|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
838-921 |
6.74e-57 |
|
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: 191.04 E-value: 6.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 838 MLAKNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 917
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAESVGI 80
|
....
gi 665388955 918 GTTL 921
Cdd:cd21199 81 PTTL 84
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
833-921 |
2.76e-41 |
|
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: 147.14 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 833 KDPLNMLAKN-GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAA 911
Cdd:cd21256 1 KDPLSALAREyGGSKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQA 80
|
90
....*....|
gi 665388955 912 AESVGIGTTL 921
Cdd:cd21256 81 AESVGIKSTL 90
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
843-921 |
9.44e-39 |
|
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: 139.78 E-value: 9.44e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 843 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTL 921
Cdd:cd21257 6 GGSKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSL 84
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
847-913 |
1.75e-31 |
|
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: 118.60 E-value: 1.75e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 847 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21200 3 KQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAE 69
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
845-933 |
3.26e-28 |
|
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: 109.28 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLVHI 924
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
....*....
gi 665388955 925 CTYMLQPKE 933
Cdd:cd21261 81 EDMMVMGRK 89
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
845-937 |
4.88e-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: 108.98 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTLVHI 924
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90
....*....|...
gi 665388955 925 CTYMLQPKETQTR 937
Cdd:cd21258 81 EDMMIMGKKPDSK 93
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
850-917 |
7.06e-28 |
|
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: 108.28 E-value: 7.06e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 850 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 917
Cdd:cd21198 6 LLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAKLGI 73
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
847-913 |
1.26e-26 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 105.17 E-value: 1.26e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 847 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAE 69
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
845-913 |
3.21e-26 |
|
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: 103.92 E-value: 3.21e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAE 69
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
845-913 |
2.52e-25 |
|
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: 101.29 E-value: 2.52e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAE 78
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
845-913 |
6.47e-25 |
|
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: 99.78 E-value: 6.47e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAE 70
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
848-917 |
4.92e-24 |
|
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: 97.36 E-value: 4.92e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665388955 848 NALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGI 917
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQeLGI 73
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
845-917 |
1.06e-23 |
|
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: 96.40 E-value: 1.06e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 917
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFASLGV 73
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
849-913 |
2.23e-23 |
|
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: 95.49 E-value: 2.23e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 849 ALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21253 5 ALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAE 69
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
843-917 |
3.43e-23 |
|
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: 95.29 E-value: 3.43e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 843 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAF-AAAESVGI 917
Cdd:cd21291 8 GLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFdIASKEIGI 83
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
845-917 |
4.78e-23 |
|
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: 94.79 E-value: 4.78e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGI 917
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQeLGI 75
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
845-936 |
8.87e-23 |
|
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: 94.30 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGIgttlvh 923
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAErQLGI------ 78
|
90
....*....|...
gi 665388955 924 icTYMLQPKETQT 936
Cdd:cd21319 79 --TKLLDPEDVFT 89
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
845-913 |
2.21e-22 |
|
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: 93.00 E-value: 2.21e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAE 72
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
850-917 |
7.09e-22 |
|
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: 91.45 E-value: 7.09e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 850 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 917
Cdd:cd21254 6 LLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFASLGI 73
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
846-917 |
1.90e-20 |
|
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: 87.21 E-value: 1.90e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 846 KRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE-SVGI 917
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAEtSLGI 73
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
845-913 |
1.46e-18 |
|
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: 81.67 E-value: 1.46e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAE 69
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
841-913 |
3.17e-18 |
|
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: 81.26 E-value: 3.17e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 841 KNGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAE 73
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
845-913 |
1.15e-17 |
|
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: 79.37 E-value: 1.15e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAE 70
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
845-914 |
1.96e-17 |
|
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: 79.33 E-value: 1.96e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES 914
Cdd:cd21322 17 SAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQ 86
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
846-913 |
2.87e-17 |
|
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: 78.38 E-value: 2.87e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 846 KRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21250 5 RPNKLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAE 72
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
847-913 |
3.46e-17 |
|
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: 77.99 E-value: 3.46e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 847 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21252 2 RRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAE 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
357-650 |
3.90e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 357 LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKI 436
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 437 EELEADLSRgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNnakcAVSHLEYRLE 516
Cdd:COG1196 298 ARLEQDIAR-----LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA----ELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 517 QLQRDKDKIAGEWQALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQ 596
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 665388955 597 ADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 650
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
845-913 |
5.95e-17 |
|
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: 77.30 E-value: 5.95e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21251 5 ARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAE 73
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
850-917 |
8.28e-17 |
|
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: 76.70 E-value: 8.28e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 850 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAA-ESVGI 917
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAhEHLGI 73
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
842-913 |
1.11e-16 |
|
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: 76.62 E-value: 1.11e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665388955 842 NGGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21195 1 SGDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAE 72
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-539 |
2.06e-16 |
|
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: 84.34 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQslcrqteKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLL 342
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------ELEELSRQISALRKDLARLEAE---VEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 343 DLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEI 422
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 423 SRLSTLLENARSKIEELEADLSRgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKN 502
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIES-----LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 665388955 503 NAKCA---VSHLEYRLEQLQRDKDKIAGEWQALEERVAEL 539
Cdd:TIGR02168 909 KRSELrreLEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
848-916 |
2.97e-16 |
|
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: 75.04 E-value: 2.97e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 848 NALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPA----NKRRNFSLAFAAAESVG 916
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASlsrfKKIENINLALSFAEKLG 73
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-641 |
4.99e-16 |
|
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: 83.18 E-value: 4.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 350 EEREAVLLKQ----EELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRL 425
Cdd:TIGR02168 666 AKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 426 STLLENARSKIEELEADLS--RGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS-------QAELRRLRDQLSGLTEE 496
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEelEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALrealdelRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 497 CKVVKNNAKCAVSH---LEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGE 573
Cdd:TIGR02168 826 LESLERRIAATERRledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 574 AECRLDQETQLRRKEAEEWQQFQADL-LMTVRVANdfKTEALSAREQLVLDN------------KTQKEKIRLLEQQLEK 640
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLeGLEVRIDN--LQERLSEEYSLTLEEaealenkieddeEEARRRLKRLENKIKE 983
|
.
gi 665388955 641 L 641
Cdd:TIGR02168 984 L 984
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
844-913 |
1.21e-15 |
|
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: 73.61 E-value: 1.21e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 844 GSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAE 71
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-689 |
1.44e-15 |
|
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: 81.65 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQ--LELQRQRERIA--LLDSQLDAANAERRQGEAQFSQA 411
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEgyELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 412 MEEISQRAIEISRLSTLLENARSKIEELEAdlsrgdktdlsEVLDVARKEKDALEERVAELQ---DQCSRSQAELRRLRD 488
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNK-----------KIKDLGEEEQLRVKEKIGELEaeiASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 489 QLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQ 568
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 569 LKLGEAECRLDQETQLRRKEAEEwqqfQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQ 648
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 665388955 649 SETPQSV---LSTVQREMEMATRRSKLSFSRQDSRLSVKTLIES 689
Cdd:TIGR02169 475 KEEYDRVekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
847-917 |
2.57e-15 |
|
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: 72.70 E-value: 2.57e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 847 RNALLKWCQNKTVGY-RNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPA--NKRRNFSLAF-AAAESVGI 917
Cdd:pfam00307 4 EKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALdVAEKKLGV 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
264-540 |
4.23e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 264 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLLD 343
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE---EYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 344 LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEIS 423
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 424 RLSTLLENARSKIEELEADLSRGDKTDLSEVLDVAR--KEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvK 501
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERleEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----E 458
|
250 260 270
....*....|....*....|....*....|....*....
gi 665388955 502 NNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 540
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
845-913 |
8.25e-15 |
|
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: 71.68 E-value: 8.25e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21289 10 SAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAE 78
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
845-913 |
8.64e-15 |
|
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: 71.66 E-value: 8.64e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21287 10 SAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAE 78
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
843-917 |
1.43e-14 |
|
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: 70.42 E-value: 1.43e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 843 GGSKRnALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES-VGI 917
Cdd:cd21243 4 GGAKK-ALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKeLGI 78
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
845-913 |
1.54e-14 |
|
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: 70.87 E-value: 1.54e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21288 10 SAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAE 78
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-712 |
1.55e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 326
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 327 QpapEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 406
Cdd:COG1196 359 E---LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 407 QFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDK--TDLSEVLDVARKEKDALEERVAELQDQcsRSQAELR 484
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAalAELLEELAEAAARLLLLLEAEADYEGF--LEGVKAA 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 485 RLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRdkDKIAGEWQALEERVAELqvqcKCHQEDKAQLQSLLAETQRHL 564
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ--NIVVEDDEVAAAAIEYL----KAAKAGRATFLPLDKIRARAA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 565 GDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDfkteALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQ 644
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR----LEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 645 QMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADESESHYSSTSSL 712
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
247-532 |
5.81e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADL-------QTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQE 319
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELrlevselEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 320 LLLRDtkqpapevsaserEQKLLDLiktsQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANA 399
Cdd:TIGR02168 324 QLEEL-------------ESKLDEL----AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 400 ERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS 479
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 665388955 480 QAELRRLRDQLSGLTEEckvvknnakcaVSHLEYRLEQLQRDKDKIAGEWQAL 532
Cdd:TIGR02168 467 REELEEAEQALDAAERE-----------LAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-620 |
6.22e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 335 SEREQKLLDLiktSQEEREAVL----LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQ 410
Cdd:TIGR02168 209 AEKAERYKEL---KAELRELELallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 411 AMEEISQRAIEISRL---------------------STLLENARSKIEELEADLSR---------GDKTDLSEVLDVARK 460
Cdd:TIGR02168 286 LQKELYALANEISRLeqqkqilrerlanlerqleelEAQLEELESKLDELAEELAEleekleelkEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 461 EKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvknnakcaVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 540
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-----------IERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 541 VqcKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQL 620
Cdd:TIGR02168 435 L--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
845-917 |
7.39e-14 |
|
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: 68.53 E-value: 7.39e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGI 917
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAERLGV 76
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-496 |
7.49e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 241 EISVACLQDKIIQMEEThySTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQEL 320
Cdd:COG1196 226 EAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 321 LLRDTKQpapEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAE 400
Cdd:COG1196 304 IARLEER---RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 401 RRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQ 480
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-----LEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250
....*....|....*.
gi 665388955 481 AELRRLRDQLSGLTEE 496
Cdd:COG1196 456 EEEEALLELLAELLEE 471
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
845-913 |
1.16e-13 |
|
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: 68.57 E-value: 1.16e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21290 13 SAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAE 81
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-591 |
1.75e-13 |
|
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: 75.10 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVL--FQSL------CRQTEKLNESRT----------QISTLQELLLRD 324
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAerYQALlkekreYEGYELLKEKEAlerqkeaierQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 325 TKQ-PAPEVSASEREQKLLDL----IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANA 399
Cdd:TIGR02169 257 TEEiSELEKRLEEIEQLLEELnkkiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 400 ERRQGEaqfsqamEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKT--DLSEVLDVARKEKDALEERVAELQDQCS 477
Cdd:TIGR02169 337 EIEELE-------REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaETRDELKDYREKLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 478 RSQAELRRLRDQLSGLTEECKVvknnakcavshLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLL 557
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAG-----------IEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350
....*....|....*....|....*....|....*.
gi 665388955 558 AETQRHLGDVQLKLGEAECRLD--QETQLRRKEAEE 591
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARasEERVRGGRAVEE 514
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
847-918 |
1.85e-13 |
|
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: 67.36 E-value: 1.85e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 847 RNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYD---QLTPANKRRNFSLAFAAAESVGIG 918
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkkPKSPFKKRENINLFLNACKKLGLP 75
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
845-921 |
2.10e-13 |
|
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: 66.93 E-value: 2.10e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAESVGIGTTL 921
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEKLGVTRLL 77
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-502 |
5.00e-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: 73.55 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 234 DKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLtdtqtenERLAEEKDVLFQSLCRQTEKLNESRTQ 313
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 314 ISTLQELLlrdtkqpapevsaSEREQKLLDLiktsQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ 393
Cdd:TIGR02168 332 LDELAEEL-------------AELEEKLEEL----KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 394 LDAANAERRQGEAQfsqameeISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQ 473
Cdd:TIGR02168 395 IASLNNEIERLEAR-------LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260
....*....|....*....|....*....
gi 665388955 474 DQCSRSQAELRRLRDQLSGLTEECKVVKN 502
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
849-913 |
5.93e-13 |
|
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: 65.95 E-value: 5.93e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 849 ALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21226 4 GLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAE 68
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-650 |
1.02e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 370 KQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRgdkt 449
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 450 dlsevldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKcavsHLEYRLEQLQRDKDKIAGEW 529
Cdd:COG1196 286 --------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE----ELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 530 QALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEwQQFQADLLMTVRVANDF 609
Cdd:COG1196 354 EEAEAELAEAEEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLERLEEELEELEEA 429
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 665388955 610 KTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 650
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-669 |
1.06e-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: 72.41 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 358 KQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAAN-------AERRQGEAQFSQAMEEISQRAIEISRLSTLLE 430
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASrkigeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 431 NARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQaeLRRLRDQLSGLTEEckVVKNNAkcAVSH 510
Cdd:TIGR02169 755 NVKSELKELEARIEE------------LEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEE--VSRIEA--RLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 511 LEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRL-DQETQLRRKEA 589
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgDLKKERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 590 EewqqfqadllmtVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLS--TVQREMEMAT 667
Cdd:TIGR02169 897 Q------------LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVE 964
|
..
gi 665388955 668 RR 669
Cdd:TIGR02169 965 EE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
260-538 |
1.23e-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: 72.02 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 260 STNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNE-SRTQISTLQELLLRDTKQPAP---EVSAS 335
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASlerSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 EREQKLLD-LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQL---DAANAERRQGEAQFSQA 411
Cdd:TIGR02169 314 ERELEDAEeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeevDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 412 ME----EISQRAIEISRLSTLLENARSKIEELEADLSR--GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRR 485
Cdd:TIGR02169 394 LEklkrEINELKRELDRLQEELQRLSEELADLNAAIAGieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 665388955 486 LRDQLsglteeckvvknnakcavSHLEYRLEQLQRDKDKIAGEWQALEERVAE 538
Cdd:TIGR02169 474 LKEEY------------------DRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-580 |
2.45e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 256 ETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEkdvlFQSLCRQTEKLNESRT------------------QISTL 317
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDdllaeaglddadaeaveaRREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 318 Q---ELLLRDTKQPAPEVSASERE-QKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ 393
Cdd:PRK02224 320 EdrdEELRDRLEECRVAAQAHNEEaESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 394 LDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRG---------DKTDLSEVLDVARKEKDA 464
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvEGSPHVETIEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 465 LEERVAELQDQCSRSQAELRRLRDqLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGewqaLEERVAELQVQCK 544
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE----LRERAAELEAEAE 554
|
330 340 350
....*....|....*....|....*....|....*.
gi 665388955 545 CHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQ 580
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
845-917 |
6.64e-12 |
|
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: 62.64 E-value: 6.64e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 845 SKRNALLKWCQNKTVGYRnidITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAES-VGI 917
Cdd:cd21184 1 SGKSLLLEWVNSKIPEYK---VKNFTTDWNDGKALAALVDALKPGLIPdNESLDKENPLENATKAMDIAEEeLGI 72
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
247-641 |
8.62e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 8.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 326
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 327 QPAPEVS----ASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERR 402
Cdd:COG1196 394 AAAELAAqleeLEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 403 QGEAQFSQAMEEISQRAIEISRLSTLLENARSKIE----ELEADLSRGDKTDLSEVLDVARKEKDALEER---------- 468
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 469 -----------------------------------------------VAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 501
Cdd:COG1196 554 eddevaaaaieylkaakagratflpldkiraraalaaalargaigaaVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 502 NNAKCAVShLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQE 581
Cdd:COG1196 634 AALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 582 TQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDN-------KTQKEKIRLLEQQLEKL 641
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdlEELERELERLEREIEAL 779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
272-559 |
1.84e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 272 LADLQTQLTDTQTENERlAEEKDVlfqslcrqTEKLNESRTQISTLQELLLRDTKQpapEVSASEREQKLLDLIKTSQEE 351
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-KEEKDL--------HERLNGLESELAELDEEIERYEEQ---REQARETRDEADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 352 REAV-LLKQE--ELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 428
Cdd:PRK02224 250 REELeTLEAEieDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 429 LENARSKIEEL--EADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECkvvkNNAKC 506
Cdd:PRK02224 330 LEECRVAAQAHneEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF----GDAPV 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 665388955 507 AVSHLEYRLEQLQRDKDkiagewqALEERVAELQVQCKCHQEDKAQLQSLLAE 559
Cdd:PRK02224 406 DLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEAEALLEA 451
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
845-913 |
5.05e-11 |
|
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: 60.62 E-value: 5.05e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21244 5 SARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAE 73
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
843-888 |
6.32e-11 |
|
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: 60.06 E-value: 6.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 665388955 843 GGSKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLP 888
Cdd:cd21196 1 SSGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQP 46
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
848-921 |
8.73e-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: 59.24 E-value: 8.73e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 848 NALLKWCqNKTVGyrNIDITNFSSSWNDGLAFCAILHSyLPDRIP-YDQLTPANKRRNFSLAFAAAESVGIGTTL 921
Cdd:cd21185 4 KATLRWV-RQLLP--DVDVNNFTTDWNDGRLLCGLVNA-LGGSVPgWPNLDPEESENNIQRGLEAGKSLGVEPVL 74
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
410-590 |
1.03e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 410 QAMEEISQRA---IEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 486
Cdd:COG4913 242 EALEDAREQIellEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 487 RDQLSGLTEEckvVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQED----KAQLQSLLAETQR 562
Cdd:COG4913 322 REELDELEAQ---IRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEE 398
|
170 180
....*....|....*....|....*....
gi 665388955 563 HLGDVQLKLGEAECRL-DQETQLRRKEAE 590
Cdd:COG4913 399 ELEALEEALAEAEAALrDLRRELRELEAE 427
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-535 |
1.75e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 EREQKLLDLIKTSQEEREAVLLKQEELGAELAemkqareagQLELQRQRERIALLDSQLDAANAERRQGEAQfsqameei 415
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRA---------ALRLWFAQRRLELLEAELEELRAELARLEAE-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 416 sqraieISRLSTLLENARSKIEELEADLSR---GDKTDLSEVLDVARKEKDALEERVAELQDQCSR-------SQAELRR 485
Cdd:COG4913 311 ------LERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAAlglplpaSAEEFAA 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 665388955 486 LRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEER 535
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
845-915 |
2.31e-10 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 64.19 E-value: 2.31e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 845 SKRNALLKWCQNKTVGYRN-IDITNFSSSWNDGLAFCAILHSYLPDRIPYDQL--TPANKRRNFSLAFAAAESV 915
Cdd:COG5069 125 TKHINLLLWCDEDTGGYKPeVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdlQKKNKALNNFQAFENANKV 198
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
356-528 |
3.98e-10 |
|
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: 61.09 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 356 LLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSk 435
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 436 IEELEAdlsrgdktdLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRL 515
Cdd:COG1579 88 NKEYEA---------LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|...
gi 665388955 516 EQLQRDKDKIAGE 528
Cdd:COG1579 159 EELEAEREELAAK 171
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-562 |
7.84e-10 |
|
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: 61.70 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 343 DLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEI 422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 423 SRLSTLLEN------ARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQcsrsQAELRRLRDQLSGLTEE 496
Cdd:COG4942 100 EAQKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 497 CKVVKNNakcavshLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQR 562
Cdd:COG4942 176 LEALLAE-------LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
267-496 |
1.08e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 267 ATLQELADLQTQLTDT-QTENERLAEEKDvlFQSLCRQ--------TEKLNESRTQISTLQElllrdtkqpapEVSASER 337
Cdd:COG4913 565 DSPEELRRHPRAITRAgQVKGNGTRHEKD--DRRRIRSryvlgfdnRAKLAALEAELAELEE-----------ELAEAEE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 338 EQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQlELQRQRERI-------ALLDSQLDAANAERRQGEAQFSQ 410
Cdd:COG4913 632 RLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLdassddlAALEEQLEELEAELEELEEELDE 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 411 AMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARkeKDALEERVAE-LQDQCSRSQAELRRLRDQ 489
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAL--GDAVERELREnLEERIDALRARLNRAEEE 788
|
....*..
gi 665388955 490 LSGLTEE 496
Cdd:COG4913 789 LERAMRA 795
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
850-914 |
1.41e-09 |
|
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: 56.12 E-value: 1.41e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 850 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAES 914
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKN 69
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-701 |
1.51e-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: 62.00 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 382 RQRERIALLDSQLDAANAERRQGEAQFSQAMEEisqRAIEISRLSTLLENARSKIEELEADLS--RGDKTDLSEVLDVAR 459
Cdd:TIGR02168 642 RPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE---RRREIEELEEKIEELEEKIAELEKALAelRKELEELEEELEQLR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 460 KEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKvvknNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAEL 539
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT----ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 540 QVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLlmtvrvandfkTEALSAREQ 619
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-----------ESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 620 LVLDNKTQKEKIRLLEQQLEKLtKQQMQQSETPQSVLSTVQREMEmaTRRSKLSFSRQDSRLSVKTLIESIEnnKAQGKA 699
Cdd:TIGR02168 864 LEELIEELESELEALLNERASL-EEALALLRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLE--GLEVRI 938
|
..
gi 665388955 700 DE 701
Cdd:TIGR02168 939 DN 940
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-491 |
1.58e-09 |
|
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: 60.93 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 260 STNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQElllrdtkqpapEVSASEREq 339
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----------ELAALEAE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 340 klldlIKTSQEEREAVLLKQEELGAELAEMKQAreagqLELQRQRERIALLDSQLDAANAERR-QGEAQFSQA----MEE 414
Cdd:COG4942 85 -----LAELEKEIAELRAELEAQKEELAELLRA-----LYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLAPArreqAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 415 ISQRAIEISRLSTLLENARSKIEELEADLSR------GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRD 488
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEeraaleALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
...
gi 665388955 489 QLS 491
Cdd:COG4942 235 EAA 237
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
250-564 |
1.77e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 250 KIIQMEETHYSTNEELQATLQELADLQTQLtdtQTENERLAeekdvLFQSLCRQTEKLNESRTQISTLQELLlrdtkQPA 329
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDY---QAASDHLN-----LVQTALRQQEKIERYQADLEELEERL-----EEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 330 PEVSASEREQKLldlikTSQEEREAVLLKQEELGAELAEMKQA-----REAGQ-------------------LELQRQRE 385
Cdd:PRK04863 368 NEVVEEADEQQE-----ENEARAEAAEEEVDELKSQLADYQQAldvqqTRAIQyqqavqalerakqlcglpdLTADNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 386 RIALLDSQLDAANAERRQGE----------AQFSQAMEEISQRAIEISRlSTLLENARSKIEELE-----ADLSRGDKTD 450
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEqklsvaqaahSQFEQAYQLVRKIAGEVSR-SEAWDVARELLRRLReqrhlAEQLQQLRMR 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 451 LSEVLDVARKEKDAlEERVAELQDQCSR---SQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD---K 524
Cdd:PRK04863 522 LSELEQRLRQQQRA-ERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQrlaA 600
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 665388955 525 IAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHL 564
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE 640
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
271-488 |
3.07e-09 |
|
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: 60.29 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 271 ELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPApevsasEREQKLLDLiKTSQE 350
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA------ENEALLEEL-RSLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 351 EREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRA----------- 419
Cdd:pfam07888 245 RLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAeadkdriekls 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 420 IEISRLSTLLENARSKIEELEADL-------------SRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 486
Cdd:pfam07888 325 AELQRLEERLQEERMEREKLEVELgrekdcnrvqlseSRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
..
gi 665388955 487 RD 488
Cdd:pfam07888 405 AD 406
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
848-916 |
3.89e-09 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 55.77 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 848 NALLKWCQNKTVGYrNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTP----------------------------- 898
Cdd:cd21224 3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQpttqtvdraqdeaedfwvaefspstgdsg 81
|
90 100
....*....|....*....|....
gi 665388955 899 ------ANKRRNFSLAFAAAESVG 916
Cdd:cd21224 82 lssellANEKRNFKLVQQAVAELG 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-539 |
4.66e-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: 60.47 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQ-----TEKLNESRTQISTLqELL 321
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRI-EAR 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 322 LRDTKQPAPEVSasEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAER 401
Cdd:TIGR02169 814 LREIEQKLNRLT--LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 402 RQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKtdlsevlDVARKEKDALEERVAE-LQDQCSRSQ 480
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-------PKGEDEEIPEEELSLEdVQAELQRVE 964
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 481 AELRRLRDQLSGLTEECKVVknnakcavshlEYRLEQLQRDKDKIAGEWQALEERVAEL 539
Cdd:TIGR02169 965 EEIRALEPVNMLAIQEYEEV-----------LKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-540 |
5.39e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 384 RERIALLDSQLDAANAERRQGEAQFSQA---MEEISQRAIEISRLSTLLEN------ARSKIEELEADLSRGDKTD---- 450
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALeaeLDALQERREALQRLAEYSWDeidvasAEREIAELEAELERLDASSddla 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 451 -LSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEeckVVKNNAKCAVSHLEYRLEQL--QRDKDKIAG 527
Cdd:COG4913 689 aLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEERfaAALGDAVER 765
|
170
....*....|....
gi 665388955 528 E-WQALEERVAELQ 540
Cdd:COG4913 766 ElRENLEERIDALR 779
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
265-657 |
9.87e-09 |
|
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: 58.75 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 265 LQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQ----TEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQK 340
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelESRVAELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 341 LLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAgqlELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAI 420
Cdd:pfam07888 116 EKDALLAQRAAHEARIRELEEDIKTLTQRVLERET---ELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 421 E---------------------ISRLSTLLENARSKIEELEAdlSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRS 479
Cdd:pfam07888 193 EfqelrnslaqrdtqvlqlqdtITTLTQKLTTAHRKEAENEA--LLEELRSLQERLNASERKVEGLGEELSSMAAQRDRT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 480 QAELRRLRDQLSGLT---EECKVVKNNAKCAVSHLEYRLEQ-LQRDKDKIA---GEWQALEERVaelqvqckchQEDKAQ 552
Cdd:pfam07888 271 QAELHQARLQAAQLTlqlADASLALREGRARWAQERETLQQsAEADKDRIEklsAELQRLEERL----------QEERME 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 553 LQSLLAETQRhlgdvqlklgEAECRLDQETQLRRkeaeEWQQFQADLlmtvRVANDFKtealsarEQLVLDNKTQKEKIR 632
Cdd:pfam07888 341 REKLEVELGR----------EKDCNRVQLSESRR----ELQELKASL----RVAQKEK-------EQLQAEKQELLEYIR 395
|
410 420 430
....*....|....*....|....*....|
gi 665388955 633 LLEQQLEKLTKQQ-----MQQSETPQSVLS 657
Cdd:pfam07888 396 QLEQRLETVADAKwseaaLTSTERPDSPLS 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
247-445 |
1.25e-08 |
|
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: 58.24 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTK 326
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 327 QPAPEV----SASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERR 402
Cdd:COG4942 119 QPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 665388955 403 QGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSR 445
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-538 |
2.37e-08 |
|
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: 57.08 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 328 PAPEVSASEREQKLLDL---IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 404
Cdd:COG4942 16 AAQADAAAEAEAELEQLqqeIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 405 EAQFSQAMEEISQRAIEISRLS-----TLLENARS-----KIEELEADLSRGDKTDLsEVLDVARKEKDALEERVAELQD 474
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGrqpplALLLSPEDfldavRRLQYLKYLAPARREQA-EELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 475 QCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAE 538
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
387-599 |
3.48e-08 |
|
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: 56.70 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 387 IALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALE 466
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-----ALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 467 ERVAELQDQCSRSQAELRRLRDQLS---------GLTEECKVVKN--NAKCAVSHLEY----------RLEQLQRDKDKI 525
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAellralyrlGRQPPLALLLSpeDFLDAVRRLQYlkylaparreQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 526 AGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAEcrldQETQLRRKEAEEWQQFQADL 599
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA----AELAELQQEAEELEALIARL 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
288-677 |
3.90e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 288 RLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPApEVSASER--EQKL------LDLIKTSQEEREAVLLKQ 359
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELE-ELSARESdlEQDYqaasdhLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 360 EELGA---ELAEMKQAREAGQLELQRQRERIALLDSQLDAAnaerRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKI 436
Cdd:COG3096 354 EDLEElteRLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----KSQLADYQQALDVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 437 EEleADLSrgdktdlsevldvarkeKDALEERVAELQDQCSRSQAELRRLRDQLSglteeckvvknNAKCAVSHLEYRLE 516
Cdd:COG3096 430 GL--PDLT-----------------PENAEDYLAAFRAKEQQATEEVLELEQKLS-----------VADAARRQFEKAYE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 517 QLQrdkdKIAGE------WQALEERVAElqvqckcHQEDKAQLQSLLAetqrhlgdVQLKLGEAECRLDQETQLRR---- 586
Cdd:COG3096 480 LVC----KIAGEversqaWQTARELLRR-------YRSQQALAQRLQQ--------LRAQLAELEQRLRQQQNAERllee 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 587 ----------------KEAEEWQQFQADLLMTVRVANDFKTEALSAREQLvldnktqKEKIRLLEQQ----------LEK 640
Cdd:COG3096 541 fcqrigqqldaaeeleELLAELEAQLEELEEQAAEAVEQRSELRQQLEQL-------RARIKELAARapawlaaqdaLER 613
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 665388955 641 LTKQQMQQSETPQSVLSTVQ----REMEMATRRSKLSFSRQ 677
Cdd:COG3096 614 LREQSGEALADSQEVTAAMQqlleREREATVERDELAARKQ 654
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
850-889 |
4.62e-08 |
|
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: 52.24 E-value: 4.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 665388955 850 LLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPD 889
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPD 44
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
264-496 |
5.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 264 ELQATLQELADLQTQLTDTQTENERLAEEKDVLfQSLCRQTEKLNESRTQISTLQELLL--------RDTKQPAPEVSAS 335
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAalrlwfaqRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 ERE-QKLLDLIKTSQEEREAVLLKQEEL--------GAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 406
Cdd:COG4913 301 RAElARLEAELERLEARLDALREELDELeaqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 407 QFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLsrgdktdlsevldvaRKEKDALEERVAELQDQCSRSQAELRRL 486
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDL---------------RRELRELEAEIASLERRKSNIPARLLAL 445
|
250
....*....|...
gi 665388955 487 RDQLS---GLTEE 496
Cdd:COG4913 446 RDALAealGLDEA 458
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
255-691 |
6.31e-08 |
|
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: 56.72 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 255 EETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTL----QELLLRDTKQPAP 330
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLaarkQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 331 EVSASEREQKLldliktsQEEREAVLLKQEELGAELAEMKQAREAGQLE-------LQRQRERIALLDSQLDAANAERRQ 403
Cdd:pfam01576 84 LEEEEERSQQL-------QNEKKKMQQHIQDLEEQLDEEEAARQKLQLEkvtteakIKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 404 GEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVldvarKEKDALEERVAELQDQCSRSQAEL 483
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELE-----KAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 484 RRLRDQLSGLTEECKVV----------KNNAKCAVSHLEYRLEQLQRD-------KDKIAGEWQALEERVAELQVQCKCH 546
Cdd:pfam01576 232 AELRAQLAKKEEELQAAlarleeetaqKNNALKKIRELEAQISELQEDleseraaRNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 547 QEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQ-LRRKEAEEWQQFQADLLMTVRvandFKTEALSAREQLVLDNK 625
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQeMRQKHTQALEELTEQLEQAKR----NKANLEKAKQALESENA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 626 TQKEKIRLLEQ---QLEKLTKQQMQQSETPQSVLSTVQRE-MEMATRRSKLsfsrQDSRLSVKTLIESIE 691
Cdd:pfam01576 388 ELQAELRTLQQakqDSEHKRKKLEGQLQELQARLSESERQrAELAEKLSKL----QSELESVSSLLNEAE 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
339-643 |
8.78e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 339 QKLLDLIKTSQEEREAVLlkQEELGAELAEmKQAREAGQL--ELQRQRERIALLDSQldAANAERRQG--EAQFSQAMEE 414
Cdd:PRK03918 134 QGEIDAILESDESREKVV--RQILGLDDYE-NAYKNLGEVikEIKRRIERLEKFIKR--TENIEELIKekEKELEEVLRE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 415 ISQRAIEISRLSTLLENARSKIEELEAdlSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLT 494
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEE--LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 495 EECKVVKnnakcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSL---LAETQRHLGDVQ--- 568
Cdd:PRK03918 287 ELKEKAE-----EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELkkkLKELEKRLEELEerh 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 569 LKLGEAECRLDQETQLRRKEAEEwqqfqadllmTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTK 643
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGL----------TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
317-496 |
1.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 317 LQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLD--SQL 394
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 395 DAANAERRQGEAQ---FSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEvldvARKEKDALEERVAE 471
Cdd:COG4717 135 EALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----LAEELEELQQRLAE 210
|
170 180
....*....|....*....|....*
gi 665388955 472 LQDQCSRSQAELRRLRDQLSGLTEE 496
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENE 235
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
845-913 |
1.33e-07 |
|
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: 50.79 E-value: 1.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 845 SKRNALLKWCQNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21238 2 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAE 70
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
849-917 |
1.35e-07 |
|
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: 50.56 E-value: 1.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 849 ALLKWCQNKTVGYrNIDITNFSSSWNDGLAFCAILHSYLPDRIPYDQLTPANKRRNFSLAFAAA-ESVGI 917
Cdd:cd21245 7 ALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAqESLGI 75
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
324-657 |
1.73e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 324 DTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRErialldsQLDAANAERRQ 403
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE-------ELKKAEEKKKA 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 404 GEAQFSQAMEEISQRAIEISRlstLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDAL--EERVAELQDQCSRSQA 481
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 482 ELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDkiagewqalEERVAELQVQCKCHQEDKA-QLQSLLAET 560
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE---------DEKKAAEALKKEAEEAKKAeELKKKEAEE 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 561 QRHLGDVQlklGEAECRLDQETQLRRKEAEE---WQQFQADLLMTVRVANDFKTEALSAREqlvldnkTQKEKIRLLEQQ 637
Cdd:PTZ00121 1715 KKKAEELK---KAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEE-------IRKEKEAVIEEE 1784
|
330 340
....*....|....*....|.
gi 665388955 638 L-EKLTKQQMQQSETPQSVLS 657
Cdd:PTZ00121 1785 LdEEDEKRRMEVDKKIKDIFD 1805
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
411-591 |
1.86e-07 |
|
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: 53.00 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 411 AMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQL 490
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELA-----ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 491 SGLTEECKVVKNNAkcavshlEYrlEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLK 570
Cdd:COG1579 76 KKYEEQLGNVRNNK-------EY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
170 180
....*....|....*....|.
gi 665388955 571 LGEAECRLDQETQLRRKEAEE 591
Cdd:COG1579 147 LDEELAELEAELEELEAEREE 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
270-594 |
3.18e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.59 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 270 QELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLlrDTKQPAPEVSASEREQKLLDLIKTSQ 349
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT--VRLQDLTEKLSEAEDMLACEQHALLR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 350 EEREA-----VLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDS-QLDAANAERRQGEAQFSQA--------MEEI 415
Cdd:TIGR00618 620 KLQPEqdlqdVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIrVLPKELLASRQLALQKMQSekeqltywKEML 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 416 SQRAIEISRLSTLLENARSKIEELEADLS------RGDKTDLSEVLDVARKEKD-ALEERVAELQDQCSRSQAELRRLrD 488
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSslgsdlAAREDALNQSLKELMHQARtVLKARTEAHFNNNEEVTAALQTG-A 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 489 QLSGLTEECKVVKNNAKCAVSHLEYRLEQLQrdkdkiagewQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQ 568
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIG----------QEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEIT 848
|
330 340
....*....|....*....|....*.
gi 665388955 569 LKLGEAECRLDQETQLRRKEAEEWQQ 594
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
263-492 |
7.18e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELAD----LQTQLTDTQTENERLAEEkdvlFQSLCRQTEKLNESRTQiSTLQELLLRDTKQPAPEVSASERE 338
Cdd:PRK04863 445 EEFQAKEQEATEellsLEQKLSVAQAAHSQFEQA----YQLVRKIAGEVSRSEAW-DVARELLRRLREQRHLAEQLQQLR 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 339 QKLLDLIKTSQEEREAVLLkQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLdaanAERRQGEAQFSQAMEEISQR 418
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERL-LAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV----SEARERRMALRQQLEQLQAR 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 419 AIEISRLSTLLENARSKIEEL-----EADLSRGDKT----DLSEVLDVARKEKDALEERVAELQDQCSR-------SQAE 482
Cdd:PRK04863 595 IQRLAARAPAWLAAQDALARLreqsgEEFEDSQDVTeymqQLLERERELTVERDELAARKQALDEEIERlsqpggsEDPR 674
|
250
....*....|
gi 665388955 483 LRRLRDQLSG 492
Cdd:PRK04863 675 LNALAERFGG 684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-490 |
7.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVL--FQSLCRQTEKLNESRTQISTLQElLLRDTKQPAPEVSASEREQK 340
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAEREIAELEA-ELERLDASSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 341 LLDL-IKTSQEEREAVLLKQEELGAELAEMKQAREagqlELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQR- 418
Cdd:COG4913 696 ELEAeLEELEEELDELKGEIGRLEKELEQAEEELD----ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENl 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 419 AIEISRLSTLLENARSKIEEL--------EADLSRGDKT--DLSEVLDVARK-EKDALEERVAELQDQC-SRSQAELRRL 486
Cdd:COG4913 772 EERIDALRARLNRAEEELERAmrafnrewPAETADLDADleSLPEYLALLDRlEEDGLPEYEERFKELLnENSIEFVADL 851
|
....
gi 665388955 487 RDQL 490
Cdd:COG4913 852 LSKL 855
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
845-913 |
1.14e-06 |
|
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: 47.76 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 845 SKRNALLKWCQNKTVGyrnIDITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPdWETWDPNDALENATEAMQLAE 67
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-539 |
1.36e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKdvlfQSLCRQTEKLNESRTQISTLQ------ELLLRDTKQPAPEVSasE 336
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEgskrklEEKIRELEERIEELK--K 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 337 REQKLLDLIKTSqEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQL-DAANAERRQGEaqFSQAMEEI 415
Cdd:PRK03918 274 EIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkELEEKEERLEE--LKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 416 SQRAIEISRLSTLLENARSKIEELE---ADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLsg 492
Cdd:PRK03918 351 EKRLEELEERHELYEEAKAKKEELErlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-- 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 665388955 493 ltEECKVVKnnAKCAV-------SHLEYRLEQLQRDKDKIAGEWQALEERVAEL 539
Cdd:PRK03918 429 --EELKKAK--GKCPVcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
260-459 |
1.67e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 260 STNEELQATLQELADLQTQLTDTQTEnerlaeekdvlfqslcrqtekLNESRTQISTLQElLLRDTKQPAPEVSASEREQ 339
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAE---------------------LAEAEARLAALRA-QLGSGPDALPELLQSPVIQ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 340 KLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERI-ALLDSQLDAANAER---RQGEAQFSQAMEEI 415
Cdd:COG3206 267 QLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREaslQAQLAQLEARLAEL 346
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 665388955 416 SQRAIEISRLSTLLENARSKIEEL-----EADLSRGDKTDLSEVLDVAR 459
Cdd:COG3206 347 PELEAELRRLEREVEVARELYESLlqrleEARLAEALTVGNVRVIDPAV 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
247-692 |
1.90e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQatlQELADLQTQLTDTQTENERLAE--------EKDVLFQ----------SLCRQTEKLN 308
Cdd:pfam15921 90 LQRRLNESNELHEKQKFYLR---QSVIDLQTKLQEMQMERDAMADirrresqsQEDLRNQlqntvheleaAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 309 ESRTQISTLQELLLrdtkqpAPEVSASEREQKLLDLIKTSQEE---------------REAVLLKQEELGAELAEMK--- 370
Cdd:pfam15921 167 DSNTQIEQLRKMML------SHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrslGSAISKILRELDTEISYLKgri 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 371 ------------QAREAGQLELQRQRERIALLDSQ--------LDAANAERRQGEA--------------QFSQAMEEIS 416
Cdd:pfam15921 241 fpvedqlealksESQNKIELLLQQHQDRIEQLISEheveitglTEKASSARSQANSiqsqleiiqeqarnQNSMYMRQLS 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 417 QRAIEISRLSTLLENAR----SKIEELEADLSRGDkTDLSEvldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSG 492
Cdd:pfam15921 321 DLESTVSQLRSELREAKrmyeDKIEELEKQLVLAN-SELTE----ARTERDQFSQESGNLDDQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 493 LTEECKVVKNNAkcavSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCkchqedKAQLQSLLAETQRHLGDVQlKLG 572
Cdd:pfam15921 396 EKEQNKRLWDRD----TGNSITIDHLRRELDDRNMEVQRLEALLKAMKSEC------QGQMERQMAAIQGKNESLE-KVS 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 573 EAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFkTEALSAREQLVLDNKTQKEKIRlleqQLEKLTKQQMQQSETP 652
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL-TASLQEKERAIEATNAEITKLR----SRVDLKLQELQHLKNE 539
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 665388955 653 QSVLSTVQREMEMAtrrsKLSFSRQDSRLSVktLIESIEN 692
Cdd:pfam15921 540 GDHLRNVQTECEAL----KLQMAEKDKVIEI--LRQQIEN 573
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
328-542 |
2.69e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 328 PAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQ 407
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 408 FSQAMEEISQRAIEISRLSTLLENarskiEELEADLSRGDKTDL-----SEVLDVARKEKDALEERVAELQDQcsrsQAE 482
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGS-----ESFSDFLDRLSALSKiadadADLLEELKADKAELEAKKAELEAK----LAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 483 LRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQ 542
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-461 |
3.13e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 114 NNKMQELHKQMERFRSE----QMQLETRITELLPYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVvNS 189
Cdd:TIGR02168 676 RREIEELEEKIEELEEKiaelEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL-SK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 190 PLSDAEKhQIIQDSQRLHSSAPASIALPSTHDAhdgtpcLTPDWDKQSSSSEISVACLQDKiiqmEETHYSTNEELQATL 269
Cdd:TIGR02168 755 ELTELEA-EIEELEERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 270 QELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELL-----LRDTKQPAPEVSASERE------ 338
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELeallnERASLEEALALLRSELEelseel 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 339 -------QKLLDLIKTSQEEREAVLLKQEELGAELAEMK-QAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQ 410
Cdd:TIGR02168 904 releskrSELRRELEELREKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665388955 411 -------AMEE---ISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKE 461
Cdd:TIGR02168 984 lgpvnlaAIEEyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
235-498 |
3.19e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.06 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 235 KQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTdtqtENERLAEEKDVLFQSLCRQTEKLN---ESR 311
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILT----EKEALQGKINILEMRLSETDARIKlaaQEK 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 312 TQISTLQELLLRDTKQPAPEvSASEREQKL-----LDLIKTsqeerEAVLLKQ--EELGAELAEMKQAREAgQLELQRQR 384
Cdd:PLN02939 194 IHVEILEEQLEKLRNELLIR-GATEGLCVHslskeLDVLKE-----ENMLLKDdiQFLKAELIEVAETEER-VFKLEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 385 eriALLDSQLdaanaerRQGEAQFSQAMEEISQ---RAIE-----ISRLSTLLENA-----------------RSKIEEL 439
Cdd:PLN02939 267 ---SLLDASL-------RELESKFIVAQEDVSKlspLQYDcwwekVENLQDLLDRAtnqvekaalvldqnqdlRDKVDKL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 440 EADLSRGDKTDLS-EVLDVARKEKDALEERV----AELQDQCSRSQAELRRLRDQLSGLTEECK 498
Cdd:PLN02939 337 EASLKEANVSKFSsYKVELLQQKLKLLEERLqasdHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
150-696 |
5.09e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.49 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 150 KLKGDLVKMQSLQEKSQMEIGN-------LKYENESLRNRLRDVVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHda 222
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDkekqvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDH-- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 223 hdgtpcLTPDWDKQSSSSEISVA---CLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQS 299
Cdd:pfam05483 294 ------LTKELEDIKMSLQRSMStqkALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 300 LCRQTEKlNESRTQISTLQelLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLE 379
Cdd:pfam05483 368 EQQRLEK-NEDQLKIITME--LQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 380 LQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQ---RAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLD 456
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 457 VARKEK------DALEERVAELQDQCSRSQAELRRLRDQLsglteECKVVKN--NAKCAVSHLEYRLEQLQRDKDKIAGE 528
Cdd:pfam05483 525 CKKQEErmlkqiENLEEKEMNLRDELESVREEFIQKGDEV-----KCKLDKSeeNARSIEYEVLKKEKQMKILENKCNNL 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 529 WQALEERVAELQvqcKCHQEDKAQLQSLLAETQR------HLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMT 602
Cdd:pfam05483 600 KKQIENKNKNIE---ELHQENKALKKKGSAENKQlnayeiKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 603 VRVANDFKTEALSAREQLvldNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQ-REMEMATRRSKLSFSRQDSRL 681
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEI---DKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKnKEQEQSSAKAALEIELSNIKA 753
|
570
....*....|....*
gi 665388955 682 SVKTLIESIENNKAQ 696
Cdd:pfam05483 754 ELLSLKKQLEIEKEE 768
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-644 |
5.41e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLlrdtk 326
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 327 qpapevsaSEREQKLLDLIKtsqeEREAVLLKqeELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEA 406
Cdd:TIGR04523 291 --------NQLKSEISDLNN----QKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 407 QFSQAMEEISQRAIEISRL-------STLLENARSKIEELEADLSRGDKTD--LSEVLDVARKEKDALEERVAELQDQCS 477
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLkkenqsyKQEIKNLESQINDLESKIQNQEKLNqqKDEQIKKLQQEKELLEKEIERLKETII 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 478 RSQAELRRLRDQLSGLteecKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQA---------------------LEERV 536
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVK----ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQkqkelkskekelkklneekkeLEEKV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 537 AELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLD-----QETQLRRKEAEEWQQFQADLLmtvrVANDFKT 611
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkenleKEIDEKNKEIEELKQTQKSLK----KKQEEKQ 588
|
410 420 430
....*....|....*....|....*....|...
gi 665388955 612 EALSAREQlvlDNKTQKEKIRLLEQQLEKLTKQ 644
Cdd:TIGR04523 589 ELIDQKEK---EKKDLIKEIEEKEKKISSLEKE 618
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
432-701 |
6.07e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 432 ARSKIEELEADLSRgdktdLSEVLDVARKEKDALE------ERVAELQDQCSRSQAELRRLRDQLsgLTEECKVVKNNAK 505
Cdd:COG1196 177 AERKLEATEENLER-----LEDILGELERQLEPLErqaekaERYRELKEELKELEAELLLLKLRE--LEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 506 cavsHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQckcHQEDKAQLQSLLAETQRHLGDVQLklgeaecrldqETQLR 585
Cdd:COG1196 250 ----ELEAELEELEAELAELEAELEELRLELEELELE---LEEAQAEEYELLAELARLEQDIAR-----------LEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 586 RKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEM 665
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270
....*....|....*....|....*....|....*.
gi 665388955 666 ATRRSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 701
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
337-678 |
6.25e-06 |
|
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: 49.89 E-value: 6.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 337 REQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQR----ERIALLDSQLDAANAERRQGEAQFSQAM 412
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRreleSRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 413 EEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSG 492
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIK-----TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 493 LTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEE---RVAELQVQCkchqEDKAQLQSLLAETQRH---LGD 566
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrKEAENEALL----EELRSLQERLNASERKvegLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 567 VQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRvandfKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQM 646
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALR-----EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEER 333
|
330 340 350
....*....|....*....|....*....|..
gi 665388955 647 QQSETPQSVLSTVQREMEMATRRSKLSFSRQD 678
Cdd:pfam07888 334 LQEERMEREKLEVELGREKDCNRVQLSESRRE 365
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
336-651 |
6.40e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQR---QRERIALLDSQLDAANAERRQGEAQFSQA- 411
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELe 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 412 -------------------MEEISQRAIEISRLSTLLENARSKIEELEADLSR------------GDKTDLSEVLDVARK 460
Cdd:PRK03918 266 erieelkkeieeleekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRleeeingieeriKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 461 EKDALEERVAELQ------DQCSRSQAELRRLRDQLSGLTEEcKVVKNnakcaVSHLEYRLEQLQRDKDKIAGEWQALEE 534
Cdd:PRK03918 346 KLKELEKRLEELEerhelyEEAKAKKEELERLKKRLTGLTPE-KLEKE-----LEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 535 RVAELQ--------VQCKC-------HQEDKAQlqsLLAETQRHLGDVQLKLGEAEcrlDQETQLRRKEAEewqqfqadl 599
Cdd:PRK03918 420 EIKELKkaieelkkAKGKCpvcgrelTEEHRKE---LLEEYTAELKRIEKELKEIE---EKERKLRKELRE--------- 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 665388955 600 lmtvrvandfkTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSET 651
Cdd:PRK03918 485 -----------LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-645 |
6.70e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQ-----------SLCRQTEKLNESRTQISTL---QELLLRDTKQP 328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRrarLEALLAALGLP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 329 APEVSAS--EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAA--------- 397
Cdd:COG4913 375 LPASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaealg 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 398 -----------------NAERRQG----------------EAQFSQAMEEISQRaieisRLSTLLENARSKIEELEADLS 444
Cdd:COG4913 455 ldeaelpfvgelievrpEEERWRGaiervlggfaltllvpPEHYAAALRWVNRL-----HLRGRLVYERVRTGLPDPERP 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 445 RGDKTDLSEVLDVARKE-KDALEERVAELQD-QCSRSQAELRRLRdqlSGLTEECkVVKNNakcavshleYRLEQLQrDK 522
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPfRAWLEAELGRRFDyVCVDSPEELRRHP---RAITRAG-QVKGN---------GTRHEKD-DR 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 523 DKIAGEW----------QALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDqeTQLRRKEAEEW 592
Cdd:COG4913 596 RRIRSRYvlgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAEL 673
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 593 QQFQADLL---MTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQ 645
Cdd:COG4913 674 EAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-519 |
6.90e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 113 ANNKMqELHKQMERFRSEQM--QLETRITELLPYQSEVAKLKGDL-VKMQSLQEKSQ-------MEIGNLKYENESLRNR 182
Cdd:pfam15921 254 SQNKI-ELLLQQHQDRIEQLisEHEVEITGLTEKASSARSQANSIqSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 183 LRD---VVNSPLSDAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSssEISVACLQDKIIQMEETHY 259
Cdd:pfam15921 333 LREakrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREK--ELSLEKEQNKRLWDRDTGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 260 STN-----EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQ-PAPEVS 333
Cdd:pfam15921 411 SITidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEElTAKKMT 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 334 ASEREQKLLDLIKTSQEE--------------REAVLLKQEEL------GAELAEMKQAREAGQLELQRQRERIALLDSQ 393
Cdd:pfam15921 491 LESSERTVSDLTASLQEKeraieatnaeitklRSRVDLKLQELqhlkneGDHLRNVQTECEALKLQMAEKDKVIEILRQQ 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 394 LD-----AANAERRQGEAQFSQAM--EEISQRAIEISRLSTLLENARSKIEELEADLSrgdKTDLSEVldvarKEKDALE 466
Cdd:pfam15921 571 IEnmtqlVGQHGRTAGAMQVEKAQleKEINDRRLELQEFKILKDKKDAKIRELEARVS---DLELEKV-----KLVNAGS 642
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 467 ERVAELQD-QCSRSQA--ELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQ 519
Cdd:pfam15921 643 ERLRAVKDiKQERDQLlnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
261-426 |
8.88e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 49.64 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 261 TNEELQATLQ-ELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQ 339
Cdd:pfam05667 325 TEEELQQQREeELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIA 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 340 KLLDLIKTSqEEREAVLLKQEE-----LGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEE 414
Cdd:pfam05667 405 KLQALVDAS-AQRLVELAGQWEkhrvpLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAE 483
|
170
....*....|..
gi 665388955 415 ISQRAIEISRLS 426
Cdd:pfam05667 484 YERLPKDVSRSA 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
263-484 |
9.07e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTL----QELLLRDTKQPAPEVSASERE 338
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELreraAELEAEAEEKREAAAEAEEEA 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 339 QKLLDLIKTSQEEREAV-------------LLKQEELGAELAEMKQAREA-GQLELQRQ------RERIALLDSQLDAAN 398
Cdd:PRK02224 568 EEAREEVAELNSKLAELkerieslerirtlLAAIADAEDEIERLREKREAlAELNDERRerlaekRERKRELEAEFDEAR 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 399 AER-RQGEAQFSQAMEEISQRAIEISRLSTLLENA----RSKIEELEadlsrgdktDLSEVLDVARKEKDALE---ERVA 470
Cdd:PRK02224 648 IEEaREDKERAEEYLEQVEEKLDELREERDDLQAEigavENELEELE---------ELRERREALENRVEALEalyDEAE 718
|
250
....*....|....
gi 665388955 471 ELQDQCSRSQAELR 484
Cdd:PRK02224 719 ELESMYGDLRAELR 732
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
234-419 |
1.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 234 DKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNE---- 309
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 310 ---SRTQISTLQELLlrDTKQPAPEVS-------ASEREQKLLDLIKTSQEE----REAVLLKQEELGAELAEMKQAREA 375
Cdd:COG3883 95 lyrSGGSVSYLDVLL--GSESFSDFLDrlsalskIADADADLLEELKADKAEleakKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 665388955 376 GQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRA 419
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
270-664 |
1.36e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 270 QELADLQTQLTDTQTENERLAEEKdVLFQSLCRQTEK----LNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLI 345
Cdd:pfam01576 103 QHIQDLEEQLDEEEAARQKLQLEK-VTTEAKIKKLEEdillLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 346 KTSQE----EREAVLLKQEELGAELAEMKQAREAGQLELQRQ-----------RERIALLDSQLDAANAERRQGEAQFSQ 410
Cdd:pfam01576 182 KNKHEamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaelqaqiaelRAQLAKKEEELQAALARLEEETAQKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 411 AMEEISQRAIEISRLSTLLEN---ARSKIEELEADLSR---GDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELR 484
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESeraARNKAEKQRRDLGEeleALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 485 RLRDQLSGLTEeckvvKNNAkcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQlqsllAETQRHL 564
Cdd:pfam01576 342 SHEAQLQEMRQ-----KHTQ--ALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQD-----SEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 565 GDVQLklgeaecrldQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLdnKTQKEkIRLLEQQLEKLtkQ 644
Cdd:pfam01576 410 LEGQL----------QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI--KLSKD-VSSLESQLQDT--Q 474
|
410 420
....*....|....*....|.
gi 665388955 645 QMQQSETPQSV-LSTVQREME 664
Cdd:pfam01576 475 ELLQEETRQKLnLSTRLRQLE 495
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
247-581 |
1.60e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEEL---QATLQELADLQTQLTDTQTENE---RLAEEKDVLFQSLCRQTEKLNESRTQISTLQEL 320
Cdd:COG3096 283 LSERALELRRELFGARRQLaeeQYRLVEMARELEELSARESDLEqdyQAASDHLNLVQTALRQQEKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 321 LlrdtkQPAPEVSASEREQKLldlikTSQEEREAVLLKQEELGAELAEMKQA-----REAGQLELQRQR----------- 384
Cdd:COG3096 363 L-----EEQEEVVEEAAEQLA-----EAEARLEAAEEEVDSLKSQLADYQQAldvqqTRAIQYQQAVQAlekaralcglp 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 385 --------ERIALLDSQLDAANAERRQGE----------AQFSQAMEEISQRAIEISRLST------LLENARS------ 434
Cdd:COG3096 433 dltpenaeDYLAAFRAKEQQATEEVLELEqklsvadaarRQFEKAYELVCKIAGEVERSQAwqtareLLRRYRSqqalaq 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 435 --------------------KIEELEADLSRGDKTDLSEVLDVARkEKDALEERVAELQDQCSRSQA---ELRRLRDQls 491
Cdd:COG3096 513 rlqqlraqlaeleqrlrqqqNAERLLEEFCQRIGQQLDAAEELEE-LLAELEAQLEELEEQAAEAVEqrsELRQQLEQ-- 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 492 glteeckvvknnakcavshleyrLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQL-- 569
Cdd:COG3096 590 -----------------------LRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVer 646
|
410
....*....|...
gi 665388955 570 -KLGEAECRLDQE 581
Cdd:COG3096 647 dELAARKQALESQ 659
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-532 |
1.61e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 118 QELHKQMERFRSEQMQLETRITELlpyQSEVAKLKGDLVKMQSLQEKSQ--MEIGNLKYENESLRNRLRDVvnsplsdAE 195
Cdd:COG4717 91 AELQEELEELEEELEELEAELEEL---REELEKLEKLLQLLPLYQELEAleAELAELPERLEELEERLEEL-------RE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 196 KHQIIQDSQRLHSSAPASIALPSTHdahdgtpcLTPDWDKQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADL 275
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQ--------LSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 276 QTQLTDTQtENERLAEEKDVL--------FQSLCRQTEKLNESRTQISTLQE-----LLLRDTKQPAPEVSASEREQKLL 342
Cdd:COG4717 233 ENELEAAA-LEERLKEARLLLliaaallaLLGLGGSLLSLILTIAGVLFLVLgllalLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 343 DLIKTSQEEREAVL--------LKQEELGAELAEMKQAREAgQLELQRQRERIALLDSQ------LDAANAErrqGEAQF 408
Cdd:COG4717 312 ALEELEEEELEELLaalglppdLSPEELLELLDRIEELQEL-LREAEELEEELQLEELEqeiaalLAEAGVE---DEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 409 SQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRD 488
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 665388955 489 QLsglteeckvvknnakcAVSHLEYRLEQLQRDKDKIAGEWQAL 532
Cdd:COG4717 468 DG----------------ELAELLQELEELKAELRELAEEWAAL 495
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
396-636 |
2.15e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 396 AANAERRQGEAqfSQAMEEISQRaieisrlstlLENARSKIEELEADLS----RGDKTDLSEVLDVARKEKDALEERVAE 471
Cdd:COG3206 163 EQNLELRREEA--RKALEFLEEQ----------LPELRKELEEAEAALEefrqKNGLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 472 LQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAkcAVSHLEYRLEQLQRDKDKIAGEW-------QALEERVAELQvqck 544
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALR---- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 545 chQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQlRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDN 624
Cdd:COG3206 305 --AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA-RLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
250
....*....|..
gi 665388955 625 KTQKEKIRLLEQ 636
Cdd:COG3206 382 ALTVGNVRVIDP 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
235-643 |
2.16e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 235 KQSSSSEISVACLQDKIIQMEETHystnEELQATLQELADLQTQLTDTQ---TENERLAEEKDVLFQSLCRQTEKLNESR 311
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERI----EELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 312 TQISTLQELL--LRDTKQPAPEVSASERE-QKLLDLIKTSQEEREAVLLKQ---------------EELGAELAEMKQAR 373
Cdd:PRK03918 321 EEINGIEERIkeLEEKEERLEELKKKLKElEKRLEELEERHELYEEAKAKKeelerlkkrltgltpEKLEKELEELEKAK 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 374 EAGQLELQRQRERIALLDS---QLDAANAERRQGEAQ----------------FSQAMEEISQRAIEISRLSTLLENARS 434
Cdd:PRK03918 401 EEIEEEISKITARIGELKKeikELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 435 KIEELEADLSRGDK-TDLSEVLDVARKEKDALEERVAElqdQCSRSQAELRRLRDQLSGLTEECKVVKNNAKcAVSHLEY 513
Cdd:PRK03918 481 ELRELEKVLKKESElIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 514 RLEQLQRDKDKIAGEWQALEERVAELQVqcKCHQEDKAQLQSL----------------LAETQRHLGDVQLKLGEAECR 577
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGF--ESVEELEERLKELepfyneylelkdaekeLEREEKELKKLEEELDKAFEE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 578 LDQE-----------TQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLV------LDN-KTQKEKIRLLEQQLE 639
Cdd:PRK03918 635 LAETekrleelrkelEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRReeikktLEKlKEELEEREKAKKELE 714
|
....
gi 665388955 640 KLTK 643
Cdd:PRK03918 715 KLEK 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
118-486 |
2.57e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 118 QELHKQMERFRSEQMQLETRITELL----PYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLSD 193
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEeeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 194 AEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTPDWDKQSSSSEISVAC-----LQDKIIQMEETHYSTNEELQAT 268
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAalaaaLQNIVVEDDEVAAAAIEYLKAA 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 269 LQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTS 348
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 349 QEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 428
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 429 LENARSKIEELEADLSrgdktdlsEVLDVARKEKDALEERVAELQDQCSRSQAELRRL 486
Cdd:COG1196 730 LEAEREELLEELLEEE--------ELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-651 |
2.77e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 269 LQELADLQTQLTDTQTENERLAEEKDVLFQSlcrqTEKLNESRTQISTLQElllrdtkqpapEVSASEREQKLLDLIKTS 348
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELRE-----------ELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 349 QEEREavllKQEELGAELAEMKQAREagqlELQRQRERIALLDSQLDAANAERRQGEAQFSQAME-EISQRAIEISRLST 427
Cdd:COG4717 135 EALEA----ELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 428 LLENARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQAELRR--------LRDQLSGLTEECKV 499
Cdd:COG4717 207 RLAELEEELEEAQEELEE------------LEEELEQLENELEAAALEERLKEARLLLliaaallaLLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 500 VKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLD 579
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 580 QETQLRRK-EAEEWQQFQADLLMTVRVANDfktEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSET 651
Cdd:COG4717 355 EAEELEEElQLEELEQEIAALLAEAGVEDE---EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
255-593 |
3.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 255 EETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQT---------EKLNESRTQISTLQELLLRDT 325
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelaelpERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 326 KQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQ-EELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 404
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 405 EAQ-------------------------------------------FSQAMEEISQRAIEISRLSTLLENARSKIEELEA 441
Cdd:COG4717 247 EARlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 442 DLSRGDKTDLSEVLDVARKEKDaLEERVAELQDQcsRSQAELRRLRDQLSGLTEECKVV--------------KNNAKCA 507
Cdd:COG4717 327 ALGLPPDLSPEELLELLDRIEE-LQELLREAEEL--EEELQLEELEQEIAALLAEAGVEdeeelraaleqaeeYQELKEE 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 508 VSHLEYRLEQL---------QRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRhlgdvQLKLGEAECRL 578
Cdd:COG4717 404 LEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQEL 478
|
410
....*....|....*
gi 665388955 579 DQETQLRRKEAEEWQ 593
Cdd:COG4717 479 EELKAELRELAEEWA 493
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
253-648 |
3.63e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 253 QMEETHYSTNEELQATLQELADLQTQLTDTQ---TENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQEllLRDTKQPA 329
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE--TQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 330 PEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQ---LDAANAERRQGEA 406
Cdd:TIGR00618 290 RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeihIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 407 QFSQAMEE---ISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEvldvarkekDALEERVAELQDQCSRSQAEL 483
Cdd:TIGR00618 370 ISCQQHTLtqhIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAF---------RDLQGQLAHAKKQQELQQRYA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 484 RRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD--KIAGEWQALEERVAELQVQCKC-------HQEDKAQLQ 554
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKKAVVLARLLELQEEPCplcgsciHPNPARQDI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 555 SLLAETQRHLG---DVQLKLGEAECRLDQETQLRRKEA----EEWQQFQADLLMTVRVANDFKTEA--LSAREQLVLD-- 623
Cdd:TIGR00618 521 DNPGPLTRRMQrgeQTYAQLETSEEDVYHQLTSERKQRaslkEQMQEIQQSFSILTQCDNRSKEDIpnLQNITVRLQDlt 600
|
410 420
....*....|....*....|....*
gi 665388955 624 NKTQKEKIRLLEQQLEKLTKQQMQQ 648
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQ 625
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
347-692 |
4.59e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 347 TSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALldsqldAANAERRQG-EAQFSQAMEEISQRAIEISRL 425
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL------VQTALRQQEkIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 426 StllENARSKIEELEADLSRGD------KTDLSEV---LDVARKE-------KDALEervaELQDQCSRSQAELRRLRDQ 489
Cdd:PRK04863 371 V---EEADEQQEENEARAEAAEeevdelKSQLADYqqaLDVQQTRaiqyqqaVQALE----RAKQLCGLPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 490 LSGLTEECKVVKNnakcAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQvqckcHQEDKAQLQSLL--AETQRHLGD- 566
Cdd:PRK04863 444 LEEFQAKEQEATE----ELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVS-----RSEAWDVARELLrrLREQRHLAEq 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 567 ---VQLKLGEAECRLDQETQLRR-------------KEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEK 630
Cdd:PRK04863 515 lqqLRMRLSELEQRLRQQQRAERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665388955 631 IRLLEQQ----------LEKLTKQQMQQSETPQSVLSTVQremEMATRRSKLSFSRQDSRLSVKTLIESIEN 692
Cdd:PRK04863 595 IQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQ---QLLERERELTVERDELAARKQALDEEIER 663
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
830-913 |
4.61e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 43.62 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 830 GERKDPLNmlaKNGGSKRNALLKWCQNKTvgyRNIDITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLA 908
Cdd:cd21315 4 GEDDGPDD---GKGPTPKQRLLGWIQSKV---PDLPITNFTNDWNDGKAIGALVDALAPGLCPdWEDWDPKDAVKNAKEA 77
|
....*
gi 665388955 909 FAAAE 913
Cdd:cd21315 78 MDLAE 82
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
333-691 |
7.11e-05 |
|
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: 46.66 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 333 SASEREQKLldliKTSQEEREAVLLKQEELGAELA---EMKQAREAGQLELQRQ------RERIAL-LDSQLDAANAERR 402
Cdd:pfam17380 283 AVSERQQQE----KFEKMEQERLRQEKEEKAREVErrrKLEEAEKARQAEMDRQaaiyaeQERMAMeRERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 403 QGEaqfsqaMEEISQR--AIEISRLSTLlenarskiEELEADLSRGDKTDLSEvLDVARKEKDALEERVAELQDQcsrsQ 480
Cdd:pfam17380 359 KRE------LERIRQEeiAMEISRMREL--------ERLQMERQQKNERVRQE-LEAARKVKILEEERQRKIQQQ----K 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 481 AELRRLRDQLSglteeckvvknnakcavshlEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAET 560
Cdd:pfam17380 420 VEMEQIRAEQE--------------------EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 561 QRHLGDVQLKLGEAECRLDQETQLRRKEAEEWQQFQAdllmTVRVANDFKTEALSAREQlvlDNKTQKEKIRLLEQQLEK 640
Cdd:pfam17380 480 EKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK----LLEKEMEERQKAIYEEER---RREAEEERRKQQEMEERR 552
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 665388955 641 LTKQQMQQSETPQSVLSTVQREMEMAtrRSKLSFSRQDSRLSVKTLIESIE 691
Cdd:pfam17380 553 RIQEQMRKATEERSRLEAMEREREMM--RQIVESEKARAEYEATTPITTIK 601
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
328-469 |
7.81e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 328 PAPEVSASEREQklldlikTSQEEREAVLLKQ-EELGAELAEMKQareagqlELQRQRERIALLDSQLDAANAERRQGEa 406
Cdd:COG2433 397 AEREKEHEEREL-------TEEEEEIRRLEEQvERLEAEVEELEA-------ELEEKDERIERLERELSEARSEERREI- 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 407 qfsQAMEEISQRAIEISRLSTLLENARSKIEELEADLSR----------GDKTDLSEVLDVARKEKDALEERV 469
Cdd:COG2433 462 ---RKDREISRLDREIERLERELEEERERIEELKRKLERlkelwklehsGELVPVKVVEKFTKEAIRRLEEEY 531
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
866-913 |
7.92e-05 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 42.76 E-value: 7.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 665388955 866 ITNFSSSWNDGLAFCAILHSYLPDRIP-YDQLTPANKRRNFSLAFAAAE 913
Cdd:cd21229 21 ITNFSTDWNDGIALSALLDYCKPGLCPnWRKLDPSNSLENCRRAMDLAK 69
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
305-537 |
2.04e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 305 EKLNESRTQISTLQELLLRDTKqpapEVSASEREQKLLDLIKtsqEEREAVLLKQEELGAELAEM-KQAREAGQLELQRQ 383
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKG----EIKSLKKELEKLEELK---KKLAELEKKLDELEEELAELlKELEELGFESVEEL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 384 RERIALLDS------QLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDV 457
Cdd:PRK03918 591 EERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 458 ARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNnakcavshLEYRLEQLQRDKDKIAgEWQALEERVA 537
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK--------LEKALERVEELREKVK-KYKALLKERA 741
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
344-691 |
2.68e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 344 LIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEIS 423
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 424 RLSTLLENARSKIEELEAdlsrgDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNN 503
Cdd:COG4372 105 SLQEEAEELQEELEELQK-----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 504 AKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQ 583
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 584 LRRKEAEEW---QQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQ 660
Cdd:COG4372 260 IEELELAILvekDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
|
330 340 350
....*....|....*....|....*....|.
gi 665388955 661 REMEMATRRSKLSFSRQDSRLSVKTLIESIE 691
Cdd:COG4372 340 ADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
850-933 |
2.92e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.13 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 850 LLKWC--QNKTVGYRNIDITNFSSSWNDGLAFCAILHSYLPDRIP----YDQLTPANKRRNFSLAFAAAESVGigttlvh 923
Cdd:cd21218 15 LLRWVnyHLKKAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDkelvLEVLSEEDLEKRAEKVLQAAEKLG------- 87
|
90
....*....|
gi 665388955 924 iCTYMLQPKE 933
Cdd:cd21218 88 -CKYFLTPED 96
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
353-495 |
3.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 353 EAVL--LKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLdaanaerrqgeaqfsQAMEEisqraiEISRLSTLLE 430
Cdd:COG2433 379 EEALeeLIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQV---------------ERLEA------EVEELEAELE 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 431 NARSKIEELEADLSRGDKTDLSEVLdvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTE 495
Cdd:COG2433 438 EKDERIERLERELSEARSEERREIR--KDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
271-591 |
3.34e-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: 44.78 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 271 ELADLQTQLTDTQTENERLAeekdvlfQSLCRQTEKLnesrtqistlQELLLRDTKQPAPEVSASEREQKLLDLIKTSQE 350
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELR-------AQLAKKEEEL----------QAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 351 E-------REAVLLKQEELGAELAEMKQARE------AGQLELQRQRER-IALLDSQLDAanaERRQGEAQF-------S 409
Cdd:pfam01576 279 DleseraaRNKAEKQRRDLGEELEALKTELEdtldttAAQQELRSKREQeVTELKKALEE---ETRSHEAQLqemrqkhT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 410 QAMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKdALEERVAELQDQCSRSQAELRRLRDQ 489
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRK-KLEGQLQELQARLSESERQRAELAEK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 490 LSGLTEECKVVKNNAKCA----------VSHLEYRL----EQLQ---RDKDKIAGEWQALEERVAELQVQCKCHQEDKAQ 552
Cdd:pfam01576 435 LSKLQSELESVSSLLNEAegkniklskdVSSLESQLqdtqELLQeetRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRN 514
|
330 340 350
....*....|....*....|....*....|....*....
gi 665388955 553 LQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKEAEE 591
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
276-661 |
3.47e-04 |
|
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: 44.34 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 276 QTQLTDTQTENERLAEEKDVLFQSLCRQtEKLNESRTqistlqelllrdTKQPAPEVSAS-EREQKLLDLiktsQEEREA 354
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEKEEKAREVERR-RKLEEAEK------------ARQAEMDRQAAiYAEQERMAM----EREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 355 VLLKQEELGAELAEMKQAREAGQLELQRQRERIALldsqldaanaERRQGEAQFSQAMEeisqraieisrlstllenARS 434
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELERLQM----------ERQQKNERVRQELE------------------AAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 435 KIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRsqaELRRLRDQLSGLTEECKVVknnakcavshleyR 514
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR---EMERVRLEEQERQQQVERL-------------R 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 515 LEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAE------TQRHLGDVQLKLGEAECRLDQETQLRR-K 587
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEerkrklLEKEMEERQKAIYEEERRREAEEERRKqQ 546
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 588 EAEEWQQFQADLLMTvrvandfkTEALSAREQLvldnktQKEKiRLLEQQLEKLTKQQMQQSETPQSVLSTVQR 661
Cdd:pfam17380 547 EMEERRRIQEQMRKA--------TEERSRLEAM------ERER-EMMRQIVESEKARAEYEATTPITTIKPIYR 605
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
359-650 |
3.79e-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: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 359 QEELGAELAEMKQAreagqleLQRQRERIALLDSQLDAANAerrqgeaqfsqameEISQRAIEISRLSTLLENARskiee 438
Cdd:pfam12128 599 EEELRERLDKAEEA-------LQSAREKQAAAEEQLVQANG--------------ELEKASREETFARTALKNAR----- 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 439 leadlsrgdkTDLSEVLDVARKEKDALEERVAELQDQCSRS----QAELRRLRDQLSGLTEECKVVKNNAKCAvsHLEYR 514
Cdd:pfam12128 653 ----------LDLRRLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDKKHQAWLEEQKEQKREARTE--KQAYW 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 515 LEQLQRDKDKIAGEWQALEERVAELQVQCK-CHQEDKAQLQSL------LAETQRHLGDVQLKLGEAECRLDQETQLRRK 587
Cdd:pfam12128 721 QVVEGALDAQLALLKAAIAARRSGAKAELKaLETWYKRDLASLgvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFDW 800
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 588 EAEEWQQFQADLLMTVRvanDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 650
Cdd:pfam12128 801 YQETWLQRRPRLATQLS---NIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSE 860
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
283-701 |
4.66e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 283 QTENERLAEEKdvlfqslcRQTEKLNESRTQISTLQELLLR--DTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQE 360
Cdd:PTZ00121 1291 KADEAKKAEEK--------KKADEAKKKAEEAKKADEAKKKaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 361 ELGAELAEMKQAREAGQL--------------ELQRQRERIALLDSQLDAANAERRQGE-----AQFSQAMEEISQRAIE 421
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKAdaakkkaeekkkadEAKKKAEEDKKKADELKKAAAAKKKADeakkkAEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 422 ISRLSTL---------LENARSKIEEL--------------EADLSRGDKTDLSEVLDVARK----EKDALEERVAELQD 474
Cdd:PTZ00121 1443 AKKADEAkkkaeeakkAEEAKKKAEEAkkadeakkkaeeakKADEAKKKAEEAKKKADEAKKaaeaKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 475 QCSRS-QAELRRLRDQLSGLTEECKV--VKNNAKCAVSHLEYRLEQLQR-DKDKIAGEWQALEERVAE----LQVQCKCH 546
Cdd:PTZ00121 1523 KADEAkKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAEEAKKaEEDKNMALRKAEEAKKAEeariEEVMKLYE 1602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 547 QEDKAQLQSLLAETQRHLGDVQLKLGEAECRldQETQLRRKEAEEWQqfQADLLMTVRVANDFKTEALSAREQlvlDNKT 626
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAE---EDKK 1675
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 627 QKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAqgKADE 701
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK--KAEE 1748
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
361-518 |
4.81e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.21 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 361 ELGAELAEMKQAREagqlelqRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQraiEISRLSTLLENARSKIEELE 440
Cdd:pfam09787 44 ALTLELEELRQERD-------LLREEIQKLRGQIQQLRTELQELEAQQQEEAESSRE---QLQELEEQLATERSARREAE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665388955 441 ADLSRgdktdLSEVLDVARKEkdaLEERVAELQDQCSRSQAELRRLRDQLSglteeckvVKNNAKCAVSHLEYRLEQL 518
Cdd:pfam09787 114 AELER-----LQEELRYLEEE---LRRSKATLQSRIKDREAEIEKLRNQLT--------SKSQSSSSQSELENRLHQL 175
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
258-472 |
4.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 258 HYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLfQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASER 337
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL-AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 338 EQKLLDliktsQEEREAVLLKQEELGAELAEMKQAREAGQLElQRQRERialLDSQLDAANAERRQGEAQFSQAMEEISQ 417
Cdd:COG4913 728 ELDELQ-----DRLEAAEDLARLELRALLEERFAAALGDAVE-RELREN---LEERIDALRARLNRAEEELERAMRAFNR 798
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665388955 418 R-------------AIE--ISRLSTL----LENARSKIEELEADLSRGDKTDLSEVLDVARKEkdaLEERVAEL 472
Cdd:COG4913 799 EwpaetadldadleSLPeyLALLDRLeedgLPEYEERFKELLNENSIEFVADLLSKLRRAIRE---IKERIDPL 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-696 |
5.35e-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: 43.89 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 467 ERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCH 546
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 547 QEDKAQLQSLLAETQRHLGDVQLKLGEaecrLDQETQLRRKEAEEWQQFQADLLMTVRVANDfktealsAREQLVLDNKT 626
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANEISRLEQQKQILRE-------RLANLERQLEE 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 627 QKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATRRSKLSFSRQDSRLSVKTLIESIENNKAQ 696
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
349-701 |
5.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 349 QEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTL 428
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 429 LENARSKIEELEADLSRgdktdlsevldvARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEckvvknnakcaV 508
Cdd:COG4372 89 LQAAQAELAQAQEELES------------LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE-----------I 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 509 SHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAECRLDQETQLRRKE 588
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 589 AEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSETPQSVLSTVQREMEMATR 668
Cdd:COG4372 226 SLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLA 305
|
330 340 350
....*....|....*....|....*....|...
gi 665388955 669 RSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 701
Cdd:COG4372 306 ALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
264-701 |
7.74e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 264 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTqistlqelllrdtkqpaPEVSASEREQKLLD 343
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLES-----------------GDDSGTPGGKKYLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 344 L---IKTSQEE-------REAVLLKQEELGAELAEMKQAREagqlELQRQRERIALLDSQLDaanaerrqgeaqfsqAME 413
Cdd:pfam05622 64 LqkqLEQLQEEnfrletaRDDYRIKCEELEKEVLELQHRNE----ELTSLAEEAQALKDEMD---------------ILR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 414 EISQRAieiSRLSTLLENARSKIEELeADLSRGDKTdLSEVLDVARKEKDALEE---RVAELQDQCSRSQAELRRLRDQL 490
Cdd:pfam05622 125 ESSDKV---KKLEATVETYKKKLEDL-GDLRRQVKL-LEERNAEYMQRTLQLEEelkKANALRGQLETYKRQVQELHGKL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 491 SglTEECKVVKnnAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELqvqcKCHQEDKAQLQSLLAETQRHLGDVQ-- 568
Cdd:pfam05622 200 S--EESKKADK--LEFEYKKLEEKLEALQKEKERLIIERDTLRETNEEL----RCAQLQQAELSQADALLSPSSDPGDnl 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 569 ------LKLGEAECRLDQETQ-LRRKEAEEWQQFQADLLMTVRVANdfktealSAREQLVLDNKTQKEKIRLLEQQLEKL 641
Cdd:pfam05622 272 aaeimpAEIREKLIRLQHENKmLRLGQEGSYRERLTELQQLLEDAN-------RRKNELETQNRLANQRILELQQQVEEL 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665388955 642 TK-QQMQQSETPQSVLSTVQREMEMATRRsKLSFSRQDSRLSVKTLIESIENNKAQgKADE 701
Cdd:pfam05622 345 QKaLQEQGSKAEDSSLLKQKLEEHLEKLH-EAQSELQKKKEQIEELEPKQDSNLAQ-KIDE 403
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
336-490 |
8.12e-04 |
|
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: 42.22 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 336 EREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERrqgeaQFSQAMEEI 415
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 416 SQRAIEISRLSTLLENARSKIEELEADLSRgDKTDLSEVLDVARKEKDALEERVAELQDQcsrsQAELRRLRDQL 490
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAE-LEAELAELEAELEEKKAELDEELAELEAE----LEELEAEREEL 168
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
343-651 |
1.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 343 DLIKTSQEEREAVLLKQEELGAELAEMKQAreagQLELQRQRERIALLDSQLDA------ANAERRQgeAQFSQAMEEIS 416
Cdd:COG5185 205 NSIKESETGNLGSESTLLEKAKEIINIEEA----LKGFQDPESELEDLAQTSDKleklveQNTDLRL--EKLGENAESSK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 417 QRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEE 496
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 497 CKVVKNNaKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQVQC-----------KCHQEDKAQLQSLLAETQRHLG 565
Cdd:COG5185 359 IKEEIEN-IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAqeilatledtlKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 566 DVQLKLGEAECRLDQETQLRRKEAEEWQQFQADLLM-TVRVANDFKTEALSAREQLVLDNKTQKEKIRL-LEQQLEKLTK 643
Cdd:COG5185 438 EVSKLLNELISELNKVMREADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAkLERQLEGVRS 517
|
....*...
gi 665388955 644 QQMQQSET 651
Cdd:COG5185 518 KLDQVAES 525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
365-575 |
1.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 365 ELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLS 444
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 445 R-GDKTDLSEVLDVARKEKDALeervaelqdqcSRSQAeLRRLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKD 523
Cdd:COG3883 97 RsGGSVSYLDVLLGSESFSDFL-----------DRLSA-LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 665388955 524 KIAGEWQALEERVAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEAE 575
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
247-487 |
1.20e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 247 LQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELL--LRD 324
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELdeLRK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 325 TKQPAPEVSASERE-----QKLLDLIKTS----QEEREaVLLKQEELGAELAEMKQAREagqlelqrqrerialLDSQLD 395
Cdd:COG1340 100 ELAELNKAGGSIDKlrkeiERLEWRQQTEvlspEEEKE-LVEKIKELEKELEKAKKALE---------------KNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 396 AANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEEL--EADLSRGDKTDLSEVLDVARKEKDALEERVAELQ 473
Cdd:COG1340 164 ELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELrkEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250
....*....|....
gi 665388955 474 DQCSRSQAELRRLR 487
Cdd:COG1340 244 KELKKLRKKQRALK 257
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
262-540 |
1.26e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 262 NEELQATLQELADLQTQLTDTQTENER----LAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASER 337
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRarieLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 338 EQKLLDLIKTSQEEREAVLLKQEE----LGAELAEMKQAREAGQLELQRQRERIALLDSQLDaanaerrqgeaQFSQAME 413
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREviscLKNELSELRRQIQRAELELQSTNSELEELQERLD-----------LLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 414 EISQRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVLDVARKEkdalEERVAELqdqcsrsQAELRRLRD---QL 490
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS--QEQDSEIVKNSKSE----LARIPEL-------EKELERLREhnkHL 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 665388955 491 SGLTEECKVVKNNakcaVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ 540
Cdd:pfam05557 217 NENIENKLLLKEE----VEDLKRKLEREEKYREEAATLELEKEKLEQELQ 262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
262-447 |
1.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 262 NEELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEV----SASER 337
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeleSLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 338 EQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAE-RRQGEAQFSQAMEEIS 416
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQElQALSEAEAEQALDELL 189
|
170 180 190
....*....|....*....|....*....|.
gi 665388955 417 QRAIEISRLSTLLENARSKIEELEADLSRGD 447
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
118-434 |
1.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 118 QELHKQMERFRSEQMQLETRITELL-----PYQSEVAKLKGDLVKMQSLQEKSQMEIGNLKYENESLRNRLRDVVNSPLS 192
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLeqlslATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 193 DAEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPCLTP-------------------DWDKQSSSSEISVACLQDKIIQ 253
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflllareKASLGKEAEELQALPALEELEE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 254 ME-------------------ETHYSTNEELQATLQELADLQTQLT--DTQTENERLAEEKDV----LFQSLCRQTEKLN 308
Cdd:COG4717 319 EEleellaalglppdlspeelLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVedeeELRAALEQAEEYQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 309 ESRTQISTLQELL---LRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGqlELQRQRE 385
Cdd:COG4717 399 ELKEELEELEEQLeelLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG--ELAELLQ 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 665388955 386 RIALLDSQLDAAnAERRQGEAQFSQAMEEISQRAIEiSRLSTLLENARS 434
Cdd:COG4717 477 ELEELKAELREL-AEEWAALKLALELLEEAREEYRE-ERLPPVLERASE 523
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
334-478 |
1.56e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 334 ASEREQKLLDLIKTSQEEREAVLLK-QEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAM 412
Cdd:PRK12705 32 AKEAERILQEAQKEAEEKLEAALLEaKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEERE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 413 EEISQRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVLDVARKEK----DALEERVAELQDQCSR 478
Cdd:PRK12705 112 KALSARELELEELEKQLDNELYRVAGLTPEQAR--KLLLKLLDAELEEEKaqrvKKIEEEADLEAERKAQ 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
333-644 |
1.59e-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: 42.26 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 333 SASEREQKLLDLIKTSQEEREAVLL---------KQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQ 403
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQLALMEfakkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 404 GEAQFSQAMEEISQRaieiSRLSTLLENARSKIEELEADLSRGDKTdlSEVLDVARKEKDALE--ERVAELQDQCSRSQA 481
Cdd:TIGR00618 241 SHAYLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEET--QERINRARKAAPLAAhiKAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 482 ELR-RLRDQLSGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQ-----------ALEERVAELQvQCKCHQED 549
Cdd:TIGR00618 315 ELQsKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsireiscqqhTLTQHIHTLQ-QQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 550 KAQLQSLLAETQRHLGDVQLKLGEAECRLDQetQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTqKE 629
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQG--QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KE 470
|
330
....*....|....*
gi 665388955 630 KIRLLeQQLEKLTKQ 644
Cdd:TIGR00618 471 REQQL-QTKEQIHLQ 484
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
263-418 |
1.74e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDvlfqslcRQTEKLNESRTQISTLQELL--LRDTKqpapEVSASEREQK 340
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIK-------RLELEIEEVEARIKKYEEQLgnVRNNK----EYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 341 LLDLIKTSQEEREAVLLKQ-EELGAELAEMKQAREAGQLELQRQRERialLDSQLDAANAERRQGEAQFSQAMEEISQR 418
Cdd:COG1579 100 SLKRRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
264-444 |
2.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 264 ELQATLQELADLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQISTLqELLLRDTKQpapevsASEREQKLLD 343
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEA------RIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 344 LIKTSQEereavllkQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQFSQAMEEISQraiEIS 423
Cdd:COG1579 84 NVRNNKE--------YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELA 152
|
170 180
....*....|....*....|.
gi 665388955 424 RLSTLLENARSKIEELEADLS 444
Cdd:COG1579 153 ELEAELEELEAEREELAAKIP 173
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
321-591 |
2.16e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 321 LLRDTKQPAPEVSASEREQKLLDL---IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAA 397
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLYEKEIEDLrrqLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 398 NAERRQGEAQFSQAMEEIS-QRAIEISRLSTLLENARSKIEELEADLSRgdKTDLSEVL--------DVARKEKDALEE- 467
Cdd:pfam00038 116 TLARVDLEAKIESLKEELAfLKKNHEEEVRELQAQVSDTQVNVEMDAAR--KLDLTSALaeiraqyeEIAAKNREEAEEw 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 468 ---RVAELQDQCSRSQAELRrlrdqlsglteeckvvknNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQ---- 540
Cdd:pfam00038 194 yqsKLEELQQAAARNGDALR------------------SAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEerye 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 541 VQCKCHQ----EDKAQLQSLLAETQRHLGDVQLKLgEAECRLDQETQLRRK--EAEE 591
Cdd:pfam00038 256 LQLADYQelisELEAELQETRQEMARQLREYQELL-NVKLALDIEIATYRKllEGEE 311
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
235-404 |
2.55e-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: 41.29 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 235 KQSSSSEISVACLQDKIIQMEETHYSTNEELQATLQELADLQTQLTDTQTENERLAEE----------------KDVLF- 297
Cdd:COG4942 48 KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaellralyrlgrqppLALLLs 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 298 ------------------QSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEEREAVLLKQ 359
Cdd:COG4942 128 pedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 665388955 360 E-ELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQG 404
Cdd:COG4942 208 LaELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
295-492 |
2.84e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 295 VLFQSLCRQTEKLNESRTQISTLQELLlrdtkqpapevsASEREQK--LLDLIKTSQEEREAVLLKQEELGAELAEMKQA 372
Cdd:PRK09039 43 FLSREISGKDSALDRLNSQIAELADLL------------SLERQGNqdLQDSVANLRASLSAAEAERSRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 373 REAGQlelqrqrERIALLDSQLDAANAERRQGEAQFSQAMEEISQRAIEISRLSTLLENARSKIEELEADLSrgdktDLS 452
Cdd:PRK09039 111 GAAAE-------GRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIA-----DLG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 665388955 453 EVLDVarkekdALEERVAELQdqcsRSQAE-LRRLRDQLSG 492
Cdd:PRK09039 179 RRLNV------ALAQRVQELN----RYRSEfFGRLREILGD 209
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
116-701 |
2.96e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 116 KMQELHKQMERFRSEQMQ-LETRITELLPY-QSEVAKLKGDLVKMQSlqeksqmEIGNLKYENESLRNRLRDVVNSPLSD 193
Cdd:TIGR00606 280 QMEKDNSELELKMEKVFQgTDEQLNDLYHNhQRTVREKERELVDCQR-------ELEKLNKERRLLNQEKTELLVEQGRL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 194 AEKHQIIQDSQRLHSSAPASIALPSTHDAHDGTPcltpdwdkqssSSEISVACLQDKIIQMEEthystnEELQATLQELA 273
Cdd:TIGR00606 353 QLQADRHQEHIRARDSLIQSLATRLELDGFERGP-----------FSERQIKNFHTLVIERQE------DEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 274 DLQTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQistlqellLRDTKQPAPEVSASEREqklldliktsqeere 353
Cdd:TIGR00606 416 DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE--------LKFVIKELQQLEGSSDR--------------- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 354 aVLLKQEELGAELAEMKQAREAGQLELQRQRErIALLDSQLDAANAERRQgeaqfSQAMEEISQRAIEISRLSTLLENAR 433
Cdd:TIGR00606 473 -ILELDQELRKAERELSKAEKNSLTETLKKEV-KSLQNEKADLDRKLRKL-----DQEMEQLNHHTTTRTQMEMLTKDKM 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 434 SKIEELEADLSRGD------------KTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 501
Cdd:TIGR00606 546 DKDEQIRKIKSRHSdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 502 NN--AKCAVSHLEYRLEQLQRDKDKIAGEW-----------QALEERVAELQVQCK-CHQEDKAQlqsllAETQRHLGDV 567
Cdd:TIGR00606 626 DKlfDVCGSQDEESDLERLKEEIEKSSKQRamlagatavysQFITQLTDENQSCCPvCQRVFQTE-----AELQEFISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 568 QLKLGEAECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQL-VLDNKTQKEKIRLLEQqlEKLTKQQM 646
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLKNDIEEQ--ETLLGTIM 778
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 665388955 647 QQSETPQSVLS--TVQREMEMATRRSKLSFSRQDSRLSVKTLIESIE--NNKAQGKADE 701
Cdd:TIGR00606 779 PEEESAKVCLTdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHE 837
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
260-646 |
3.39e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 260 STNEELQATLQELADL-QTQLTDTQTENERLAEEKDVLFQSLCRQTEKLNESRTQIStlqelllrdtkqpapevsasere 338
Cdd:COG5185 250 QTSDKLEKLVEQNTDLrLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID----------------------- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 339 qklldlIKTSQEEREAVlLKQEELGAELAEMKQAREAGqleLQRQRERIALLDSQLDAANAERRQGEAQFSqAMEEISQR 418
Cdd:COG5185 307 ------IKKATESLEEQ-LAAAEAEQELEESKRETETG---IQNLTAEIEQGQESLTENLEAIKEEIENIV-GEVELSKS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 419 AIEISRLSTLLENARSKIEELEADLSRGDKtdlsEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEEC- 497
Cdd:COG5185 376 SEELDSFKDTIESTKESLDEIPQNQRGYAQ----EILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELn 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 498 KVVKNNAKCAVSHLEYRLEQLQRD----KDKIAGEWQALEERVAELqvqckchqedKAQLQSLLAETQRHLGDVQLKLGE 573
Cdd:COG5185 452 KVMREADEESQSRLEEAYDEINRSvrskKEDLNEELTQIESRVSTL----------KATLEKLRAKLERQLEGVRSKLDQ 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665388955 574 AECRLDQETQLRRKEAEEWQQFQADLLMTVRVANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQM 646
Cdd:COG5185 522 VAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQA 594
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
456-668 |
4.04e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 456 DVARKEKDALEERVAELQDQCSRSQAELRRLRDQ--LSGLTEECKVVKNNakcaVSHLEYRLEQLQRDKDKIAGEWQALE 533
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQ----LSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 534 ERVAELQVQCKCHQEDKA--QLQSLLAETQRHLGDVQLKLGEAECRLdqeTQLRRKEAEEWQQFQAdllMTVRVANDFKT 611
Cdd:COG3206 247 AQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSARYTPNHPDV---IALRAQIAALRAQLQQ---EAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 665388955 612 EALSAREQLvldnktqkekiRLLEQQLEKLTKQQMQQSETpQSVLSTVQREMEMATR 668
Cdd:COG3206 321 ELEALQARE-----------ASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARE 365
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
345-505 |
4.29e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 345 IKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAanAERRQGEAQfsQAMEEISQRAIEISR 424
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELER--TEERLAEAL--EKLEEAEKAADESER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 425 LSTLLENARSKIEELEADLsrgdKTDLSEVLDVARKEKDALEE---RVAELQDQCSRSQAELRRLRDQLSGLTEECKVVK 501
Cdd:pfam00261 79 GRKVLENRALKDEEKMEIL----EAQLKEAKEIAEEADRKYEEvarKLVVVEGDLERAEERAELAESKIVELEEELKVVG 154
|
....
gi 665388955 502 NNAK 505
Cdd:pfam00261 155 NNLK 158
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
415-627 |
4.56e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 40.74 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 415 ISQRAIEISRLSTLLENARSKIEELEadlsrgDKTDLSEVLDVARKEKdALEErvaELQDQCSRSQAELRRLRDQLSGLT 494
Cdd:PRK10361 11 IALVGVAIGWLFASYQHAQQKAEQLA------EREEMVAELSAAKQQI-TQSE---HWRAECELLNNEVRSLQSINTSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 495 EECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAElQVQCKCHQEDKAQLQSLLAETQRHLGDVQLKLGEA 574
Cdd:PRK10361 81 ADLREVTTRMEAAQQHADDKIRQMINSEQRLSEQFENLANRIFE-HSNRRVDEQNRQSLNSLLSPLREQLDGFRRQVQDS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 665388955 575 ecrLDQETQLRRKEAEEWQQFQadllmtvRVANDFKTEALSAREQLVLDNKTQ 627
Cdd:PRK10361 160 ---FGKEAQERHTLAHEIRNLQ-------QLNAQMAQEAINLTRALKGDNKTQ 202
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-630 |
4.84e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 331 EVSASEREQKLLDLIKTSQEEREAVLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERRQGEAQfsQ 410
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK--K 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 411 AMEEISQRAIEISRLSTLLENARSKIEELEADLSRGDKTDLSEVLDVARKEKDALEERVAELqdqcSRSQAELRRLRDQL 490
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE----AKKKAEEAKKADEA 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 491 SGLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERvAELQVQCKCHQEDKAQLQSLLAETQRHLGDVQLK 570
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665388955 571 LGEAECRLDQ--ETQLRRKEAEEWQQFQADllmtVRVANDFKTEALSAREQLVLDNKTQKEK 630
Cdd:PTZ00121 1400 AEEDKKKADElkKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADEAKKKAEEAK 1457
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
263-491 |
5.25e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 263 EELQATLQELADLQTQLTDTQTENERLAEEKDVLfqslcrqteklnesRTQISTLQELllrdtkQPAP-EVSASEREQKL 341
Cdd:COG0497 158 EEYREAYRAWRALKKELEELRADEAERARELDLL--------------RFQLEELEAA------ALQPgEEEELEEERRR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 342 L----DLIKTSQEEREAvlLKQEELGAeLAEMKQAReagqlelqRQRERIALLDSQLDAAnaerrqgeaqfSQAMEEIsq 417
Cdd:COG0497 218 LsnaeKLREALQEALEA--LSGGEGGA-LDLLGQAL--------RALERLAEYDPSLAEL-----------AERLESA-- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 418 rAIEISRLSTLLENARSKIE----ELEA---------DLSRGDKTDLSEVLDVARK------EKDALEERVAELQDQCSR 478
Cdd:COG0497 274 -LIELEEAASELRRYLDSLEfdpeRLEEveerlallrRLARKYGVTVEELLAYAEElraelaELENSDERLEELEAELAE 352
|
250
....*....|...
gi 665388955 479 SQAELRRLRDQLS 491
Cdd:COG0497 353 AEAELLEAAEKLS 365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
288-491 |
5.58e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 288 RLAEEKDVLFQSLCRQTEKLNESRTQISTLQELLLRDTKQPAPEVSASEREQKLLDLIKTSQEE--REAVLLKQEE---- 361
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEekKKAEELKKAEeenk 1660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 362 -LGAELA-----EMKQAREAGQLELQRQRERIALLDSQLDAANAER-RQGEAQFSQAMEEISQ----RAIEISRLSTLLE 430
Cdd:PTZ00121 1661 iKAAEEAkkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKaeeeNKIKAEEAKKEAE 1740
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665388955 431 NARSKIEELEADLSRGDK-----TDLSEVLDVARKEKDALEERVAELQDQCSRSQAElRRLRDQLS 491
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKiahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD-KKIKDIFD 1805
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
332-643 |
7.75e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 39.41 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 332 VSASEREQKLLDLIKTSQEEREAvLLKQEELGAELAEMKQAREAGQLELQRQRERIALLDSQLDAANAERrqgeAQFSQA 411
Cdd:pfam15905 49 TPATARKVKSLELKKKSQKNLKE-SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREK----TSLSAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 412 MEEISQRAIEISRLSTLLenarskieeleadlsrgdKTDLSEvlDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLS 491
Cdd:pfam15905 124 VASLEKQLLELTRVNELL------------------KAKFSE--DGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGME 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 492 GLTEECKVVKNNAKCAVSHLEYRLEQLQRDKDKIAGEWQALEERVAELQV---QCKCHQEDKAQLQSLLAETQRHLGDVQ 568
Cdd:pfam15905 184 GKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCvseQVEKYKLDIAQLEELLKEKNDEIESLK 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665388955 569 LKLGEAECRLDQETQLRRKEAEEWQQFQADLLmtvrvandfkTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTK 643
Cdd:pfam15905 264 QSLEEKEQELSKQIKDLNEKCKLLESEKEELL----------REYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
434-539 |
8.15e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 434 SKIEELEADLsrgdkTDLSEVLDVARKEKDALEERVAELQDQCSRSQAELRRLRDQLSGLTEECKvvknNAKCAVSHLEY 513
Cdd:COG4026 128 PEYNELREEL-----LELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFD----NIKSEYSDLKS 198
|
90 100
....*....|....*....|....*.
gi 665388955 514 RLEQLqrdKDKIAGEWQALEERVAEL 539
Cdd:COG4026 199 RFEEL---LKKRLLEVFSLEELWKEL 221
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
426-701 |
8.69e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 426 STLLENARSKIEELEADLSRGDKT-DLSEVLDVARKEKDALE--------------ERVAELQDQCSRSQAELRRLRDQL 490
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPEsELEDLAQTSDKLEKLVEqntdlrleklgenaESSKRLNENANNLIKQFENTKEKI 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 491 SGLTEECKVVKnnakcavsHLEYRLEQLQRdkdkiAGEWQALEERVAELQvqckchqEDKAQLQSLLAETQRHLGDVQLK 570
Cdd:COG5185 299 AEYTKSIDIKK--------ATESLEEQLAA-----AEAEQELEESKRETE-------TGIQNLTAEIEQGQESLTENLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665388955 571 LGEAECRLDQETQLRRKEAEewqqfqadllmtvrvANDFKTEALSAREQLVLDNKTQKEKIRLLEQQLEKLTKQQMQQSE 650
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEE---------------LDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIE 423
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 665388955 651 TPQSVLSTVQREMEMAtrrSKLSFSRQDSRLSVKTLIESIENNKAQGKADE 701
Cdd:COG5185 424 ELQRQIEQATSSNEEV---SKLLNELISELNKVMREADEESQSRLEEAYDE 471
|
|
| |
