEQ---HRAVKLHDNLI-------ISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:TIGR00618 502 EPCPLCGsciHPNPARQDIDNpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 50949456 763 IKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR00618 582 SKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
442-801 |
6.10e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 442 KVIL--MESLCQQSDKLEHFSRqieyfRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLsnt 519
Cdd:TIGR01612 496 KLILmrMKDFKDIIDFMELYKP-----DEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKEL--- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 520 lkmaEQDNKEAQEMIGALKERSHHMERIIEsEQKGKAALAATLEEyKATVASDQIEMNR----LKAQLENEKQKVAELYS 595
Cdd:TIGR01612 568 ----EEENEDSIHLEKEIKDLFDKYLEIDD-EIIYINKLKLELKE-KIKNISDKNEYIKkaidLKKIIENNNAYIDELAK 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 596 IH--------NSGDK--SDIQDLLESV---RLDKEKAEtLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQeeakkqi 662
Cdd:TIGR01612 642 ISpyqvpehlKNKDKiySTIKSELSKIyedDIDALYNE-LSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ------- 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 663 edlNMTLEKLRSDLDEKETERSDMKETIFELEDEVeqHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHrRLREE 742
Cdd:TIGR01612 714 ---NMETATVELHLSNIENKKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSK 787
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 743 SAEWRQFQADlqtAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR01612 788 ISEIKNHYND---QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
597-825 |
6.11e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 597 HNSGDKSDIQDLLE----SVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI---EDLNMTL 669
Cdd:pfam00038 26 QNKLLETKISELRQkkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELnlrTSAENDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 670 EKLRSDLDEKETERSDMKETIFELEDEVEQHRavKLHDNLIiSDLENTVKKLQDQ-------KHDME---REIKTLH--- 736
Cdd:pfam00038 106 VGLRKDLDEATLARVDLEAKIESLKEELAFLK--KNHEEEV-RELQAQVSDTQVNvemdaarKLDLTsalAEIRAQYeei 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 737 -RRLREESAEWRQFQ-ADLQTAVVIANDIKSEAQEEIGDLKRRLH------EAQEK-NEKLTKELEEIKSRkQEEERGRV 807
Cdd:pfam00038 183 aAKNREEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQsleielQSLKKqKASLERQLAETEER-YELQLADY 261
|
250
....*....|....*...
gi 50949456 808 YNYMNAVERDLAALRQGM 825
Cdd:pfam00038 262 QELISELEAELQETRQEM 279
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
616-792 |
6.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 616 KEKAETLASSLQEDLAHTRNDANR-----LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 691 FELEDEVEQHRAvklhdnlIISDLENTVKKLqdqkhdmEREIKTLHRRLREESAEWRQFQADLQTAVVIANdIKSEAQEE 770
Cdd:PRK12704 106 EKREEELEKKEK-------ELEQKQQELEKK-------EEELEELIEEQLQELERISGLTAEEAKEILLEK-VEEEARHE 170
|
170 180
....*....|....*....|...
gi 50949456 771 IGDLKRRLH-EAQEKNEKLTKEL 792
Cdd:PRK12704 171 AAVLIKEIEeEAKEEADKKAKEI 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
708-804 |
7.86e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 708 NLIISDLENTVKKLQDQKHDME---REIKTLHRRLREESAEWRQ-FQADLQTAVVIANDIKSEAQEEIGDLKRRL----- 778
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110
....*....|....*....|....*....|....
gi 50949456 779 --------HEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PRK00409 599 ggyasvkaHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
404-806 |
8.14e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 404 EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSdklEHFSrQIEYFRSLLdehhisyvidedv 483
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET---ELCA-EAEEMRARL------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 484 kSGRYMELEQRYMDLaeNARFEREQLLGVQQHlsntlkmaeQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAA--- 560
Cdd:pfam01576 67 -AARKQELEEILHEL--ESRLEEEEERSQQLQ---------NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkik 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 561 TLEEYKATVASDQIEMNRLKAQLEN-----------EKQKVAELYSIHNSGDK--SDIQDLL---ESVRLDKEKA----E 620
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEEriseftsnlaeEEEKAKSLSKLKNKHEAmiSDLEERLkkeEKGRQELEKAkrklE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 621 TLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALarleeetaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 691 FELEDEVEQHRAvKLHDNLiisDLENTVKKLQDQKhdmEREIKTLHRRLREESaewRQFQADLQ-------TAVVIANDI 763
Cdd:pfam01576 295 RDLGEELEALKT-ELEDTL---DTTAAQQELRSKR---EQEVTELKKALEEET---RSHEAQLQemrqkhtQALEELTEQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 50949456 764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
727-784 |
9.13e-04 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 41.95 E-value: 9.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 50949456 727 DMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 784
Cdd:PRK10884 97 DLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNQLIVAQKK 154
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
828-967 |
1.01e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 828 SRRSSTSSEPTPTVKTLIKSF----DSASQVPNPAAAAIPRT----PLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLT 899
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFalppDQPERPPQPQAPPPPQPqpqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50949456 900 ALSDKRPNY---GEIPVQEHLLRTSSASRPASLPRVPameSAKTLSVSRRSSEEMKRDISAQEGASPASLM 967
Cdd:PHA03247 2958 AVPQPWLGAlvpGRVAVPRFRVPQPAPSREAPASSTP---PLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
398-804 |
1.04e-03 |
|
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: 43.17 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 398 ERIHQMEENQHSTSEELQATLQE----LADLQQITQELNSENERLG---EEKVILMESLCQQSDKLEHFSRQIEYFRSLL 470
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKVSlklEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 471 DEHHISYVIDEDVKSGRYMELEQRYMDL----------AENARFEREQLLGVQ----QHLSNTLKmAEQDNKEaqemiga 536
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqAENARLEMHFKLKEDhekiQHLEEEYK-KEINDKE------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 537 lKERSHHMERIIESEQKGKAaLAATLEEYKATV----ASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS--------- 603
Cdd:pfam05483 240 -KQVSLLLIQITEKENKMKD-LTFLLEESRDKAnqleEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 604 DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE-- 678
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEmt 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 679 -----KETERSDMKETIFELEDEVEQHRAV-KLHDNLIISDLENT--VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQ 750
Cdd:pfam05483 398 kfknnKEVELEELKKILAEDEKLLDEKKQFeKIAEELKGKEQELIflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 50949456 751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
490-796 |
1.20e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 490 ELEQRYMDLAEN--ARFErEQLLGVQQhLSNTLKM--AEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAAT 561
Cdd:PRK04778 68 EWRQKWDEIVTNslPDIE-EQLFEAEE-LNDKFRFrkAKHEINEIESLLDLIEEDIEQIleelQELLESEEKNREEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 562 LEEY---KATV---------ASDQIEmnrlkAQLENEKQKVAELYSIHNSGDKsdiqdllesvrldkEKAETLASSLQED 629
Cdd:PRK04778 146 KDLYrelRKSLlanrfsfgpALDELE-----KQLENLEEEFSQFVELTESGDY--------------VEAREILDQLEEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 630 LAHTRNDANRLQDAIAKVEDEYRAfqeeakkQIEDLNMTLEKLRSD---LDEKetersDMKETIFELEDEVEQHRAvklh 706
Cdd:PRK04778 207 LAALEQIMEEIPELLKELQTELPD-------QLQELKAGYRELVEEgyhLDHL-----DIEKEIQDLKEQIDENLA---- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 707 dnlIISDLEntVKKLQDQKHDMEREIKTLHRRLREEsaewrqfqadlqtavVIAndiKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:PRK04778 271 ---LLEELD--LDEAEEKNEEIQERIDQLYDILERE---------------VKA---RKYVEKNSDTLPDFLEHAKEQNK 327
|
330
....*....|
gi 50949456 787 KLTKELEEIK 796
Cdd:PRK04778 328 ELKEEIDRVK 337
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
516-799 |
1.21e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 516 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVaelys 595
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL----- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 596 ihnsgdkSDIQDLLESVRLDKEKaetlassLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSD 675
Cdd:TIGR04523 471 -------KVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 676 LDEKETERSDMKETIFELEDeveqhravklhdnliisdlENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQT 755
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDF-------------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 50949456 756 AVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:TIGR04523 594 KEKEKKDLIKEIEEkekKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
607-823 |
1.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 607 DLLESVRLDKEKAETLASSLQEDLAHTR-------------NDANRLQDAIAKVEDEYRAFQ-----EEAKKQIEDLNMT 668
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPvkgsnvieisytsPDPELAAAVANALAEAYLEQNlelrrEEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 669 LEKLRSDLDEKETERSDMKET--IFELEDEVEQHRAvklhdnlIISDLENTVKKLQDQKhdmeREIKTLHRRLREESAEW 746
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQ-------QLSELESQLAEARAEL----AEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 747 RQFQADLQTAVVIANDIK--SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvyNYMNAVERDLAALRQ 823
Cdd:COG3206 253 PDALPELLQSPVIQQLRAqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----RILASLEAELEALQA 327
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
398-665 |
1.48e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 398 ERIHQMEENQHSTSEELQATLQEL-ADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHfSRQIEYFRSLL 470
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFqAKEQEATEELLSLEQKLSVAQAAHsqfeqaYQLVRKIAGEVSR-SEAWDVARELL 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 471 DEHhisyvidedvksgrymeleqrymdlaENARFEREQLLGVQQHLSnTLKMAEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:PRK04863 503 RRL--------------------------REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 551 EQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSI----HNSgdksdiQDLLEsvRLDKEKAETLASSl 626
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawLAA------QDALA--RLREQSGEEFEDS- 626
|
250 260 270
....*....|....*....|....*....|....*....
gi 50949456 627 qEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDL 665
Cdd:PRK04863 627 -QDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
404-794 |
1.48e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 404 EENQH--STSEELQATLQELADLQQITQELNSENERLGEEKVILM----ESLCQQSDKLEHFSRQIEYFRSLLDEhhisy 477
Cdd:pfam10174 67 EENQHlqLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelteENFRRLQSEHERQAKELFLLRKTLEE----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 478 videdvksgryMELEQRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGAlKERSHHMERIIESEQKGKA 556
Cdd:pfam10174 142 -----------MELRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIAEA-EMQLGHLEVLLDQKEKENI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 557 ALAATLeEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDL------ 630
Cdd:pfam10174 210 HLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSL--------ERNIRDLEDEVQMLKTNGLLHTEDREEEIkqmevy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 631 -AHT---RNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTL--------------EKLRSDLDEKETE 682
Cdd:pfam10174 281 kSHSkfmKNKIDQLKQELSKKESELLALQtkletltnqnSDCKQHIEVLKESLtakeqraailqtevDALRLRLEEKESF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 683 RSDMKETIFELEDE--VEQHRAVKLHDNLIISD-----LENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQAD 752
Cdd:pfam10174 361 LNKKTKQLQDLTEEksTLAGEIRDLKDMLDVKErkinvLQKKIENLQEQLRDKDKQLAGLKERvksLQTDSSNTDTALTT 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 50949456 753 LQTAVVIANDI-----------KSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:pfam10174 441 LEEALSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
575-959 |
1.50e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 575 EMNRLKAQLENEKQKVAELYS----IHNSGDKSDIQDL--LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:PTZ00108 1003 KLERELARLSNKVRFIKHVINgelvITNAKKKDLVKELkkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 649 DEYRAFQEEAKKQIEDLNMT-LEKLRSDLDEKETERSDMKETifeledEVEQhravklhdnLIISDLENTVKKLQDQKHD 727
Cdd:PTZ00108 1083 GAAVSYDYLLSMPIWSLTKEkVEKLNAELEKKEKELEKLKNT------TPKD---------MWLEDLDKFEEALEEQEEV 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 728 MEREI----------KTLHRRLR------EESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEK-LTK 790
Cdd:PTZ00108 1148 EEKEIakeqrlksktKGKASKLRkpklkkKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSdQED 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 791 ELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNpaaaaiPRTPLSPS 870
Cdd:PTZ00108 1228 DEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPD------GESNGGSK 1301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 871 PMKTPPAAAVSPMQRHSISGPISTSKPLTALSDKRpnygeipVQEHLLRTSSASRPASLPRVPAMESAKTLSvsrrSSEE 950
Cdd:PTZ00108 1302 PSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKK-------SKTRVKQASASQSSRLLRRPRKKKSDSSSE----DDDD 1370
|
....*....
gi 50949456 951 MKRDISAQE 959
Cdd:PTZ00108 1371 SEVDDSEDE 1379
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
412-808 |
2.00e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKs 485
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskseLARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLK- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 486 gRYMELEQRYMDLAENARFEREQLLG--------VQQH---------LSNTLKMAEQDNKEAQEMIGALKERSHHMERII 548
Cdd:pfam05557 235 -RKLEREEKYREEAATLELEKEKLEQelqswvklAQDTglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 549 -ESEQKGKAALAATLEEYKATVASDQI-------------EMNRLKAQLEN-EKQKVAELYSIHNSGDKSDIQDLLESVR 613
Cdd:pfam05557 314 rELEQELAQYLKKIEDLNKKLKRHKALvrrlqrrvllltkERDGYRAILESyDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEdeyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFEL 693
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 694 EDEVEQH-----------RAVKLHDNliisdleNTVKKLQDQKHDMER---EIKTLHRRLreesaewRQFQADLQTAVVI 759
Cdd:pfam05557 468 EMELERRclqgdydpkktKVLHLSMN-------PAAEAYQQRKNQLEKlqaEIERLKRLL-------KKLEDDLEQVLRL 533
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 50949456 760 ANDIKSEAQEEIGDLKRRLHEAQEKNEKltkeLEEIKSRKQEEERGRVY 808
Cdd:pfam05557 534 PETTSTMNFKEVLDLRKELESAELKNQR----LKEVFQAKIQEFRDVCY 578
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
412-813 |
2.17e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI---------SYVIDED 482
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyeseiktaeSDLSMEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 483 VKSGRYMELEQRYMDLAENARF-EREQLLGVQqhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKaalaat 561
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYkNRNYINDYF-----KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY------ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 562 leeykatvaSDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAnrlq 641
Cdd:PRK01156 339 ---------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAFISEILKIQEIDP---- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 642 DAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETE------RSDMKETIFELEDEVEQHravklhdnlIISDLE 715
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNmemlngQSVCPVCGTTLGEEKSNH---------IINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 716 NTVKKLQDQKHDMEREIKTLHRRLRE-ESAEWRQFQADLQTAVVIANDIKSeAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDlKKRKEYLESEEINKSINEYNKIES-ARADLEDIKIKINELKDKHDKYEEIKNR 554
|
410
....*....|....*....
gi 50949456 795 IKSRKQEEERGRVYNYMNA 813
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNA 573
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
656-823 |
2.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 656 EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKtl 735
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEELE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 736 hrRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVE 815
Cdd:COG4372 105 --SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*...
gi 50949456 816 RDLAALRQ 823
Cdd:COG4372 183 QALDELLK 190
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
544-864 |
2.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 544 MERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdiQDLLESVRLDKEKAETLA 623
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL------------EEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 624 SSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqiedLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV 703
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ----LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 704 KLhdNLIISDLENTVKKLQDQ---------KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDL 774
Cdd:COG4372 173 LQ--ALSEAEAEQALDELLKEanrnaekeeELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 775 KRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQV 854
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
330
....*....|
gi 50949456 855 PNPAAAAIPR 864
Cdd:COG4372 331 ALAILLAELA 340
|
|
| CH_AtFIM_like_rpt2 |
cd21296 |
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
1017-1094 |
2.39e-03 |
|
second calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409145 Cd Length: 109 Bit Score: 38.65 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 1017 LLKWC--QKKTEGYQNIdITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFMLAFQAAESVGIKSTLDINEMV 1094
Cdd:cd21296 15 LLKWMnfHLKKAGYKKT-VTNFSSDVKDAEAYAYLLNVLAPEHCDPATLEAKDPLERAKLVLEQAEKMNCKRYLTAKDIV 93
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
508-806 |
2.84e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 508 QLLGVQQHLSNTLKMAEQDN--KEAQEMIGALKE-RSHHMERIIESEQKGKAALAATleEYKATVASDQ----IEMNRLK 580
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEM--DRQAAIYAEQermaMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 581 AQLENEKQKvAELYSIHNSGDKSDIQDLLESVRLDKEKAEtlasslqedlahtRNDANRLQDAIAKvedEYRAFQEEAKK 660
Cdd:pfam17380 351 ERIRQEERK-RELERIRQEEIAMEISRMRELERLQMERQQ-------------KNERVRQELEAAR---KVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 661 QIEDLNMTLEKLRSDldEKETERSDMKETIFELEDEVEQHRAVKLhdnliisDLENTVKKLQDQKHDMEReiktlhRRLR 740
Cdd:pfam17380 414 KIQQQKVEMEQIRAE--QEEARQREVRRLEEERAREMERVRLEEQ-------ERQQQVERLRQQEEERKR------KKLE 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50949456 741 EESAEWRQFQADLQTAVVIandikseaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKIL--------EKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
495-801 |
3.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 495 YMDLAENARFEREQLLGVQQHLSN---TLKMAEQDNKEAQEMIGALKERSHHMERIIESeQKGKAALAATLEEYKATVAS 571
Cdd:PRK04863 274 YMRHANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 572 DQIEMNRLKAQLENEKQKVAElysihnsgdksdIQDLLESVRLDKEKAET----LASSL---QE--DLAHTR----NDAN 638
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEE------------ADEQQEENEARAEAAEEevdeLKSQLadyQQalDVQQTRaiqyQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 639 RLQD-----------AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEK---------------ETERSDMKETIFE 692
Cdd:PRK04863 421 QALErakqlcglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvrkiagEVSRSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 693 LEDEVEQHRAvklhdnliisdlentvkkLQDQKHDMEREIKTLHRRLREESAEWR-------QFQADLQTAVViANDIKS 765
Cdd:PRK04863 501 LLRRLREQRH------------------LAEQLQQLRMRLSELEQRLRQQQRAERllaefckRLGKNLDDEDE-LEQLQE 561
|
330 340 350
....*....|....*....|....*....|....*.
gi 50949456 766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
419-778 |
3.31e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 419 QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhisyvideDVKSGRYMELEQRYMDL 498
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV----------RLQDLTEKLSEAEDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 499 AENarfeREQLLGVQQHLSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQiemnR 578
Cdd:TIGR00618 612 CEQ----HALLRKLQPEQDLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ----L 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 579 LKAQLENEKQKVA---ELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQE------DLAHTRNDANRLQDAI--AKV 647
Cdd:TIGR00618 681 ALQKMQSEKEQLTywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDlaaredALNQSLKELMHQARTVlkART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 648 EDEYRAFQEEAkkQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR-----AVKLHDNLIISDLENTVKKLQ 722
Cdd:TIGR00618 761 EAHFNNNEEVT--AALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdedILNLQCETLVQEEEQFLSRLE 838
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50949456 723 dQKHDMEREIKTLHRRLREES---AEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRL 778
Cdd:TIGR00618 839 -EKSATLGEITHQLLKYEECSkqlAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKF 896
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
555-825 |
3.35e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 555 KAALAATLEEYKATVASDQ----IEMNRLKAQLENEK-QKVAELYSihnsgdksDIQDLLESVRLDKEKAETLAS----- 624
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALHelgvVHIEDLKEELSNERlRKLRSLLT--------KLSEALDKLRSYLPKLNPLREekkkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 625 ---SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEaKKQIEDLNMTLEKLRS-DLDEKETERSDMKETIF-----ELED 695
Cdd:PRK05771 80 svkSLEELIKDVEEELEKIEKEIKELEEEISELENE-IKELEQEIERLEPWGNfDLDLSLLLGFKYVSVFVgtvpeDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 696 EVEQhrAVKLHDNLIISDLENT----VKKLQDQKHDMEREIKTLhrrlreesaEWRQFQAdlqtavviaNDIKSeAQEEI 771
Cdd:PRK05771 159 ELKL--ESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKL---------GFERLEL---------EEEGT-PSELI 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50949456 772 GDLKRRLHEAQEKNEKLTKELEEIKsRKQEEERGRVYNYM-NAVERDLAALRQGM 825
Cdd:PRK05771 218 REIKEELEEIEKERESLLEELKELA-KKYLEELLALYEYLeIELERAEALSKFLK 271
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
539-659 |
3.44e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 539 ERSHHMERII-------ESEQKGKAALAATLEEykatvasdqieMNRLKAQLENEKQKVAELYSihnsgDKSDIQDLLES 611
Cdd:PRK11637 149 EESQRGERILayfgylnQARQETIAELKQTREE-----------LAAQKAELEEKQSQQKTLLY-----EQQAQQQKLEQ 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50949456 612 VRLDKEKAET-LASSLQED---LAHTRNDANRLQDAIAKVEDEYRAFQE-EAK 659
Cdd:PRK11637 213 ARNERKKTLTgLESSLQKDqqqLSELRANESRLRDSIARAEREAKARAErEAR 265
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-592 |
3.89e-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: 40.90 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 476 syVIDEDVKSGRYMELE--------------QRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKER 540
Cdd:COG4942 109 --LLRALYRLGRQPPLAlllspedfldavrrLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 50949456 541 SHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
660-754 |
3.92e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.97 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDeVEQHRAV--KLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELEL-LDEDTKVykLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
|
90
....*....|....*..
gi 50949456 738 RLREESAEWRQFQADLQ 754
Cdd:pfam01920 81 QLEKLEKELEELKEELY 97
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
656-810 |
4.16e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 656 EEAKKQIEDLNMTLEKLRSDLDEKETErsdMKETIFELEDEVEQhrAVKLHDNL--IISDLENTVKKLqdqKHDMEREIK 733
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERE---LEQKAEEAEALLKE--AEKLKEELeeKKEKLQEEEDKL---LEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 734 TLHRRLREESAEWRQFQADLQTAVVIAndIKSEAQEEIgdlKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNY 810
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQKGGYAS--VKAHELIEA---RKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
507-736 |
4.80e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMEriIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEeaKTIKAE--IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 585 NeKQKVAELYSIHN-----SGDKSDIQDLLESVrldKEKAETLASSLqedlahtrNDANRLQDAIAKVEDEYRafqeEAK 659
Cdd:PHA02562 273 Q-FQKVIKMYEKGGvcptcTQQISEGPDRITKI---KDKLKELQHSL--------EKLDTAIDELEEIMDEFN----EQS 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50949456 660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKTLH 736
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE-------LAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
520-804 |
4.91e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 520 LKMAEQDNKEAQEMIGAlkERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS 599
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 600 GDKSDiqdllESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAfqEEAKKQIEDLNMTL--EKLRSDLD 677
Cdd:PTZ00121 1580 LRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEaeEKKKAEEL 1652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 678 EKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDME--REIKTLHRRLREESAEWRQFQADLQT 755
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAK-----KAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50949456 756 AVVIANDIKSEAQEEigdlKRRLHEAQ--EKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121 1728 NKIKAEEAKKEAEED----KKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
516-802 |
6.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 516 LSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQkgkaalaatleEYKATVASDQIEMNRLKAQLENEKQKVAELYS 595
Cdd:TIGR04523 347 LKKELTNSESENSEKQR---ELEEKQNEIEKLKKENQ-----------SYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 596 -IHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFqeeaKKQIEDLNMTLEKLR 673
Cdd:TIGR04523 413 qIKKlQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL----SRSINKIKQNLEQKQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 674 SDLDEKETERSDMKETIFELEDEVeqhraVKLHDNliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADl 753
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKV-----KDLTKK--ISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE- 560
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 50949456 754 qtavvianDIKSEAQEEIgdlkRRLHEAQEKNEKLTKELEEIKSRKQEE 802
Cdd:TIGR04523 561 --------KEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKE 597
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-673 |
7.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 412 EELQATLQELADLQQITQELNSENERLgeekvilmeslcqqSDKLEHFSRQIEYFRSLLDehhISYVIDEdvksgrYMEL 491
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDAL--------------QERREALQRLAEYSWDEID---VASAERE------IAEL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 492 EQRYMDL-AENARFE--REQLLGVQQhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIES--------EQKGKAALAA 560
Cdd:COG4913 674 EAELERLdASSDDLAalEEQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDElqdrleaaEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 561 TLEEYKATVASDQIE----------MNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDL 630
Cdd:COG4913 750 LLEERFAAALGDAVErelrenleerIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50949456 631 AHTRNDANRL--QDAIAKVED---EYRAFQEEAKKQIEDLNMTLEKLR 673
Cdd:COG4913 830 PEYEERFKELlnENSIEFVADllsKLRRAIREIKERIDPLNDSLKRIP 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
407-673 |
9.58e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 407 QHSTSEELQATLQELAD------LQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQieyfrslldehHISYVID 480
Cdd:COG3206 143 TSPDPELAAAVANALAEayleqnLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK-----------NGLVDLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 481 EDVKS--GRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQE--MIGALKERshhmeriieseqkgKA 556
Cdd:COG3206 212 EEAKLllQQLSELESQL----AEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQ--------------LA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50949456 557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRND 636
Cdd:COG3206 274 ELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE-----------AQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
250 260 270
....*....|....*....|....*....|....*..
gi 50949456 637 ANRLqdaiAKVEDEYRAFQEEAKKQIEDLNMTLEKLR 673
Cdd:COG3206 343 LAEL----PELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| |
