|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
34-138 |
3.40e-72 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 238.07 E-value: 3.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 34 DAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIRLVNI 113
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1397727989 114 RSDEIVDGNPKLTLGLIWTIILHFQ 138
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
151-255 |
1.67e-70 |
|
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: 233.44 E-value: 1.67e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
22-147 |
1.21e-59 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 203.29 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRDTDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALD 101
Cdd:cd21236 3 YENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALD 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727989 102 YLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIILHFQISDVVVPGQ 147
Cdd:cd21236 83 YLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
31-149 |
1.05e-57 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 197.17 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 31 DERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIRL 110
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHFQISDVVVPGQED 149
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
31-147 |
5.29e-51 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 178.30 E-value: 5.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 31 DERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIRL 110
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHFQISDVVVPGQ 147
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGE 117
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
36-297 |
7.63e-50 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 191.31 E-value: 7.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGL-RIIDLFDDLRDGHNLISLLEVLAHDILPR--ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:COG5069 9 VQKKTFTKWTNEKLISGGQkEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHFQISDvvVPGQEDISAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHR 191
Cdd:COG5069 89 IGPQDIVDGNPKLILGLIWSLISRLTIAT--INEEGELTKHINLLLWCDEDTGGYkPEVDTFDFFRSWRDGLAFSALIHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 192 NRPDLIDFR--QARSNSNKQNLELAFTVAEKEFGVTRLLDPEDV-DVPNPDEKSILTYVSSLYDVFPQVPSVEQSLRDNE 268
Cdd:COG5069 167 SRPDTLDPNvlDLQKKNKALNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYIIRFGLLEKIDIALHRVY 246
|
250 260 270
....*....|....*....|....*....|....
gi 1397727989 269 RQLKVEEYRDLA-----SSLLRWLSDVTVFMQNR 297
Cdd:COG5069 247 RLLEADETLIQLrlpyeIILLRLLNLIHLKQANW 280
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
151-254 |
1.27e-47 |
|
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: 167.97 E-value: 1.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYYHYF 105
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
151-255 |
5.26e-47 |
|
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: 166.32 E-value: 5.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 230
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
151-255 |
1.12e-45 |
|
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: 162.49 E-value: 1.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21243 5 GAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLDP 84
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21243 85 EDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
151-254 |
3.08e-45 |
|
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: 161.02 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYYHYF 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
150-255 |
6.74e-45 |
|
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: 160.19 E-value: 6.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 150 ISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
149-255 |
1.25e-44 |
|
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: 159.44 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 149 DISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLL 228
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1397727989 229 DPEDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
22-135 |
1.59e-44 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 159.45 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRD-TDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIA 99
Cdd:cd21246 1 FERSRIKAlADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1397727989 100 LDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21246 81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
36-139 |
9.34e-44 |
|
first 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 links 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 156.77 E-value: 9.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRII-DLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIRLVNIR 114
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKPPIkDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1397727989 115 SDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
139-254 |
1.17e-43 |
|
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: 157.14 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 139 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 218
Cdd:cd21216 1 IQDISV---EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727989 219 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21216 78 EKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHAF 114
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
22-135 |
3.73e-42 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 152.84 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRD-TDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIA 99
Cdd:cd21193 1 FEKGRIRAlQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1397727989 100 LDYLRLKgIRLVNIRSDEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21193 81 LAFLKTK-VRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
151-254 |
1.26e-41 |
|
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: 150.78 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21249 4 SAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLDP 83
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21249 84 EDVAVPHPDERSIMTYVSLYYHYF 107
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
147-257 |
2.92e-41 |
|
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: 150.16 E-value: 2.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 147 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTR 226
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 227 LLDPEDVDVPNPDEKSILTYVSSLYDVFPQV 257
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFYHYFSKM 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
151-255 |
8.54e-40 |
|
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: 145.64 E-value: 8.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21192 3 SAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLEV 82
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21192 83 EDVLVDKPDERSIMTYVSQFLRMFP 107
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
32-139 |
1.10e-39 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 145.60 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAVQKKTFTKWVNKHLMKAG--LRIIDLFDDLRDGHNLISLLEVLAHDILPRERG-HM-RFHKIQNVQIALDYLRLKG 107
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKppMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGrRLkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1397727989 108 IRLVNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
37-135 |
5.23e-39 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 143.30 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIALDYLRLKGIRLVNIRS 115
Cdd:cd21214 6 QRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVSIGA 85
|
90 100
....*....|....*....|
gi 1397727989 116 DEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21214 86 EEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
22-135 |
6.36e-39 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 144.40 E-value: 6.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRD-TDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIA 99
Cdd:cd21318 23 FECSRIKAlADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKA 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 1397727989 100 LDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21318 103 LQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
150-248 |
9.04e-39 |
|
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: 142.67 E-value: 9.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 150 ISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1397727989 230 PEDVDVPNPDEKSILTYVS 248
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
22-135 |
1.38e-38 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 143.27 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRD-TDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIA 99
Cdd:cd21317 16 FERSRIKAlADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKA 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1397727989 100 LDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21317 96 LQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
10866-10933 |
1.52e-38 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 140.42 E-value: 1.52e-38
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 10866 IQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 10933
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCR 68
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
147-260 |
5.04e-38 |
|
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: 140.96 E-value: 5.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 147 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTR 226
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|....
gi 1397727989 227 LLDPEDVDVPNPDEKSILTYVSSLYDVFPQVPSV 260
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKAL 114
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
156-255 |
2.69e-37 |
|
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: 138.33 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 156 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 235
Cdd:cd21187 5 LLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDVNV 84
|
90 100
....*....|....*....|
gi 1397727989 236 PNPDEKSILTYVSSLYDVFP 255
Cdd:cd21187 85 EQPDKKSILMYVTSLFQVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
151-254 |
6.53e-37 |
|
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: 137.48 E-value: 6.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21253 1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDA 80
|
90 100
....*....|....*....|....*
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21253 81 EDmVALKVPDKLSILTYVSQYYNYF 105
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
32-139 |
2.11e-36 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 136.16 E-value: 2.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAVQKKTFTKWVNKHLMK--AGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHM--RFHKIQNVQIALDYLRLKG 107
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1397727989 108 IRLVNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
147-260 |
5.53e-36 |
|
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: 135.57 E-value: 5.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 147 QEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQ-ARSNSNkQNLELAFTVAEKEFGVT 225
Cdd:cd21322 13 RETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKlTKSNAT-YNLQQAFNTAEQHLGLT 91
|
90 100 110
....*....|....*....|....*....|....*
gi 1397727989 226 RLLDPEDVDVPNPDEKSILTYVSSLYDVFPQVPSV 260
Cdd:cd21322 92 KLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKAL 126
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
10864-10933 |
6.74e-36 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 133.34 E-value: 6.74e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10864 ELIQDEVRRQVCKCTCIKQFRIHKIGEGKYRFGDSQKLRLVRILRSTVMVRVGGGWVALDEFLVKNDPCR 10933
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCR 70
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
139-254 |
9.84e-36 |
|
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: 134.19 E-value: 9.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 139 ISDVvvpGQEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 218
Cdd:cd21291 1 IADI---NEEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727989 219 EKEFGVTRLLDPEDV-DVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21291 78 SKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
35-137 |
5.17e-35 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 132.14 E-value: 5.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR--ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21215 3 DVQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTN 82
|
90 100
....*....|....*....|....*
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21215 83 IGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
151-257 |
4.88e-34 |
|
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: 129.45 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|....*..
gi 1397727989 231 EDVDVPNPDEKSILTYVSSLYDVFPQV 257
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYYHYFSKM 108
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
32-139 |
6.04e-34 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 129.18 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAVQKKTFTKWVNKHLMK--AGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIR 109
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKhsPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1397727989 110 LVNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
31-139 |
8.77e-34 |
|
first 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. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 128.50 E-value: 8.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 31 DERDAVQKKTFTKWVNKHLMKAGLRII-DLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIR 109
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKPPIeDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1397727989 110 LVNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
154-254 |
2.55e-33 |
|
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: 127.02 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 154 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPED- 232
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|..
gi 1397727989 233 VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEAF 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10157-10367 |
4.75e-33 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 130.26 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10157 FHGELNKFISWLTDTEKTLNNLQPVSRLvERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyFSQKQDVVLIKNLLS 10236
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10237 SIQHRWEKIVSRSAERTRHLERGYKEAKQFNDTWkDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQP 10316
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 10317 VYDGVNKAGRLLKERCPSDDVPTIQAMLTELKSHWNNVCSKSVDRQRKLEE 10367
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
152-254 |
1.02e-32 |
|
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: 125.34 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 152 AREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 231
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 1397727989 232 D-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21197 81 DmVTMHVPDRLSIITYVSQYYNHF 104
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
152-254 |
6.57e-31 |
|
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: 120.36 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 152 AREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 231
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|....
gi 1397727989 232 D-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
22-135 |
8.33e-31 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 121.69 E-value: 8.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 22 YEEARLRD-TDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNVQIA 99
Cdd:cd21316 38 FERSRIKAlADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKA 117
|
90 100 110
....*....|....*....|....*....|....*.
gi 1397727989 100 LDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIIL 135
Cdd:cd21316 118 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
24-140 |
1.10e-30 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 120.25 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 24 EARLRDTDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR--ERGHMRFHKIQNVQIALD 101
Cdd:cd21311 3 ERDLAEDAQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKfnKRPTFRSQKLENVSVALK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1397727989 102 YLRL-KGIRLVNIRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21311 83 FLEEdEGIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
152-255 |
1.99e-30 |
|
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: 118.74 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 152 AREALLLWSRRTTEGYpGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPE 231
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1397727989 232 DVDVPNPDEKSILTYVSSLYDVFP 255
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
151-254 |
2.40e-30 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 118.68 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 230
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPN-PDEKSILTYVSSLYDVF 254
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIRAHF 104
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
36-139 |
5.05e-30 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 117.77 E-value: 5.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR--ERGHMRFHKIQNVQIALDYLRLKGIRLVNI 113
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1397727989 114 RSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
35-139 |
1.32e-29 |
|
first 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 first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 116.65 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAGL-RIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRFHKIQNVQIALDYLRLKGIRLVNI 113
Cdd:cd21232 1 DVQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNI 80
|
90 100
....*....|....*....|....*.
gi 1397727989 114 RSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21232 81 GGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
154-254 |
2.34e-29 |
|
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: 115.64 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 154 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDV 233
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1397727989 234 DVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
36-137 |
3.01e-29 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 115.66 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR---ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21183 4 IQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLVN 83
|
90 100
....*....|....*....|....*
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21183 84 IGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10262-10476 |
5.20e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 118.70 E-value: 5.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10262 EAKQFNDTWKDLITWLIEAEKTLeTETSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQ 10341
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10342 AMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDaLLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELG 10421
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 10422 ARTTTIAFLQKSAKEIISRAEGDVC-SLQSDLIELNAAWDRVCKLSVSKQDRLEHA 10476
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10374-10584 |
5.94e-29 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 118.70 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10374 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 10453
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10454 ELNAAWDRVCKLSVSKQDRLEHAQRLAEEFHkKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEA 10533
Cdd:cd00176 83 ELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 10534 NLRETLNIGQDIMKRCHPDSVPIMKQWLSVIRARWEELTALGRQRSARLSN 10584
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
156-261 |
5.98e-29 |
|
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: 114.64 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 156 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNK-QNLELAFTVAEKEFGVTRLLDPEDVD 234
Cdd:cd21233 5 LLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPEDVA 84
|
90 100
....*....|....*....|....*..
gi 1397727989 235 VPNPDEKSILTYVSSLYDVFPQVPSVE 261
Cdd:cd21233 85 TAHPDKKSILMYVTSLFQVLPQQVSIE 111
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
139-263 |
4.03e-28 |
|
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: 112.90 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 139 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 218
Cdd:cd21289 1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727989 219 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVFPQVPSVEQS 263
Cdd:cd21289 78 EKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHAFAGAEQAETA 123
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
36-137 |
5.41e-28 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 111.81 E-value: 5.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR---ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21228 4 IQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLVS 83
|
90 100
....*....|....*....|....*
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21228 84 IDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
139-254 |
1.77e-27 |
|
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: 111.33 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 139 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 218
Cdd:cd21287 1 IQDISV---EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVA 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727989 219 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21287 78 EKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF 114
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
137-254 |
2.07e-27 |
|
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: 110.95 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 137 FQISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFT 216
Cdd:cd21290 2 FAIQDISV---EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFE 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1397727989 217 VAEKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21290 79 VAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF 117
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
156-255 |
7.14e-27 |
|
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: 108.51 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 156 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 235
Cdd:cd21234 5 LLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPEDVAV 84
|
90 100
....*....|....*....|
gi 1397727989 236 PNPDEKSILTYVSSLYDVFP 255
Cdd:cd21234 85 QLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
32-141 |
9.36e-27 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 108.82 E-value: 9.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAVQKKTFTKWVNKHLMKAG--LRIIDLFDDLRDGHNLISLLEVLA-HDILPRER-GHMRFHKIQNVQIALDYLRLKG 107
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNppLEVKDLFVDIQDGKILMALLEVLSgQNLLQEYKpSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1397727989 108 IRLVNIRSDEIVDGNPKLTLGLIWTIILHFQISD 141
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
139-263 |
1.75e-26 |
|
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: 108.24 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 139 ISDVVVpgqEDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVA 218
Cdd:cd21288 1 IQDISV---EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727989 219 EKEFGVTRLLDPED-VDVPNPDEKSILTYVSSLYDVFPQVPSVEQS 263
Cdd:cd21288 78 EKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHAFAGAEQAETA 123
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
36-140 |
2.25e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 108.19 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRE---RGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21310 16 IQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLVS 95
|
90 100
....*....|....*....|....*...
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21310 96 IDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
151-251 |
2.37e-26 |
|
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: 107.04 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1397727989 231 EDVDV--PNPDEKSILTYVSSLY 251
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9938-10150 |
4.79e-26 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 110.23 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9938 QFDHAHKELKNWMDLVDVTLDEITPVyGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMtSEGIAQAQGLKTKM 10017
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10018 EDMEKTWENIQAKSRAKQDMLEDGLREAQgFTGELQDILAKINDIEGQLIiSKPVGGLPETAKEQLEKFMDVYAELEKLE 10097
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1397727989 10098 PQVQSLNVMGEKLGGKSKGPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDA 10150
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9497-9715 |
7.46e-26 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 109.84 E-value: 7.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9497 ARHFHEAHTELVVWLDDVEPVLSELDVLSvDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQS 9576
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9577 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQsAEFTDKLENMLDTLTvTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEM 9656
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDL-QQFFRDADDLEQWLE-EKEAALASEDLGKDLESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 9657 RHNALESVKNAAEELLRqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETL 9715
Cdd:cd00176 158 HEPRLKSLNELAEELLE---EGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
21-139 |
8.39e-26 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 106.38 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 21 QYEEARLRDTDE-RDAVQKKTFTKWVNKHLMK--AGLRIIDLFDDLRDGHNLISLLEVLAHDILPR-ERGHMRFHKIQNV 96
Cdd:cd21247 4 EYEKGHIRKLQEqRMTMQKKTFTKWMNNVFSKngAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1397727989 97 QIALDYLRLKgIRLVNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:cd21247 84 SKAITFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
151-255 |
2.24e-25 |
|
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: 104.68 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGY-PGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSN--SNKQNLELAFTVAEKEFGVTR- 226
Cdd:pfam00307 2 ELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPKv 81
|
90 100
....*....|....*....|....*....
gi 1397727989 227 LLDPEDVDvpNPDEKSILTYVSSLYDVFP 255
Cdd:pfam00307 82 LIEPEDLV--EGDNKSVLTYLASLFRRFQ 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9068-9281 |
3.78e-25 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 107.53 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9068 KFQDAMASLLDWLAETEELVAMQKAPSPEQrVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 9147
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9148 QQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDpLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHE 9227
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9228 PAMKQLATAGKKLQDYCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAL 9281
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10044-10257 |
6.99e-25 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 106.76 E-value: 6.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10044 EAQGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLGgKSKGPALANLR 10123
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKE-ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLI-EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10124 QNLQHLNQRCDYIRSRACDRKKKLEDAEGMATNFHgELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDIS 10203
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 10204 KHREAMVALEKMGTHLKYFSQKQDVVLIKNLLSSIQHRWEKIVSRSAERTRHLE 10257
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
151-254 |
9.09e-25 |
|
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: 102.82 E-value: 9.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 230
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAES-VGIPTTLTI 86
|
90 100
....*....|....*....|....*
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21199 87 DEmVSMERPDWQSVMSYVTAIYKHF 111
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
148-254 |
3.97e-24 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 101.18 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 148 EDISAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRL 227
Cdd:cd21251 2 ESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISPI 81
|
90 100
....*....|....*....|....*...
gi 1397727989 228 LDPEDV-DVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21251 82 MTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
151-254 |
5.09e-24 |
|
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: 100.63 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 230
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|....*
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQLRAHF 104
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
35-139 |
1.10e-23 |
|
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: 99.67 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAG--LRIIDLFDDLRDGHNLISLLEVLAHD-ILPRERGHMRFHKIQNVQIALDYLRLK-GIRL 110
Cdd:pfam00307 1 LELEKELLRWINSHLAEYGpgVRVTNFTTDLRDGLALCALLNKLAPGlVDKKKLNKSEFDKLENINLALDVAEKKlGVPK 80
|
90 100
....*....|....*....|....*....
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHFQI 139
Cdd:pfam00307 81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
156-254 |
1.11e-23 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 99.73 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 156 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLD-PEDVD 234
Cdd:cd21195 9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
|
90 100
....*....|....*....|
gi 1397727989 235 VPNPDEKSILTYVSSLYDVF 254
Cdd:cd21195 89 AQEPDKLSMVMYLSKFYELF 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8521-8735 |
5.57e-23 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 101.37 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8521 QAEKFEADCKELLTWISEAANNLQESEPlSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAI 8600
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP--DAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8601 ADKVGELQGEWTRLQQEVTVQDSRLTMAgSHAQQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEM 8680
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 8681 MKKSHDRERLNSEGTSLVE-CVDSGKEAIKQQVAVINERWDAVNKALSERASHLED 8735
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEeGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
10479-10668 |
2.95e-22 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 99.44 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10479 LAEEFHKKAQQLLSWLADAERQLHYRGPIPDEEpLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSVPImK 10558
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLE-SVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10559 QWLSVIRARWEELTALGRQRSARLSNGLTDLRHNNvLLEDLLAWLNNAEmtlADVDRQTIPQDMAIIQQLIKEHQDFQNE 10638
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKE---AALASEDLGKDLESVEELLKKHKELEEE 154
|
170 180 190
....*....|....*....|....*....|
gi 1397727989 10639 MSSRQPDVDRLTKADKRRPSSVTQDSLSHI 10668
Cdd:cd00176 155 LEAHEPRLKSLNELAEELLEEGHPDADEEI 184
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
151-256 |
3.75e-22 |
|
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: 95.44 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|....*..
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVFPQ 256
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFYRCLVQ 107
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
36-140 |
5.89e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 95.54 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR---ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21308 20 IQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLVS 99
|
90 100
....*....|....*....|....*...
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21308 100 IDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
36-140 |
7.12e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 95.53 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPR---ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21309 17 IQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLVS 96
|
90 100
....*....|....*....|....*...
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21309 97 IDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8194-8405 |
1.24e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 97.52 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8194 FMQDMQDILQWLDLKDHETDSAQPlPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQQL 8273
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH--PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8274 QELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEqQLTLWLAQKDRMLDVLGPVAMEPNmLASQMEQVKVLREELSAQE 8353
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLES-VEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 8354 PTYDHFLNCAHGILERCGDKSQDGIAvsRRLDTVSKAWNKLQSRLNERSKNL 8405
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIE--EKLEELNERWEELLELAEERQKKL 209
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
151-252 |
1.96e-21 |
|
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: 93.11 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVDV--PNPDEKSILTYVSSLYD 252
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
39-136 |
2.26e-21 |
|
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: 92.76 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 39 KTFTKWVNKHLMKAG-LRIIDLFDDLRDGHNLISLLEVLAHDILPR---ERGHMRFHKIQNVQIALDYLRLKGIRLVNIR 114
Cdd:smart00033 1 KTLLRWVNSLLAEYDkPPVTNFSSDLKDGVALCALLNSLSPGLVDKkkvAASLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1397727989 115 SDEIVDGnPKLTLGLIWTIILH 136
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8956-9170 |
2.95e-21 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 96.36 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8956 QHLTQALNLVWGDIDKASSTLDAMGPaGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLE 9035
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEAL-EAELAAHEERVEALNELGEQLIEEGHPDAEE--IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9036 TDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMaSLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVT 9115
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESV-EELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 9116 DRTPSMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEE 9170
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
156-254 |
3.19e-21 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 92.64 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 156 LLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDV 235
Cdd:cd21250 9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88
|
90 100
....*....|....*....|
gi 1397727989 236 PN-PDEKSILTYVSSLYDVF 254
Cdd:cd21250 89 AEePDKLSMVMYLSKFYELF 108
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
151-249 |
4.68e-21 |
|
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: 91.91 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21184 1 SGKSLLLEWVNSKI---PEYKVKNFTTDWNDGKALAALVDALKPGLIpDNESLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1397727989 230 PEDVDVPNPDEKSILTYVSS 249
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
151-254 |
7.79e-21 |
|
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: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKeFGVTRLLDP 230
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|....*
gi 1397727989 231 EDVDVPN-PDEKSILTYVSSLYDVF 254
Cdd:cd21254 80 SDMVLLAvPDKLTVMTYLYQIRAHF 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
151-252 |
1.35e-20 |
|
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: 90.88 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVDV--PNPDEKSILTYVSSLYD 252
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9390-9603 |
1.41e-20 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 94.43 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9390 EVVNELGDLVDWFVDADSRLQNQQPIaSDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAmEDNSAIRNKM 9469
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9470 DELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHtELVVWLDDVEPVLSELDVLSvDADQVKKQQEKAKVLKQEVADRK 9549
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9550 PIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAM 9603
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9718-9933 |
1.74e-20 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 94.05 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9718 AEKFWDELHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMvGTTEQPEVQK 9797
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9798 NVDDAGASLAAISDQYSKRSQELESALAQAVHFQDqLMKLLVWLQEAEDEFSEFEPVASEfETIKKQWDELKNFKTRVEP 9877
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDL-ESVEELLKKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 9878 KNVEIESLNQHVTELTKSSTPEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMAL 9933
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9826-10040 |
1.80e-20 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 94.05 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9826 QAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEfETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSStPEQASVLR 9905
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9906 EPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHkELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDIT 9985
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 9986 AHQESVESISKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQAKSRAKQDMLED 10040
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
151-254 |
7.54e-20 |
|
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: 88.93 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 230
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|....*
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIYKYF 111
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
154-250 |
8.50e-20 |
|
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: 88.14 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 154 EALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSN----KQNLELAFTVAEKEFGVTRLLD 229
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSL 250
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9608-9824 |
1.02e-19 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 92.12 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9608 EFTDKLENMLDTLTVTAEQVRSAEPISAqPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEavkdVR 9687
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE----IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9688 QKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDeLHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIE 9767
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 9768 ASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESAL 9824
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
153-251 |
1.57e-19 |
|
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: 88.22 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 153 REALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPED 232
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1397727989 233 -VDVPNPDEKSILTYVSSLY 251
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
151-254 |
2.26e-19 |
|
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: 87.82 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEkEFGVTRLLDP 230
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|....*
gi 1397727989 231 ED-VDVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIYKYF 117
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
793-857 |
6.38e-19 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 84.62 E-value: 6.38e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 793 PLSLRAQPVRSPLRLRTLCSCHLPEVNLQRGEECFLISNSQLVKWRIKTLKGIETECPSVCLLIP 857
Cdd:pfam17902 1 PLKQRRSPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
619-785 |
1.36e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 88.66 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 619 LSEFLQGATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLM 698
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 699 ASLQARWSWLLQLVTCLDAHLKHTIAHNQFFEEARHCEQWMARHTELLQNRFARDNIpmEQAELLIRELQELQEQLREYE 778
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDL--ESVEELLKKHKELEEELEAHE 159
|
....*..
gi 1397727989 779 RRIASLT 785
Cdd:cd00176 160 PRLKSLN 166
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
37-137 |
4.98e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.40 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNKHLMKAGLR--IIDLFDDLRDGHNLISLLEVLAHDILPR--ERGHMRFHKIQNVQIALDYLRLKGIRLVN 112
Cdd:cd21212 1 EIEIYTDWANHYLEKGGHKriITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1397727989 113 IRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8878-9776 |
9.12e-18 |
|
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: 93.20 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8878 AELGSQLadmkDFLTRLGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQH 8957
Cdd:TIGR02168 196 NELERQL----KSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8958 LTQALNLVWGDIDKASSTLDAmgpaggnvttVKALQEEL---KGFVKSTMEPLQKQFESVSRQGQALIKTAV-AGSNTTG 9033
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELYA----------LANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9034 LETDLESLAERWAGLVEKVAEHEKnldsallrtgKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKM 9113
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEA----------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9114 VTDRtpsMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAAN 9193
Cdd:TIGR02168 412 LEDR---RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9194 KRFTALEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQL------------ATAGKKLQDY-CKGEDVIMiqlKIDGVQ 9260
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELisvdegyeaaieAALGGRLQAVvVENLNAAK---KAIAFL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9261 KQNGELRSHIedcleqMEEALPLAKHFQEAHAEFLSWASKVepelraleLGVPDEetnIEELANQLTEEMQPLLdiinse 9340
Cdd:TIGR02168 566 KQNELGRVTF------LPLDSIKGTEIQGNDREILKNIEGF--------LGVAKD---LVKFDPKLRKALSYLL------ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9341 gaelaevapgdAGLRVediinrdnkrFDNLRDQIEKRAQKVQLARqrsseVVNELGDLV--DWFVDADSRLQNQQPIA-- 9416
Cdd:TIGR02168 623 -----------GGVLV----------VDDLDNALELAKKLRPGYR-----IVTLDGDLVrpGGVITGGSAKTNSSILErr 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9417 SDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSaIRNKMDELKQWVDTVSgsaNERQSLLEQAVPF 9496
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLE---AEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9497 ARHFHEAHTELVVWLDDVEpvlSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALvamcgSKGAEQVQS 9576
Cdd:TIGR02168 753 SKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-----NEEAANLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9577 MLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAepiSAQPDKLREQIEENKAMEEDLEM 9656
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL---LNERASLEEALALLRSELEELSE 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9657 RHNALESVKNAAEELLrqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGR-QRALEETLAVAEKFWDELHALNSSLKDL 9735
Cdd:TIGR02168 902 ELRELESKRSELRREL----EELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1397727989 9736 QEALSS---VDQPALEP-EAIREQQEELEALKEDIEASQADFEEV 9776
Cdd:TIGR02168 978 ENKIKElgpVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8556-9375 |
2.89e-17 |
|
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: 91.66 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8556 LREQMRQNRTLQQELSLKEpeIRQLLEKGDKL-VKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQ 8634
Cdd:TIGR02168 215 YKELKAELRELELALLVLR--LEELREELEELqEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8635 FTERLDKMAMWLQMTEEKLEKmkpedvdqntVVHKLKELQG-VQNEMMKKSHDRERLNsegtslvecvdsgkeAIKQQVA 8713
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLAN----------LERQLEELEAqLEELESKLDELAEELA---------------ELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8714 VINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNslglsakdpKHINRIKDLLEDtgwLASQ 8793
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---------NEIERLEARLER---LEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8794 LNNTETMLNSIEVD---------GGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELE 8864
Cdd:TIGR02168 416 RERLQQEIEELLKKleeaelkelQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8865 SELGSKTPVSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQASSLC--NAGY--VSDPELLKSQVEALSNqhaSLTER 8940
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALggRLQAvvVENLNAAKKAIAFLKQ---NELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8941 ATQRQSDVVANQHSIQHLTQALNLVWG------DIDKASSTLD-AMGPAGGNVTTVKALQE--ELKGFVKSTMEPLQKQF 9011
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRkALSYLLGGVLVVDDLDNalELAKKLRPGYRIVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9012 ESVSRQGQALIKTAVAGSNTTGLETDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETE-ELVAMQ 9090
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9091 KAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVVDRTAIL 9168
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeIEELEAQIEQLKEELKALREALDELRAEL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9169 EEVQGLAGEFQDVLDPLTTWLDAANKRFTALEPHSPDAEG--------IEHLIQELKKLQKEVNEHEPAMKQLATAGKKL 9240
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieslaaeIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9241 QD--YCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFlswASKVEPELRALELGVPDEETN 9318
Cdd:TIGR02168 893 RSelEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEE 969
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 9319 IEELANQLTEEMQPLldiinsegaelaevapGDAGLRVEDIINRDNKRFDNLRDQIE 9375
Cdd:TIGR02168 970 ARRRLKRLENKIKEL----------------GPVNLAAIEEYEELKERYDFLTAQKE 1010
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8448-8625 |
3.75e-17 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 84.42 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8448 KQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKtdLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEa 8527
Cdd:cd00176 37 ALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE--IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFR- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8528 DCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPTTEvRAIADKVGEL 8607
Cdd:cd00176 114 DADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDAD-EEIEEKLEEL 191
|
170
....*....|....*...
gi 1397727989 8608 QGEWTRLQQEVTVQDSRL 8625
Cdd:cd00176 192 NERWEELLELAEERQKKL 209
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7687-7908 |
9.74e-17 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 83.26 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7687 KHRQFNDVAFKLLTWLTDMEGQLSSvkqDAGLSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNSLSGQAAEq 7766
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSS---TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7767 qqvakLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMnELVSWMDSAEQVVTTQLPISLRrPELNAQLQSFS 7846
Cdd:cd00176 77 -----IQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDL-ESVEELLKKHK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 7847 AVDADVTNHQSALDAVKALANELVKTCELDIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEE 7908
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9174-9382 |
1.44e-16 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 82.88 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9174 LAGEFQDVLDPLTTWLDAANKRFTALEPhSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDVIMIQ 9253
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9254 LKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHaEFLSWASKVEPELRALELGvpDEETNIEELANQL------T 9327
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLG--KDLESVEELLKKHkeleeeL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 9328 EEMQPLLDIINSEGAELAEVAPGDAGLRVEDIINRDNKRFDNLRDQIEKRAQKVQ 9382
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9355-10103 |
1.50e-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: 88.96 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9355 RVEDIINRDNKRFDNLRDQIEKrAQKVQLARQRSSEVvnELGDLVDWFVDADSRLQNqqpiasdldlLQQQLAEQKVMNE 9434
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQAEK-AERYKELKAELREL--ELALLVLRLEELREELEE----------LQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9435 EINNQKVKardtlsaskkllSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFAR-HFHEAHTELVVWLDD 9513
Cdd:TIGR02168 257 ELTAELQE------------LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILReRLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9514 VEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRkpiVDRLNKTgtalvamcgskgAEQVQSMLDDDNRRMDNVRTKVR 9593
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAE---LEELEAE------------LEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9594 DRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSA--EPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEEL 9671
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9672 LRQAGDEQDEAVKDVRQKLEELTKLyKDIQERGRGRQRALEETLAVAEKF-------WDELH-----------ALNSSL- 9732
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISvdegyeaaieaALGGRLq 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9733 ----KDLQEALSSVDQPA---------LEPEAIREQqeELEALKEDIEASQADF-----------EEVQQTGDTLLG--- 9785
Cdd:TIGR02168 549 avvvENLNAAKKAIAFLKqnelgrvtfLPLDSIKGT--EIQGNDREILKNIEGFlgvakdlvkfdPKLRKALSYLLGgvl 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9786 ----------------------------------MVGTTEQP-----EVQKNVDDAGASLAAISDQYSKRSQELESALAQ 9826
Cdd:TIGR02168 627 vvddldnalelakklrpgyrivtldgdlvrpggvITGGSAKTnssilERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9827 AVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQW-DELKNFKTRVEPKNVEIESLNQHVTEL--TKSSTPEQASV 9903
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLeERIAQLSKELTELEAEIEELEERLEEAeeELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9904 LREPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHKELKNWMDLVDVTLDEITPVYGDPKLVEIELAK-LRIVQN 9982
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAeIEELEE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9983 DITAHQESVESISKEaqRLMTSEGIAQAQGLKTKMEDMEKTWEN----IQAKSRAKQDMLEDGLREAQGFTGELQDILAK 10058
Cdd:TIGR02168 867 LIEELESELEALLNE--RASLEEALALLRSELEELSEELRELESkrseLRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1397727989 10059 IND---IEGQLIISKPVGGLPETAKeqlekfmdVYAELEKLEPQVQSL 10103
Cdd:TIGR02168 945 LSEeysLTLEEAEALENKIEDDEEE--------ARRRLKRLENKIKEL 984
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8154-8298 |
3.37e-16 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 81.72 E-value: 3.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8154 DDLSEVQQQLLDITQRYEIVGERLADRQQELQLMLtSIRTFMQDMQDILQWLDLKDHETDSaQPLPTNEKDAKKRLKEHE 8233
Cdd:cd00176 72 PDAEEIQERLEELNQRWEELRELAEERRQRLEEAL-DLQQFFRDADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHK 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 8234 VFHREILSKEGLVEDIRKKAQDLLKTRHGVPGEEmLQQQLQELDDKWHGLRALSEQQRKGLEDMV 8298
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
38-135 |
3.80e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 78.15 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 38 KKTFTKWVNKHLMKAGLRII-DLFDDLRDGHNLISLLEVLAHDILPRERGH--MRFHKIQNVQIALDYLRLKGI-RLVNI 113
Cdd:cd00014 1 EEELLKWINEVLGEELPVSItDLFESLRDGVLLCKLINKLSPGSIPKINKKpkSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1397727989 114 RSDEIV-DGNPKLTLGLIWTIIL 135
Cdd:cd00014 81 EPEDLYeKGNLKKVLGTLWALAL 103
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10265-10366 |
1.69e-15 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 76.21 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10265 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 10344
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 10345 TELKSHWNNVCSKSVDRQRKLE 10366
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9034-9778 |
1.74e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9034 LETDLESLaERWAGLVEKVAEHEKNLDSALLR--TGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQ 9111
Cdd:TIGR02168 198 LERQLKSL-ERQAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9112 KMVTDRTPSMKAVQDSGNQLITGLDpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDA 9191
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLE-QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9192 ANKRFTALEPHSPDAEGIEH---------------LIQELKKLQKEVNEHEPAMKQLATAGKKLQDYCKGEDVIMIQLKI 9256
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEeleeqletlrskvaqLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9257 DGVQKQNGELRSHIED---CLEQMEEALP-LAKHFQEAHAEFLSWASKVE---PELRALE------LGVPDEETNIEELA 9323
Cdd:TIGR02168 436 KELQAELEELEEELEElqeELERLEEALEeLREELEEAEQALDAAERELAqlqARLDSLErlqenlEGFSEGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9324 NQLTEEMQPLLDIINS-EGAELA-EVApgdAGLRVEDII-NRDNKRFDNLRDQIEKRAQKV----------QLARQRSSE 9390
Cdd:TIGR02168 516 SGLSGILGVLSELISVdEGYEAAiEAA---LGGRLQAVVvENLNAAKKAIAFLKQNELGRVtflpldsikgTEIQGNDRE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9391 VVNELGDLVDW---FVDADSRLQNQ-QPIASDL---DLLQQQLAEQKVMNEEINNQkVKARDTLSASKKLLSDSAMEDNS 9463
Cdd:TIGR02168 593 ILKNIEGFLGVakdLVKFDPKLRKAlSYLLGGVlvvDDLDNALELAKKLRPGYRIV-TLDGDLVRPGGVITGGSAKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9464 AI--RNKMDELKQWVDTVSGSANErqslLEQAVPFARHFHEAHTELVVWLDDVEPVLS-ELDVLSVDADQVKKQQEKA-- 9538
Cdd:TIGR02168 672 ILerRREIEELEEKIEELEEKIAE----LEKALAELRKELEELEEELEQLRKELEELSrQISALRKDLARLEAEVEQLee 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9539 ------KVLKQEVADRKPIVDRLNKTGTALVAmcGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSNsidQAMQQSAEFTDK 9612
Cdd:TIGR02168 748 riaqlsKELTELEAEIEELEERLEEAEEELAE--AEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9613 LENMLDTLTVTAEQVRSAEPISAQPDKLREQIEE-NKAME------EDLEMRHNALESVKNAAEELLRQAGDEQDEAVKD 9685
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESlAAEIEeleeliEELESELEALLNERASLEEALALLRSELEELSEE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9686 VRQKLEELTKLYKDIQERgRGRQRALEETLAVAEKFWDEL-HALNSSLKD-LQEALSSVDQPALEPEAIREQQEELEALK 9763
Cdd:TIGR02168 903 LRELESKRSELRRELEEL-REKLAQLELRLEGLEVRIDNLqERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
810
....*....|....*....
gi 1397727989 9764 EDI----EASQADFEEVQQ 9778
Cdd:TIGR02168 982 KELgpvnLAAIEEYEELKE 1000
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7805-8014 |
2.66e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 79.03 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7805 QDITQAMNELVSWMDSAEQVVTTQLPISlRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQR 7884
Cdd:cd00176 3 QQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7885 LTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEkLEQTNLWVHDGILQLDSKELSKL--SSDDMKQQLEKLAREKHNRL 7962
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGKDleSVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 7963 RTIQEIQVAAEQLLQDPRTGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASD 8014
Cdd:cd00176 160 PRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
37-137 |
5.83e-15 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 74.64 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNKHLMK-AGLRII-DLFDDLRDGHNLISLLEVLAHDIL------PRERGHMRfhkiQNVQIALDYLRLKGI 108
Cdd:cd21213 1 QLQAYVAWVNSQLKKrPGIRPVqDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1397727989 109 RLVNIRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
153-252 |
9.42e-15 |
|
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: 73.91 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 153 REALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSN---KQNLELAFTVAEKEF-GVTRLL 228
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLGlPELDLF 80
|
90 100
....*....|....*....|....
gi 1397727989 229 DPEDVdVPNPDEKSILTYVSSLYD 252
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
523-712 |
9.91e-15 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 77.49 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 523 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE--EQKLYTQ-KLSSVE 599
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEghPDAEEIQeRLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 600 VAYSLLLNTSSRRLKFLE---SLSEFLQGATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNLIRQVEARERHFNAV 676
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1397727989 677 QEKGGAMILDRHPAASM-VEVLMASLQARWSWLLQLV 712
Cdd:cd00176 166 NELAEELLEEGHPDADEeIEEKLEELNERWEELLELA 202
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
151-254 |
1.92e-14 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 73.16 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTVAEKEFGVTRLLDP 230
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|....
gi 1397727989 231 EDVdVPNPDEKSILTYVSSLYDVF 254
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFHSAF 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9139-9933 |
5.67e-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: 80.49 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9139 ERKHiESElQQLNSRWEALtKRVVDrtaILEEVQG----------LAGEFQDVLDPLTTW-LDAANKRFTALEphspdaE 9207
Cdd:TIGR02168 172 ERRK-ETE-RKLERTRENL-DRLED---ILNELERqlkslerqaeKAERYKELKAELRELeLALLVLRLEELR------E 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9208 GIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDvimiQLKIDGVQKQNGELRSHIEDcLEQMEEalplakHF 9287
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLE-VSEL----EEEIEELQKELYALANEISR-LEQQKQ------IL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9288 QEAHAEFLSWASKVEPELRALElgvpDEETNIEELANQLTEEMQPLLDIINSEGAELAEVAPGDAGLrvediinrdNKRF 9367
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL---------ESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9368 DNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLD--LLQQQLAEQKVMNEEINNQKVKARD 9445
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkLEEAELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9446 TLSASKKLLSdSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARH----FHEAHtelvvWLDDVEPVLSEL 9521
Cdd:TIGR02168 455 ELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkalLKNQS-----GLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9522 --------------------DVLSVDADQVK------KQQEKAKVLKQE---VADRKPIVDRL----NKTGTALVAMCGS 9568
Cdd:TIGR02168 529 isvdegyeaaieaalggrlqAVVVENLNAAKkaiaflKQNELGRVTFLPldsIKGTEIQGNDReilkNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9569 KGAEQVQSMLDDdnrRMDNVRTkvrdrSNSIDQAMQQSAEfTDKLENM--LDTLTVTAEQVRSAEPISAQP--------- 9637
Cdd:TIGR02168 609 KFDPKLRKALSY---LLGGVLV-----VDDLDNALELAKK-LRPGYRIvtLDGDLVRPGGVITGGSAKTNSsilerrrei 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9638 DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQ---ERGRGRQRALEET 9714
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleERIAQLSKELTEL 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9715 LAVAEKFWDELHALNSSLKDLQEALSSVDQPAL----EPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTT 9790
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9791 EQpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFET-IKKQWDELK 9869
Cdd:TIGR02168 840 LE-DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESkRSELRRELE 918
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9870 NFKTRVEPKNVEIESLNQHVTELtKSSTPEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMAL 9933
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNL-QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8339-9061 |
5.82e-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: 80.49 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8339 MEQVKVLREELSAQEPTydhflncahgiLERCGDKSQDGIAVSRRLDTVSKAW--NKLQSRLNERSKNLSSVEGISVEFA 8416
Cdd:TIGR02168 188 LDRLEDILNELERQLKS-----------LERQAEKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8417 SLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELKQ----LESELIVQQPRLARA-RDLCRQLCDKAKDASTKTDLR 8491
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrLEQQKQILRERLANLeRQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8492 SKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFE---ADCKELLTWISEAANNLQESEP-LSSDLDILREQM-RQNRTL 8566
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELEsrlEELEEQLETLRSKVAQLELQIAsLNNEIERLEARLeRLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8567 QQELSLKEPEIRQLLEKGDKLVKESSPTTEvRAIAdkvgELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKMAMWL 8646
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEELE-EELE----ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8647 QMTEEKLEKMKPEDVDQNTVVHKLKELQGV---------------------------------------------QNEMM 8681
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGIlgvlselisvdegyeaaieaalggrlqavvvenlnaakkaiaflkQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8682 K--------------KSHDRERLNSEGT-----------------------SLVECVDSGKEAIKQQVA----------- 8713
Cdd:TIGR02168 572 RvtflpldsikgteiQGNDREILKNIEGflgvakdlvkfdpklrkalsyllGGVLVVDDLDNALELAKKlrpgyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8714 --VINERW------DAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKL-AVHNSLGLSAKDPKHINR-IKDL 8783
Cdd:TIGR02168 652 gdLVRPGGvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeELEEELEQLRKELEELSRqISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8784 LEDTGWLASQLNNTETMLNSIEvdgGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLEL 8863
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8864 ESELgsktpvSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQAsslcnagyvsdpELLKSQVEALSNQHASLTERATQ 8943
Cdd:TIGR02168 809 RAEL------TLLNEEAANLRERLESLERRIAATERRLEDLEEQI------------EELSEDIESLAAEIEELEELIEE 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8944 RQSDVVANQHSIQHLTQALNLVWGDIDKASSTLDAMGpaggnvTTVKALQEELkgfvkstmEPLQKQFESVSRQGQALik 9023
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELE------SKRSELRREL--------EELREKLAQLELRLEGL-- 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 1397727989 9024 tavagsnTTGLETDLESLAERWAGLVEKVAEHEKNLDS 9061
Cdd:TIGR02168 935 -------EVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
9283-9494 |
1.08e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.40 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9283 LAKHFQEAHAEFLSWASKVEPELRALELGvpDEETNIEELANQ---LTEEMQPL---LDIINSEGAELAEVAPGDAGlRV 9356
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYG--DDLESVEALLKKheaLEAELAAHeerVEALNELGEQLIEEGHPDAE-EI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9357 EDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVvNELGDLVDWFVDADSRLQNQQPIaSDLDLLQQQLAEQKVMNEEI 9436
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFF-RDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 9437 NNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAV 9494
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
27-137 |
1.53e-13 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409071 Cd Length: 121 Bit Score: 71.08 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 27 LRDTDERDAVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHM----RFHKIQNVQIALDY 102
Cdd:cd21222 7 FDEAPEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPLHEYHLtpstDDEKLHNVKLALEL 86
|
90 100 110
....*....|....*....|....*....|....*
gi 1397727989 103 LRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21222 87 MEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
36-133 |
2.66e-13 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 70.25 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 36 VQKKTFTKWVNKHLMKAGL-RIIDLFDDLRDGHNLISLLEVLAHDILPRE---RGHMRFHKIQNVQIALDYLR--LKgIR 109
Cdd:cd21225 4 VQIKAFTAWVNSVLEKRGIpKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEedLK-IR 82
|
90 100
....*....|....*....|....
gi 1397727989 110 LVNIRSDEIVDGNPKLTLGLIWTI 133
Cdd:cd21225 83 VQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
45-134 |
2.96e-13 |
|
first 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 the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 69.93 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 45 VNKHLMKAGLR--------------IIDLFDDLRDGHNLISLLEVLAHDILPRERGHM----RFHKIQNVQIALDYLR-- 104
Cdd:cd21223 1 LTRHLGYLGYVlshvqtpldefdfaVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKea 80
|
90 100 110
....*....|....*....|....*....|..
gi 1397727989 105 --LKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21223 81 gvLRGGDGGGITAKDIVDGHREKTLALLWRII 112
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8192-8295 |
6.47e-13 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 68.51 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8192 RTFMQDMQDILQWLDLKDhETDSAQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQQ 8271
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH--PDAEEIEE 77
|
90 100
....*....|....*....|....
gi 1397727989 8272 QLQELDDKWHGLRALSEQQRKGLE 8295
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8523-8625 |
1.00e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 68.13 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8523 EKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPttEVRAIAD 8602
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP--DAEEIEE 77
|
90 100
....*....|....*....|...
gi 1397727989 8603 KVGELQGEWTRLQQEVTVQDSRL 8625
Cdd:smart00150 78 RLEELNERWEELKELAEERRQKL 100
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8301-8518 |
1.02e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.71 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8301 LRDMREHEQqltlWLAQKDRMLDVLGPVAmEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaV 8380
Cdd:cd00176 6 LRDADELEA----WLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8381 SRRLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRgLADWLSDFSDKLDGQGKVSSQPDKQhKQLQELKQLESEL 8460
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVE-ELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 8461 IVQQPRLARARDLCRQLCDKAKDASTKtDLRSKLTALEKDMNDTTRKLEICKAAVEEA 8518
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADE-EIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10374-10474 |
1.14e-12 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 68.13 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10374 QFTEALDALLDWLAKVEPALADDaPVHGDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 10453
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727989 10454 ELNAAWDRVCKLSVSKQDRLE 10474
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8631-8834 |
1.19e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.32 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8631 HAQQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQ 8710
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8711 QVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLaEATSALNKWENKLAVHNSLGLSAKDPKHINRIKDLLEDTGWL 8790
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1397727989 8791 ASQLNNTETMLNSIEVDGGETS--NLRDELNKLRGQHQTLQGELSE 8834
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDAdeEIEEKLEELNERWEELLELAEE 204
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
151-257 |
1.28e-12 |
|
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: 67.79 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWsrrTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21230 1 TPKQRLLGW---IQNKIPQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90 100
....*....|....*....|....*...
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSlydvFPQV 257
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLSQ----FPKA 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9625-10576 |
2.77e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9625 EQVRSAEPISAQPDKLREQIEE---------------NK--AMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAVKDVR 9687
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEaagiskykerrketeRKleRTRENLDRLEDILNELERQLKSLERQA--EKAERYKELK 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9688 QKLEELTK--LYKDIQERgRGRQRALEETLAVAEkfwDELHALNSSLKDLQEALSSVD--QPALEpEAIREQQEELEALK 9763
Cdd:TIGR02168 220 AELRELELalLVLRLEEL-REELEELQEELKEAE---EELEELTAELQELEEKLEELRleVSELE-EEIEELQKELYALA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9764 EDIEASQADFEEVQQTgdtllgmvgtteqpevQKNVDDAGASLAAISDQYSKRSQELESALAQAvhfQDQLMKLLVWLQE 9843
Cdd:TIGR02168 295 NEISRLEQQKQILRER----------------LANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9844 AEDEFSEFEpvasefetikkqwDELKNFKTRVEPKNVEIESLNQHVTELTKS--STPEQASVLREPMTQLNIRWNNLLTN 9921
Cdd:TIGR02168 356 LEAELEELE-------------AELEELESRLEELEEQLETLRSKVAQLELQiaSLNNEIERLEARLERLEDRRERLQQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9922 IGDRQRELQMAlltagqfdhahkelknwmdlvdvtldeitpvygDPKLVEIELAKLRIVQNDITAHQESVESISKEAQrl 10001
Cdd:TIGR02168 423 IEELLKKLEEA---------------------------------ELKELQAELEELEEELEELQEELERLEEALEELR-- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10002 mtsEGIAQAQGLKTKMEDMEktweniqAKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-----IISKPVGGlp 10076
Cdd:TIGR02168 468 ---EELEEAEQALDAAEREL-------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlseLISVDEGY-- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10077 ETAKEQ-LEKFMDvYAELEKLEPQVQSLNVMGEKLGGKSKGPALANLRQNlqhlnqrcdYIRSRACDRKKKLEDaegmat 10155
Cdd:TIGR02168 536 EAAIEAaLGGRLQ-AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGT---------EIQGNDREILKNIEG------ 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10156 nFHGELNKFISWLTDTEKTLNNLQPVSRLVERVTSQIEDHRDLqkdisKHREAMVALE-----KMGTHLKYFSQKQDVVL 10230
Cdd:TIGR02168 600 -FLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKL-----RPGYRIVTLDgdlvrPGGVITGGSAKTNSSIL 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10231 IKNllSSIQHRWEKIvSRSAERTRHLERGYKEAKQFNDTWKDLITWLIEAEKTLETETSVAnepdkiKAQISKHKEFQRR 10310
Cdd:TIGR02168 674 ERR--REIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL------RKDLARLEAEVEQ 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10311 LGAKQpvydgvnkaGRLLKERCPSDDVPTIQ-AMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDALLDWLAKV 10389
Cdd:TIGR02168 745 LEERI---------AQLSKELTELEAEIEELeERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10390 EPALADDAPVHGDIdtvngfldihkafQQELGARTTTIAFLQKSAK---EIISRAEGDVCSLQSDLIELNAAWDRVCKLS 10466
Cdd:TIGR02168 816 NEEAANLRERLESL-------------ERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESELEALLNER 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10467 VSKQDRLEHAQRLAEEFHKKAQQLLSWLADAERQLhyrgpipDEEPLILQQMEEHK-KFEESLLRQEANLRETLNIGQDI 10545
Cdd:TIGR02168 883 ASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLeGLEVRIDNLQERLSEEYSLTLEE 955
|
970 980 990
....*....|....*....|....*....|..
gi 1397727989 10546 MKRCHPDSVPIMKQW-LSVIRARwEELTALGR 10576
Cdd:TIGR02168 956 AEALENKIEDDEEEArRRLKRLE-NKIKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9436-10312 |
7.12e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.55 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9436 INNQKVKARDTLSaskkLLSDSAMEDNS-AI--RNKMDELkqwvdtVSGSANERQSLLEQAVPFARHF---HEAHTELVV 9509
Cdd:TIGR02168 114 INGQPCRLKDIQD----LFLDTGLGKRSySIieQGKISEI------IEAKPEERRAIFEEAAGISKYKerrKETERKLER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9510 W---LDDVEPVLSEL----DVLSVDADQVKKQQEKAKVLKQevADRKPIVDRLNKTGTALvamcgskgaEQVQSMLDDDN 9582
Cdd:TIGR02168 184 TrenLDRLEDILNELerqlKSLERQAEKAERYKELKAELRE--LELALLVLRLEELREEL---------EELQEELKEAE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9583 RRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKAMEEDLEMRHNALE 9662
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEAQLEELE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9663 SVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSV 9742
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9743 DQPALEPEAIREQQEELEAlkediEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAGASLAAISDQYSKRSQELES 9822
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLK-----KLEEAELKELQAELEEL-----EEELEELQEELERLEEALEELREELEEAEQALDA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9823 ALAQAVHFQDQLmKLLVWLQEAEDEFsefepvaseFETIKKQWDELKNFKT---------RVEPK---NVEI---ESLNQ 9887
Cdd:TIGR02168 480 AERELAQLQARL-DSLERLQENLEGF---------SEGVKALLKNQSGLSGilgvlseliSVDEGyeaAIEAalgGRLQA 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9888 HVTELTKS-----STPEQASVLREPMTQLNIRWNNLLT-NIGDRQRELQMALLTAGQFDHAHKELKNWMD-------LVD 9954
Cdd:TIGR02168 550 VVVENLNAakkaiAFLKQNELGRVTFLPLDSIKGTEIQgNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlVVD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9955 ------------------VTLDE--ITP---VYGDPKLVE-------IELAKLRivqNDITAHQESVESISKEAQRLMTs 10004
Cdd:TIGR02168 630 dldnalelakklrpgyriVTLDGdlVRPggvITGGSAKTNssilerrREIEELE---EKIEELEEKIAELEKALAELRK- 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10005 egiaQAQGLKTKMEDMEKTWENIQAKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-IISKPVGGLPETAKEQL 10083
Cdd:TIGR02168 706 ----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeELEERLEEAEEELAEAE 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10084 EKFMDVYAELEKLEPQVQSLNVMGEKLGGKSK--GPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEGMATNFHGEL 10161
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTllNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10162 NKFISWLTDTEKTLNNLQPVSRLVERVTSQIEDHRD-LQKDISKHREAMVALEKMGTHLkyfsqkqdvvliKNLLSSIQH 10240
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEeLSEELRELESKRSELRRELEEL------------REKLAQLEL 929
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 10241 RWEKIVSRSAERtrhlergykeAKQFNDTWKDlitwliEAEKTLETETSVANEPDKIKAQISKHKEFQRRLG 10312
Cdd:TIGR02168 930 RLEGLEVRIDNL----------QERLSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKELG 985
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
8862-9063 |
7.92e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.01 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8862 ELESELgSKTPVSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQASSLCNAGYvSDPELLKSQVEALSNQHASLTERA 8941
Cdd:cd00176 18 EKEELL-SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGH-PDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8942 TQRQSDvVANQHSIQHLTQALNLVWGDIDKASSTLDAMgPAGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQAL 9021
Cdd:cd00176 96 EERRQR-LEEALDLQQFFRDADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKEL-EEELEAHEPRLKSLNELAEEL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1397727989 9022 IKTAVAGSNTTgLETDLESLAERWAGLVEKVAEHEKNLDSAL 9063
Cdd:cd00176 173 LEEGHPDADEE-IEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10481-10582 |
1.02e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 65.43 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10481 EEFHKKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSVPImKQW 10560
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEI-EER 78
|
90 100
....*....|....*....|..
gi 1397727989 10561 LSVIRARWEELTALGRQRSARL 10582
Cdd:smart00150 79 LEELNERWEELKELAEERRQKL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9138-9768 |
1.21e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9138 AER-KHIESELQQLnsRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEphspdaEGIEHLIQEL 9216
Cdd:COG1196 212 AERyRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR------LELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9217 KKLQKEVNEHEpamKQLATAGKKLQDYCkgEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAlplakhfQEAHAEFls 9296
Cdd:COG1196 284 EEAQAEEYELL---AELARLEQDIARLE--ERRRELEERLEELEEELAELEEELEELEEELEEL-------EEELEEA-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9297 waskvEPELRALELgvpdEETNIEELANQLTEEMQPLLDIINSEGAELAEVApgDAGLRVEDIINRDNKRFDNLRDQIEK 9376
Cdd:COG1196 350 -----EEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEELLEAL--RAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9377 RAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQpiASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSD 9456
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9457 SAMEDNSAirnkmdelkqwvdtvsgsANERQSLLEQAVPFARHFHEAHTELVVWLDDVEPVL------SELDVLSVDADQ 9530
Cdd:COG1196 497 LEAEADYE------------------GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9531 VKKQQEKAKVLKQEVADRKPI--VDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRTKVRDRSnsidqamqqsaE 9608
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLdkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT-----------L 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9609 FTDKLENMLDTLTVTAEQVRSAEpisaqpdKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQ 9688
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVT-------LEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9689 KLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNssLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEA 9768
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL--LEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
30-136 |
1.32e-11 |
|
third 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. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein 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, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 65.38 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 30 TDERDavqKKTFTKWVNKhlMKAGLRIIDLFDDLRDGhnlISLLEVL----------AHDILPRERghMRFHKIQNVQIA 99
Cdd:cd21219 1 EGSRE---ERAFRMWLNS--LGLDPLINNLYEDLRDG---LVLLQVLdkiqpgcvnwKKVNKPKPL--NKFKKVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1397727989 100 LDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTIILH 136
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
168-248 |
1.68e-11 |
|
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: 64.71 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 168 PGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDVPNPDEKSILTY 246
Cdd:cd21229 17 PELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPEDLSSPHLDELSGMTY 96
|
..
gi 1397727989 247 VS 248
Cdd:cd21229 97 LS 98
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9068-9169 |
1.72e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 64.66 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9068 KFQDAMASLLDWLAETEELVAmQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITgLDPAERKHIESEL 9147
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 9148 QQLNSRWEALTKRVVDRTAILE 9169
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
38-134 |
2.56e-11 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 64.52 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 38 KKTFTKWVNKHLMK----AGLRII-----DLFDDLRDGHNLISLLEVLAHDILPRERGHMR-----FHKIQNVQIALDYL 103
Cdd:cd21217 3 KEAFVEHINSLLADdpdlKHLLPIdpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 104 RLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
39-140 |
3.71e-11 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. 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, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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 an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 64.18 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 39 KTFTKWVNKhlMKAGLRIIDLFDDLRDGHNLISLLEVL---------AHDILPRERGHMRfhKIQNVQIALDYLRLKGIR 109
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwsrVNKPFKKLGANMK--KIENCNYAVELGKKLKFS 84
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 110 LVNIRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21298 85 LVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9639-10225 |
3.91e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9639 KLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrgrqraLEETLAVA 9718
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE--------LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9719 EKFWDELHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEasqaDFEEVQQTGDTLLGMVGTTEQPEVQKN 9798
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELE------ERIEELKKEIEELEEKVK----ELKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9799 VDDAGASlaaisdQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRVEPK 9878
Cdd:PRK03918 311 EIEKRLS------RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9879 nvEIESLNQHVTELTKSSTPeqasvLREPMTQLNIRWNNLLTNIGDRQR---ELQMA---------LLTagqfDHAHKEL 9946
Cdd:PRK03918 385 --TPEKLEKELEELEKAKEE-----IEEEISKITARIGELKKEIKELKKaieELKKAkgkcpvcgrELT----EEHRKEL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9947 KNWMDLvdvtldEItpvygdpKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTSEGIA-QAQGLKTKM-----EDM 10020
Cdd:PRK03918 454 LEEYTA------EL-------KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeQLKELEEKLkkynlEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10021 EKTWENIQ------AKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQL-----IIS----KPVGGLPETAKEqLEK 10085
Cdd:PRK03918 521 EKKAEEYEklkeklIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaellkELEelgfESVEELEERLKE-LEP 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10086 FMDVYAELEKLEPQVQSLNvmgEKLggKSKGPALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAE-GMATNFHGELNKF 10164
Cdd:PRK03918 600 FYNEYLELKDAEKELEREE---KEL--KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRE 674
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 10165 ISWLTDTEKTLNNlqpvsrLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKYFSQK 10225
Cdd:PRK03918 675 LAGLRAELEELEK------RREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8340-8909 |
6.23e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8340 EQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDGIAVSRRLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASL- 8418
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELe 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8419 ---------TRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELKQLESELIvqqpRLARARDlcrqlcdkakdastktD 8489
Cdd:PRK03918 245 keleslegsKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI----KLSEFYE----------------E 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8490 LRSKLTALEKDMNDTTRKLEickaAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQE 8569
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8570 LSLKEPE-IRQLLEKGDKLVKESspTTEVRAIADKVGELQGEWTRLQ-----------------QEVTVQDSRLTMAGSH 8631
Cdd:PRK03918 381 LTGLTPEkLEKELEELEKAKEEI--EEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8632 A---------QQFTERLDK-----------------------MAMWLQMTEEKLEKMKPEDVDQNTvvhklKELQGVQNE 8679
Cdd:PRK03918 459 AelkriekelKEIEEKERKlrkelrelekvlkkeseliklkeLAEQLKELEEKLKKYNLEELEKKA-----EEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8680 MMKKSHDRERLNSEGTSLvecvdsgkEAIKQQVAVINERWDAVNKALSERASHLEDLG-QRLGEVQDSLAEATSALNKWe 8758
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKL--------EELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEY- 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8759 nklavhnslgLSAKD-PKHINRIKDLLEDtgwLASQLNNTETMLNSIEVDGGETSNLRDELNK---------LRGQHQTL 8828
Cdd:PRK03918 605 ----------LELKDaEKELEREEKELKK---LEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeeLREEYLEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8829 QGELSELVAEMETGAQIVEQFQGLLKivggqflELESELGsktpvSRDDAELGSQ-LADMKDFLTRLGEKVETLKDLEQQ 8907
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLE-------KLKEELE-----EREKAKKELEkLEKALERVEELREKVKKYKALLKE 739
|
..
gi 1397727989 8908 AS 8909
Cdd:PRK03918 740 RA 741
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9350-9913 |
7.96e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 7.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9350 GDAGLRVEDIinRDNKR--FDNLRDQIEKRAQKvqlarqrssevvnelgDLVDwfvdadsrlqnqqpiasDLDLLQQQLA 9427
Cdd:PRK02224 172 SDARLGVERV--LSDQRgsLDQLKAQIEEKEEK----------------DLHE-----------------RLNGLESELA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9428 EQKVMNEEINNQKVKARDTLSASkkllsDSAMEDNSAIRNKMDELKQWVD----TVSGSANERQSLLEQAvpfarhfHEA 9503
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEA-----DEVLEEHEERREELETLEAEIEdlreTIAETEREREELAEEV-------RDL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9504 HTELVVWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADR----KPIVDRLNKTGTALV--AMCGSKGAEQVQSM 9577
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRleecRVAAQAHNEEAESLRedADDLEERAEELREE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9578 LDDDNRRMDNVRTKVRDRSNSID----QAMQQSAEFTD------KLENMLDTLTVTAEQVRSAE---------------- 9631
Cdd:PRK02224 365 AAELESELEEAREAVEDRREEIEeleeEIEELRERFGDapvdlgNAEDFLEELREERDELREREaeleatlrtarervee 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9632 ----------PISAQP----------DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAG--------------- 9676
Cdd:PRK02224 445 aealleagkcPECGQPvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrierleerredleel 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9677 -DEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQ 9755
Cdd:PRK02224 525 iAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9756 QEELEALKEDIEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAgaslaaisdqyskRSQELESALAQAVHFQDQLM 9835
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLAEK-----RERKRELEAEFDEA-------------RIEEAREDKERAEEYLEQVE 666
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 9836 KLLVWLQEAEDEF-SEFEPVASEFETIKKQWDELKNFKTRVEpknvEIESLNQHVTELtkSSTPEQasvLREPMTQLNI 9913
Cdd:PRK02224 667 EKLDELREERDDLqAEIGAVENELEELEELRERREALENRVE----ALEALYDEAEEL--ESMYGD---LRAELRQRNV 736
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10157-10257 |
8.74e-11 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 62.73 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10157 FHGELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyFSQKQDVVLIKNLLS 10236
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727989 10237 SIQHRWEKIVSRSAERTRHLE 10257
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
8264-9122 |
9.99e-11 |
|
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: 69.76 E-value: 9.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8264 PGEEMLQQQLQELddkwhglralsEQQRKGLEDMVSDLRDMreHEQQlTLWLAQKDRMLDV-LGPVAMEPNMLASQMEQV 8342
Cdd:pfam15921 71 PGKEHIERVLEEY-----------SHQVKDLQRRLNESNEL--HEKQ-KFYLRQSVIDLQTkLQEMQMERDAMADIRRRE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8343 KVLREELSAQEPTYDHFLNCAHGILERCGDKSQDGIAVSRRL-----DTVSKAWNKLQSRLNERSKNLSSVEGIS-VEFA 8416
Cdd:pfam15921 137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlsheGVLQEIRSILVDFEEASGKKIYEHDSMStMHFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8417 SLTRGLADWLSDFSDKLDG-QGKVSSQPDkqhkQLQELK---QLESELIVQQprlarARDLCRQLCdkAKDASTKTDLRS 8492
Cdd:pfam15921 217 SLGSAISKILRELDTEISYlKGRIFPVED----QLEALKsesQNKIELLLQQ-----HQDRIEQLI--SEHEVEITGLTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8493 KLTALEKDMNDTTRKLEICKaavEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDldilreqmrQNRTLQQELSL 8572
Cdd:pfam15921 286 KASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED---------KIEELEKQLVL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8573 KEPEIRQLLEKGDKLVKESSpttevrAIADKVGELQGEWTRLQQEVTV---QDSRL---TMAGSHAQQFTER-LDKMAMW 8645
Cdd:pfam15921 354 ANSELTEARTERDQFSQESG------NLDDQLQKLLADLHKREKELSLekeQNKRLwdrDTGNSITIDHLRReLDDRNME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8646 LQMTEEKLEKMKPEDvdQNTVVHKLKELQGvQNEMMKKShdrerlnsegTSLVECVDSGKEAIKQQVavinERWDAVNKA 8725
Cdd:pfam15921 428 VQRLEALLKAMKSEC--QGQMERQMAAIQG-KNESLEKV----------SSLTAQLESTKEMLRKVV----EELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8726 LSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLavhnslGLSAKDPKHINRIKDlledtgwlasQLNNTETMLNSIE 8805
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRV------DLKLQELQHLKNEGD----------HLRNVQTECEALK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8806 VDGGETSNLrdeLNKLRGQHQTLqgelSELVAE--METGAQIVEQFQgLLKIVGGQFLELEsELgsKTPVSRDDA---EL 8880
Cdd:pfam15921 555 LQMAEKDKV---IEILRQQIENM----TQLVGQhgRTAGAMQVEKAQ-LEKEINDRRLELQ-EF--KILKDKKDAkirEL 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8881 GSQLADMKDFLTRL----GEKVETLKDLEQQASSLCNAGYVSdpellKSQVEALSNQHASLTE--RATQRQSDVVANQHS 8954
Cdd:pfam15921 624 EARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTS-----RNELNSLSEDYEVLKRnfRNKSEEMETTTNKLK 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8955 IQhltqaLNLVWGDIDKASSTLDAMGPAGGNVTTV---------------KALQEELKgFVKSTMEPLQKQF----ESVS 9015
Cdd:pfam15921 699 MQ-----LKSAQSELEQTRNTLKSMEGSDGHAMKVamgmqkqitakrgqiDALQSKIQ-FLEEAMTNANKEKhflkEEKN 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9016 RQGQALIKTAVAGSNTTGletDLESLAERWAGLVEKVAEHEKNLDSALLRtgkfqdamaslldwLAETEELVAMQkapsp 9095
Cdd:pfam15921 773 KLSQELSTVATEKNKMAG---ELEVLRSQERRLKEKVANMEVALDKASLQ--------------FAECQDIIQRQ----- 830
|
890 900 910
....*....|....*....|....*....|
gi 1397727989 9096 EQRVVRAQLQEQ---KLVQKMVTDRTPSMK 9122
Cdd:pfam15921 831 EQESVRLKLQHTldvKELQGPGYTSNSSMK 860
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9080-9854 |
1.15e-10 |
|
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: 69.76 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9080 LAETEELVAMQKApSPEQRVVRAQ--LQEQKLVQKMVTD-RTPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRW 9154
Cdd:pfam15921 94 LNESNELHEKQKF-YLRQSVIDLQtkLQEMQMERDAMADiRRRESQSQEDLRNQLQNTVHELEaaKCLKEDMLEDSNTQI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9155 EALTKRVVDRTAILEEVQGLAGEFQD--------------------------VLDPLTTWLDAANKRFTALEPH-----S 9203
Cdd:pfam15921 173 EQLRKMMLSHEGVLQEIRSILVDFEEasgkkiyehdsmstmhfrslgsaiskILRELDTEISYLKGRIFPVEDQlealkS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9204 PDAEGIEHLIQELK-KLQKEVNEHEPAMKQLAtagKKLQDYCKGEDVIMIQLKIDGVQKQNGE---LR--SHIEDCLEQM 9277
Cdd:pfam15921 253 ESQNKIELLLQQHQdRIEQLISEHEVEITGLT---EKASSARSQANSIQSQLEIIQEQARNQNsmyMRqlSDLESTVSQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9278 EEALPLAKHFQEAHAEflswasKVEPELRALELGVPDEETNIEELANQ---LTEEMQPLLDIINSEGAELAEVAPGDAGL 9354
Cdd:pfam15921 330 RSELREAKRMYEDKIE------ELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9355 RVEDIINrdNKRFDNLRDQIEKRAQKVQlarqRSSEVVNELgdlvdwfvdaDSRLQNQqpiasdldlLQQQLAEQKVMNE 9434
Cdd:pfam15921 404 WDRDTGN--SITIDHLRRELDDRNMEVQ----RLEALLKAM----------KSECQGQ---------MERQMAAIQGKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9435 EInnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAvpfarhfheaHTELVVWLDDV 9514
Cdd:pfam15921 459 SL--EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT----------NAEITKLRSRV 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9515 EPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKG-------AEQVQSMLDDDNRRMDN 9587
Cdd:pfam15921 527 DLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGrtagamqVEKAQLEKEINDRRLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9588 VRTKVRDrsnsidqamqqsaeftdklenmldtltvtaeqvrsaepisaqpDKLREQIEENKAMEEDLEmrhnaLESVK-- 9665
Cdd:pfam15921 607 QEFKILK-------------------------------------------DKKDAKIRELEARVSDLE-----LEKVKlv 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9666 NAAEELLRQAGD---EQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSV 9742
Cdd:pfam15921 639 NAGSERLRAVKDikqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9743 DqpALEPEAIR---EQQEELEALKEDIEASQADFEEVQQTGDTllgmvGTTEQPEVQKNVDDAGASLAAISDQYSKRSQE 9819
Cdd:pfam15921 719 E--GSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEAMTN-----ANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
810 820 830
....*....|....*....|....*....|....*
gi 1397727989 9820 LESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPV 9854
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDI 826
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9511-10347 |
1.20e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9511 LDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKT-GTALV----AMCGSKgaEQVQSMLDDDNRRM 9585
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYeGYELLkekeALERQK--EAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9586 DNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLD--TLTVTAEqvrsAEPISAQPDKLREQIEENKAMEEDLEmrhnalES 9663
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeQLRVKEK----IGELEAEIASLERSIAEKERELEDAE------ER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9664 VKNAAEELLRQAGD--EQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSS 9741
Cdd:TIGR02169 324 LAKLEAEIDKLLAEieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9742 V----DQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVgTTEQPEVQKNVDDAGASLAAISDQYSKRS 9817
Cdd:TIGR02169 404 LkrelDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9818 QELESAlaqavhfQDQLMKLLVWLQEAEDEFSEFEPVASEFET----IKKQWDELknfkTRVEPKNV-EIES-----LNQ 9887
Cdd:TIGR02169 483 KELSKL-------QRELAEAEAQARASEERVRGGRAVEEVLKAsiqgVHGTVAQL----GSVGERYAtAIEVaagnrLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9888 HVTElTKSSTPEQASVLRE----PMTQLNirwnnlLTNIGDRQRELQmALLTAGQFDHAhkelknwMDLVDVTlDEITP- 9962
Cdd:TIGR02169 552 VVVE-DDAVAKEAIELLKRrkagRATFLP------LNKMRDERRDLS-ILSEDGVIGFA-------VDLVEFD-PKYEPa 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9963 ---VYGDPKLVE-IELAK-LRIVQNDITAHQESVE--------SISKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQA 10029
Cdd:TIGR02169 616 fkyVFGDTLVVEdIEAARrLMGKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10030 KSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQLiiskpvgglpETAKEQLEKFMDVYAELEKlepqvqslnvmgek 10109
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----------EKLKERLEELEEDLSSLEQ-------------- 751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10110 lggkskgpALANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEGMATnfHGELNKFISWLTDTEKTlnnlqpVSRLVERVt 10189
Cdd:TIGR02169 752 --------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEE------VSRIEARL- 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10190 sqiedhRDLQKDISKHREAMVALEKMGTHLkyfsqKQDVVLIKNLLSSIQHRWEKIVSRSAERTRHLERGYKEAKQFNDT 10269
Cdd:TIGR02169 815 ------REIEQKLNRLTLEKEYLEKEIQEL-----QEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10270 WKDLITWLIEAEKTLEtetSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKA-----GRLLKERCPSDDVPTIQAML 10344
Cdd:TIGR02169 884 LGDLKKERDELEAQLR---ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkGEDEEIPEEELSLEDVQAEL 960
|
...
gi 1397727989 10345 TEL 10347
Cdd:TIGR02169 961 QRV 963
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
9238-10023 |
1.44e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 69.70 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9238 KKLQDYckGEDVIMIQLKIDGVQKQNgelrshiedcLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEET 9317
Cdd:TIGR01612 565 KELEEE--NEDSIHLEKEIKDLFDKY----------LEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENN 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9318 N--IEELAN----QLTEEMQPLLDIINSEGAELAEVAPGD---------AGLRVEDIINRDNK-RFDNLRDQIEKRAQKV 9381
Cdd:TIGR01612 633 NayIDELAKispyQVPEHLKNKDKIYSTIKSELSKIYEDDidalynelsSIVKENAIDNTEDKaKLDDLKSKIDKEYDKI 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9382 Q-----LARQRSSEVVNELGDLVDWFVDADSRLQNQqpIASDLD-LLQQQLAEQKVMNEEINNQKvKARDTLSASKKLLS 9455
Cdd:TIGR01612 713 QnmetaTVELHLSNIENKKNELLDIIVEIKKHIHGE--INKDLNkILEDFKNKEKELSNKINDYA-KEKDELNKYKSKIS 789
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9456 D--SAMEDNSAIRNKMDE--------LKQWVDTVSGSANERQSLLEQaVPFARHFHEAHTELVVWLDD--VEPVLSELDV 9523
Cdd:TIGR01612 790 EikNHYNDQINIDNIKDEdakqnydkSKEYIKTISIKEDEIFKIINE-MKFMKDDFLNKVDKFINFENncKEKIDSEHEQ 868
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9524 LSVDADQVKKQ--QEKAKVLKQEVADRKPIVDRLNKT-------------GTALVAMCGSKgAEQVQSMLDDDNRRMD-- 9586
Cdd:TIGR01612 869 FAELTNKIKAEisDDKLNDYEKKFNDSKSLINEINKSieeeyqnintlkkVDEYIKICENT-KESIEKFHNKQNILKEil 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9587 NVRTKVRDRSNSIDQAmqqsaeFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLemrhnalesvKN 9666
Cdd:TIGR01612 948 NKNIDTIKESNLIEKS------YKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANL----------GK 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9667 AAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQ----------------ERGRGRQRALEETLAVAE----------- 9719
Cdd:TIGR01612 1012 NKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEiaihtsiyniideiekEIGKNIELLNKEILEEAEinitnfneike 1091
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9720 ----------------KFWDELHALNSSLKDLQEalsSVDQPALEPEAIREQQE----ELEALKEDIEA------SQADF 9773
Cdd:TIGR01612 1092 klkhynfddfgkeeniKYADEINKIKDDIKNLDQ---KIDHHIKALEEIKKKSEnyidEIKAQINDLEDvadkaiSNDDP 1168
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9774 EEVQQTGDTLLGMVgtteqpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSE--- 9850
Cdd:TIGR01612 1169 EEIEKKIENIVTKI------DKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmi 1242
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9851 --FEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLN-------QHVTelTKSSTPEQASVLREPMTQLnIRWNNLLTN 9921
Cdd:TIGR01612 1243 kaMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNishdddkDHHI--ISKKHDENISDIREKSLKI-IEDFSEESD 1319
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9922 IGDRQRELQMALLTAGQFDHAhkelknwmdlVDVTLDEITPVYGDPKLVEIE--LAKLRIVQNDITAHQESVESISKEAQ 9999
Cdd:TIGR01612 1320 INDIKKELQKNLLDAQKHNSD----------INLYLNEIANIYNILKLNKIKkiIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
890 900
....*....|....*....|....
gi 1397727989 10000 RLMTSegIAQAQGLKTKMEDMEKT 10023
Cdd:TIGR01612 1390 KLIKK--IKDDINLEECKSKIEST 1411
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10046-10148 |
1.90e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 61.58 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10046 QGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANLRQN 10125
Cdd:smart00150 1 QQFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQL-IEEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727989 10126 LQHLNQRCDYIRSRACDRKKKLE 10148
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
32-131 |
2.53e-10 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.06 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAvqkKTFTKWVNKHLMKAGlrIIDLFDDLRDGHNLISLLEVLAHDI--------LPRERGHMRFHKIQNVQIALDYL 103
Cdd:cd21300 6 EREA---RVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1397727989 104 RLKGIRLVNIRSDEIVDGNPKLTLGLIW 131
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9498-9600 |
3.04e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 61.19 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9498 RHFHEAHTELVVWLDDVEPVLSELDVlSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMcGSKGAEQVQSM 9577
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDL-GKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727989 9578 LDDDNRRMDNVRTKVRDRSNSID 9600
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8552-9389 |
3.21e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8552 DLDILREQMrqnrtlqQELSLKEPEIRQLLekgDKLVKESSPTTEVRAIADKVGELQG-----EWTRLQQEVTVQDSRLT 8626
Cdd:TIGR02169 178 ELEEVEENI-------ERLDLIIDEKRQQL---ERLRREREKAERYQALLKEKREYEGyellkEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8627 MAGSHAQQFTERLDKMAMWLQMTEEKLEK-----MKPEDVDQNTVVHKLKELQG----------VQNEMMKKSHDRERln 8691
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEElnkkiKDLGEEEQLRVKEKIGELEAeiaslersiaEKERELEDAEERLA-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8692 sEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAvhnslGLSA 8771
Cdd:TIGR02169 326 -KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-----KLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8772 KDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEVD----GGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVE 8847
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8848 QFQGLLKIVGGQFLELESELGSKTPVSRDDA----ELGSQLADMKDFLTRLGE-KVETLKDLEQQASSLCNAGYVSDPEL 8922
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARASEERVRGGRaveeVLKASIQGVHGTVAQLGSvGERYATAIEVAAGNRLNNVVVEDDAV 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8923 LKSQVEALSNQHAS------LTE-RATQRQSDVVANQHSIQHltqALNLVwgDIDkasstlDAMGPAggnvtTVKALQEE 8995
Cdd:TIGR02169 560 AKEAIELLKRRKAGratflpLNKmRDERRDLSILSEDGVIGF---AVDLV--EFD------PKYEPA-----FKYVFGDT 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8996 LkgfVKSTME---PLQKQFESVSRQGQALIKTAV----------AGSNTTGLETDLESLAER-------WAGLVEKVAEH 9055
Cdd:TIGR02169 624 L---VVEDIEaarRLMGKYRMVTLEGELFEKSGAmtggsraprgGILFSRSEPAELQRLRERleglkreLSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9056 EKNLDSAllrTGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQ-----------EQKLVQKMVTDRTPSMKAV 9124
Cdd:TIGR02169 701 ENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeienvksELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9125 QDSGNQLITGLDPAERKHIESELQQLN---SRWEAltkRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEp 9201
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEeevSRIEA---RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9202 hspdaEGIEHLIQELKKLQKEVNEHEPAMKQLataGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDCLEQMEEAL 9281
Cdd:TIGR02169 854 -----KEIENLNGKKEELEEELEELEAALRDL---ESRLGD---------LKKERDELEAQLRELERKIEELEAQIEKKR 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9282 PLAKHFQEAHAEFLSWASKVEPELRALElGVPDEETNIEELANQ---LTEEMQPLLDIINSEGAELAEVApgdaglrved 9358
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAElqrVEEEIRALEPVNMLAIQEYEEVL---------- 985
|
890 900 910
....*....|....*....|....*....|.
gi 1397727989 9359 iinrdnKRFDNLRDQIEKraqkvqLARQRSS 9389
Cdd:TIGR02169 986 ------KRLDELKEKRAK------LEEERKA 1004
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8520-8616 |
3.25e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 61.18 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8520 QQAEKFEADCKELLTWISEAANNLQeSEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKESSPTTEvrA 8599
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASE--E 77
|
90
....*....|....*..
gi 1397727989 8600 IADKVGELQGEWTRLQQ 8616
Cdd:pfam00435 78 IQERLEELNERWEQLLE 94
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10265-10367 |
4.15e-10 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 60.80 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10265 QFNDTWKDLITWLIEAEKTLETEtSVANEPDKIKAQISKHKEFQRRLGAKQPVYDGVNKAGRLLKERCPsDDVPTIQAML 10344
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH-YASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727989 10345 TELKSHWNNVCSKSVDRQRKLEE 10367
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9207-9931 |
5.74e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9207 EGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgEDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEAlplAKH 9286
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKIGELEAEIASLERSIAEKERELEDA---EER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9287 FQEAHAEFlswaSKVEPELRALElgvpdeeTNIEELA---NQLTEEMQPLLDIINSEGAELAEVAPGDAGLRVEDI---- 9359
Cdd:TIGR02169 324 LAKLEAEI----DKLLAEIEELE-------REIEEERkrrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyre 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9360 -INRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRL-----------QNQQPIASDLDLLQQQL- 9426
Cdd:TIGR02169 393 kLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKedkaleikkqeWKLEQLAADLSKYEQELy 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9427 ---AEQKVMNEEINnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVS--GSANER-QSLLEQAVPFARHF 9500
Cdd:TIGR02169 473 dlkEEYDRVEKELS-KLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAqlGSVGERyATAIEVAAGNRLNN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9501 HEAHTELV------------------VWLDDVEPVLSELDVLSVDA------DQVKKQQEKAKVLKQ-----------EV 9545
Cdd:TIGR02169 552 VVVEDDAVakeaiellkrrkagratfLPLNKMRDERRDLSILSEDGvigfavDLVEFDPKYEPAFKYvfgdtlvvediEA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9546 ADRKPIVDRL------------NKTGTALVAMCGS----KGAEQVQSM------LDDDNRRMDNVRTKVRDRSNSIDQAM 9603
Cdd:TIGR02169 632 ARRLMGKYRMvtlegelfeksgAMTGGSRAPRGGIlfsrSEPAELQRLrerlegLKRELSSLQSELRRIENRLDELSQEL 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9604 QQSAEFTDKLENMLDTLTVTAEQVRS-AEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDE-QDE 9681
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHS 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9682 AVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQP---------ALEPE-- 9750
Cdd:TIGR02169 792 RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlngkkeELEEEle 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9751 ----AIREQQEELEALKEDIEASQADFEEVQQTGDTLlgmvgTTEQPEVQKNVDDAGASLAAISDQYSkrsqELESALAQ 9826
Cdd:TIGR02169 872 eleaALRDLESRLGDLKKERDELEAQLRELERKIEEL-----EAQIEKKRKRLSELKAKLEALEEELS----EIEDPKGE 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9827 AVHFQDQLM---KLLVWLQEAEDEFSEFEPV----ASEFETIKKQWDELKNFKTRVEPKNVEIEslnqhvtELTKSSTPE 9899
Cdd:TIGR02169 943 DEEIPEEELsleDVQAELQRVEEEIRALEPVnmlaIQEYEEVLKRLDELKEKRAKLEEERKAIL-------ERIEEYEKK 1015
|
810 820 830
....*....|....*....|....*....|..
gi 1397727989 9900 QASVLREPMTQLNIRWNNLLTNIGDRQRELQM 9931
Cdd:TIGR02169 1016 KREVFMEAFEAINENFNEIFAELSGGTGELIL 1047
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7874-8675 |
6.16e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7874 ELDIARAVeQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKLEQTNLwvhdgilqldskelsklssddmkqqlek 7953
Cdd:TIGR02168 224 ELELALLV-LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL---------------------------- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7954 larEKHNRLRTIQEIQvaaeqllqdprtGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWL 8033
Cdd:TIGR02168 275 ---EVSELEEEIEELQ------------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8034 SQMEARLDEFQPVaidvgiVEQQKMELQPMLQEYEDYAPKIDEVNDLGNAYEAMINPGDRPISPIR-RIGRsrrlpgiLS 8112
Cdd:TIGR02168 340 AELEEKLEELKEE------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNnEIER-------LE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8113 PRLRSpsptfptspSTQRASPLssessgVSSRKSSADNLLLDDLSEVQQQLLDITQRYEIVGERLADRQQELQLMLTSIR 8192
Cdd:TIGR02168 407 ARLER---------LEDRRERL------QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8193 TFMQDMQDILQWLDLKDHETDSAQPLPTNEKDAKKRLKEhevfhrEILSKEGLvEDIRKKAQDLLKTRHG-------VPG 8265
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA------LLKNQSGL-SGILGVLSELISVDEGyeaaieaALG 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8266 EEM-------LQQQLQELD-DKWH----------------GLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLAqkdrm 8321
Cdd:TIGR02168 545 GRLqavvvenLNAAKKAIAfLKQNelgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS----- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8322 lDVLGPVAMEPNmLASQMEQVKVLREELSAQepTYDHFLNCAHGILERCGDKSQDGI-AVSRRLDTVSKAWNKLQSRLNE 8400
Cdd:TIGR02168 620 -YLLGGVLVVDD-LDNALELAKKLRPGYRIV--TLDGDLVRPGGVITGGSAKTNSSIlERRREIEELEEKIEELEEKIAE 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8401 RSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQ-----------GKVSSQPDKQHKQLQELKQ----LESELIVQQP 8465
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarleaevEQLEERIAQLSKELTELEAeieeLEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8466 RLARARDLCRQLCDKAKDAST-KTDLRSKLTALEKDMNDTTRKLeickAAVEEASQQAEKFEADCKELLTWISEAANNLQ 8544
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEeLKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8545 ES-EPLSSDLDILREQMRQ-NRTLQQELSLKEPEIRQLLEKGDKLVKESsptTEVRAIADKVGELQGEWTRLQQEVTVQD 8622
Cdd:TIGR02168 852 EDiESLAAEIEELEELIEElESELEALLNERASLEEALALLRSELEELS---EELRELESKRSELRRELEELREKLAQLE 928
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 8623 SRLTMAGSHAQQFTERLdkmAMWLQMTEEKLEKMKPEDVDQNTVVH-KLKELQG 8675
Cdd:TIGR02168 929 LRLEGLEVRIDNLQERL---SEEYSLTLEEAEALENKIEDDEEEARrRLKRLEN 979
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9938-10039 |
6.62e-10 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 60.04 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9938 QFDHAHKELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMtSEGIAQAQGLKTKM 10017
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI-EEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 10018 EDMEKTWENIQAKSRAKQDMLE 10039
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9588-9822 |
6.96e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9588 VRTKVRDRSNSIDQAMQQSAEFTDkLENMLDTLTVTAEQVRSAEPISAQPDK---LREQIEENKAMEEDL-----EMRHN 9659
Cdd:COG4913 213 VREYMLEEPDTFEAADALVEHFDD-LERAHEALEDAREQIELLEPIRELAERyaaARERLAELEYLRAALrlwfaQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9660 ALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwdELHALNSSLKDLQEAL 9739
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLER---ELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9740 SSVD-QPALEPEAIREQQEELEALKEDIEASQAdfeevqqtgdtllgmvgtteqpEVQKNVDDAGASLAAISDQYSKRSQ 9818
Cdd:COG4913 369 AALGlPLPASAEEFAALRAEAAALLEALEEELE----------------------ALEEALAEAEAALRDLRRELRELEA 426
|
....
gi 1397727989 9819 ELES 9822
Cdd:COG4913 427 EIAS 430
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8191-8296 |
1.57e-09 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 59.25 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8191 IRTFMQDMQDILQWLDLKDHETDSaQPLPTNEKDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRHgvPGEEMLQ 8270
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGH--YASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1397727989 8271 QQLQELDDKWHGLRALSEQQRKGLED 8296
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
7809-7907 |
2.88e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 58.11 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7809 QAMNELVSWMDSAEQVVTTQlPISLRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELVKTCELDiARAVEQRLTSL 7888
Cdd:smart00150 5 RDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEEL 82
|
90
....*....|....*....
gi 1397727989 7889 DEKFSSLQAKCRQRDRDLE 7907
Cdd:smart00150 83 NERWEELKELAEERRQKLE 101
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9259-9910 |
3.17e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9259 VQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALElgvpdeetniEELAN--QLTEEMQPLLDI 9336
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELR----------EELEKleKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9337 INSEGAELAEVApGDAGLRVEDIINRDnKRFDNLRDQIEKRAQKVQLAR--QRSSEVVNELGDLVDWFVDADSRLQNQqp 9414
Cdd:PRK03918 240 IEELEKELESLE-GSKRKLEEKIRELE-ERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKR-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9415 iasdLDLLQQQLAEQKVMNEEINNQKVKARDTlsasKKLLSDsamednsaIRNKMDELKQWVDTVsgsaNERQSLLEQAV 9494
Cdd:PRK03918 316 ----LSRLEEEINGIEERIKELEEKEERLEEL----KKKLKE--------LEKRLEELEERHELY----EEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9495 PF-ARHFHEAHTELVVWLDDVEPVLSELDvlsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKT-GTALVamCGSKGAE 9572
Cdd:PRK03918 376 RLkKRLTGLTPEKLEKELEELEKAKEEIE------EEISKITARIGELKKEIKELKKAIEELKKAkGKCPV--CGRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9573 QVQ-SMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENM--LDTLTVTAEQVRSAEpisaqpDKLR----EQIE 9645
Cdd:PRK03918 448 EHRkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELE------EKLKkynlEELE 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9646 ENKAMEEDLEMRHNALES-VKNAAEELLRQAGDEQDEAV--KDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFW 9722
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGeIKSLKKELEKLEELKKKLAEleKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9723 DELHALNSSLKDLQEalssvdqpalEPEAIREQQEELEALKEDIEASQADFEEVQQtgdtllgmvgttEQPEVQKNVDDa 9802
Cdd:PRK03918 602 NEYLELKDAEKELER----------EEKELKKLEEELDKAFEELAETEKRLEELRK------------ELEELEKKYSE- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9803 gASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRV-EPKNVE 9881
Cdd:PRK03918 659 -EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVkKYKALL 737
|
650 660
....*....|....*....|....*....
gi 1397727989 9882 IESLNQHVTELtksstpeqASVLREPMTQ 9910
Cdd:PRK03918 738 KERALSKVGEI--------ASEIFEELTE 758
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
39-133 |
3.44e-09 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 58.12 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 39 KTFTKWVNKHLMKAGLR--IIDLFDDLRDGHNLISLLEVLAHDIL------PRERGHMrfhkIQNVQIALDYLRLKGIRL 110
Cdd:cd21286 3 KIYTDWANHYLAKSGHKrlIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTI 133
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8488-8944 |
3.56e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8488 TDLRSKLTALEKDMNDTTRKLEICkaavEEASQQAEKFEADCKELLTwisEAANNLQESEPLSSDLDILREQM----RQN 8563
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERY----EEQREQARETRDEADEVLE---EHEERREELETLEAEIEDLRETIaeteRER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8564 RTLQQELSLKEPEIRQLLEKGDKLVKESSPTT-EVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKM 8642
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8643 amwlqmtEEKLEKMKPEdvdqntvvhklkelqgvqnemmkkshdRERLNSEGTSLVECVDSGK---EAIKQQVAVINERW 8719
Cdd:PRK02224 355 -------EERAEELREE---------------------------AAELESELEEAREAVEDRReeiEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8720 DAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNSL---------GLSAKDPKHINRIKDLLEDTGWL 8790
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkcpecGQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8791 ASQLNNTETMLNSIE--VDGGET-SNLRDELNKLRGQHQTLQgelsELVAEMETGA-QIVEQFQGLLKIVGgqflELESE 8866
Cdd:PRK02224 481 EAELEDLEEEVEEVEerLERAEDlVEAEDRIERLEERREDLE----ELIAERRETIeEKRERAEELRERAA----ELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8867 LGSKtpvsRDDAELGSQLAD-----MKDFLTRLGEKVETLKDLEQQASSLcnagyvSDPELLKSQVEALSNQHASLTERA 8941
Cdd:PRK02224 553 AEEK----REAAAEAEEEAEeareeVAELNSKLAELKERIESLERIRTLL------AAIADAEDEIERLREKREALAELN 622
|
...
gi 1397727989 8942 TQR 8944
Cdd:PRK02224 623 DER 625
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10374-10474 |
3.93e-09 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 58.10 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10374 QFTEALDALLDWLAKVEPALADDAPVHgDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLI 10453
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLE 83
|
90 100
....*....|....*....|.
gi 1397727989 10454 ELNAAWDRVCKLSVSKQDRLE 10474
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLE 104
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
9068-9170 |
4.16e-09 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 58.10 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9068 KFQDAMASLLDWLAETEELVAMQKAPSPEQRVvRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAErKHIESEL 9147
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGKDLESV-QALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727989 9148 QQLNSRWEALTKRVVDRTAILEE 9170
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
34-133 |
4.55e-09 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 58.44 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 34 DAVQKKTFTKWVNKHLMKAGLR--IIDLFDDLRDGHNLISLLEVLAHDIL------PRERGHMrfhkIQNVQIALDYLRL 105
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSGHKrlIKDLQQDVTDGVLLAEIIQVVANEKIedingcPKNRSQM----IENIDACLSFLAA 83
|
90 100
....*....|....*....|....*...
gi 1397727989 106 KGIRLVNIRSDEIVDGNPKLTLGLIWTI 133
Cdd:cd21285 84 KGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
151-256 |
7.00e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 57.77 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....*..
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSlydvFPQ 256
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQ----FPK 110
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
621-720 |
9.00e-09 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 56.95 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 621 EFLQGATAELTWLAEREEVeVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVLMA 699
Cdd:smart00150 2 QFLRDADELEAWLEEKEQL-LASEDLGKDLeSVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90 100
....*....|....*....|.
gi 1397727989 700 SLQARWSWLLQLVTCLDAHLK 720
Cdd:smart00150 81 ELNERWEELKELAEERRQKLE 101
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10478-10582 |
1.23e-08 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 56.56 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10478 RLAEEFHKKAQQLLSWLADAERQLHyRGPIPDEEPLILQQMEEHKKFEESLLRQEANLRETLNIGQDIMKRCHPDSvPIM 10557
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKEALLS-SEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS-EEI 78
|
90 100
....*....|....*....|....*
gi 1397727989 10558 KQWLSVIRARWEELTALGRQRSARL 10582
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9238-9869 |
1.32e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9238 KKLQDYCKGEDVI----MIQLKIDGVQKQNGELRSHIEdcleQMEEALPLAKHFQ------EAHAEFLSWASKVEPELRA 9307
Cdd:PTZ00121 1030 EELTEYGNNDDVLkekdIIDEDIDGNHEGKAEAKAHVG----QDEGLKPSYKDFDfdakedNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9308 LELGVPDEETNIEElANQLTEEMQPLLDIINSEGAELAEVA-------PGDAGLRVEDI----INR---DNKRFDNLRDQ 9373
Cdd:PTZ00121 1106 TETGKAEEARKAEE-AKKKAEDARKAEEARKAEDARKAEEArkaedakRVEIARKAEDArkaeEARkaeDAKKAEAARKA 1184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9374 IE-KRAQKVQLARQ-RSSEVVNELGDLVDwfVDADSRLQNQQPIAS--DLDLLQQQLAEQKVMNEEINNQKVKARDTLSA 9449
Cdd:PTZ00121 1185 EEvRKAEELRKAEDaRKAEAARKAEEERK--AEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9450 SKKLLSDSAMEDNSAirNKMDELKQwVDTVSGSANERQSLLEQAVPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDA- 9528
Cdd:PTZ00121 1263 AHFARRQAAIKAEEA--RKADELKK-AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAe 1339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9529 -----DQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVqsmldddnRRMDNVRTKVRDRSNSIDQAM 9603
Cdd:PTZ00121 1340 eakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK--------KKADEAKKKAEEDKKKADELK 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9604 QQSAEftdklENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDL---EMRHNALESVKnaAEELLRQAgdEQD 9680
Cdd:PTZ00121 1412 KAAAA-----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeEAKKKAEEAKK--ADEAKKKA--EEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9681 EAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQ----------------EALSSVDQ 9744
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadelkkaEELKKAEE 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9745 PALEPEAIREQQEELEALKEDIEASQAdfEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAI--SDQYSKRSQELES 9822
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkAEEEKKKVEQLKK 1640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1397727989 9823 ALAQAVHFQDQLMKllvwlqEAEDEFSEFEPVASEFETIKKQWDELK 9869
Cdd:PTZ00121 1641 KEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8805-9309 |
1.54e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8805 EVDGGETSNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELEsELGSKTPVSRDD-AELGSQ 8883
Cdd:PRK02224 195 QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-TLEAEIEDLRETiAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8884 LADMKDfltRLGEKVETLKDLEQQASSLcnagyVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQ-HLTQAL 8962
Cdd:PRK02224 274 REELAE---EVRDLRERLEELEEERDDL-----LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQaHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8963 NLVWGDIDKASSTLDAMGPAGGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRqgqaliktAVAGSNTT--GLETDLES 9040
Cdd:PRK02224 346 SLREDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRE--------RFGDAPVDlgNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9041 LAERWAGLVEKVAEHEKNLDSALLRtgkfqdamaslldwLAETEELVAMQKAPSPEQRV-----VRAQLQEQKLVQKMVT 9115
Cdd:PRK02224 417 LREERDELREREAELEATLRTARER--------------VEEAEALLEAGKCPECGQPVegsphVETIEEDRERVEELEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9116 DRTpSMKAVQDSGNQLITGLDPAerKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTwlDAANKR 9195
Cdd:PRK02224 483 ELE-DLEEEVEEVEERLERAEDL--VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA--EAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9196 FTALEPHSpDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYckGEDVIMIQLKIDGVQKQNGELRSHIEDCLE 9275
Cdd:PRK02224 558 EAAAEAEE-EAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADA--EDEIERLREKREALAELNDERRERLAEKRE 634
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1397727989 9276 QMEEalpLAKHFQEA--------HAEFLSWASKVEPELRALE 9309
Cdd:PRK02224 635 RKRE---LEAEFDEArieearedKERAEEYLEQVEEKLDELR 673
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8267-8895 |
1.61e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 62.68 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8267 EMLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLAQKDRMLD-------VLGPVAMEPNMLASQM 8339
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEeqlkkqqLLKQLRARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8340 EQVKVLREELSAQEPTYDHFLNCAHgiLERCGDKSQDGIAvsrrldtvskawnKLQSRLNERSKNLSSVEGISVEFASLT 8419
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHIKA--VTQIEQQAQRIHT-------------ELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8420 ---RGLADWLSD---FSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKT----D 8489
Cdd:TIGR00618 342 eqrRLLQTLHSQeihIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTsafrD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8490 LRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNL--------QESEPLSSDLDILREQMR 8561
Cdd:TIGR00618 422 LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkeqihlQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8562 QNRTLQQELSLKEPEIRQL------------LEKGDKLVKESSPTT--EVRAIADKVGELQGEWTRLQQE---VTVQDSR 8624
Cdd:TIGR00618 502 EPCPLCGSCIHPNPARQDIdnpgpltrrmqrGEQTYAQLETSEEDVyhQLTSERKQRASLKEQMQEIQQSfsiLTQCDNR 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8625 LTMAGSHAQQFTERLDKmamWLQMtEEKLEKMKPEDVDQntvvhKLKELQGVQNEMMKKSHDR---ERLNSEGTSLV--- 8698
Cdd:TIGR00618 582 SKEDIPNLQNITVRLQD---LTEK-LSEAEDMLACEQHA-----LLRKLQPEQDLQDVRLHLQqcsQELALKLTALHalq 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8699 -----ECVDSGKEAIKQQVAVINERWDAVNKALSERASHL----EDLGQ---RLGEVQDSLAEATSALNKWENKLAVHNS 8766
Cdd:TIGR00618 653 ltltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAQcqtLLRELETHIEEYDREFNEIENASSSLGS 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8767 lGLSAKDPKHINRIKDLLEDTGW-LASQLNNTETMLNSIEVD---GGETSNLRDELNKLRGQHQTLQGELSELVAEM--- 8839
Cdd:TIGR00618 733 -DLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAAlqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgqe 811
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 8840 ------------ETGAQIVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGSQLADMKDFLTRLG 8895
Cdd:TIGR00618 812 ipsdedilnlqcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8812-9402 |
1.94e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8812 SNLRDELNKLRGQHQTLQgELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpVSRDDAELGSQLADMKDFL 8891
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-LEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8892 TRLGEKVETLKDLEQQASslcNAGYvSDPELLKSQVEALSNQHASLTERATQRQ--------------SDVVANQHSIQH 8957
Cdd:COG4913 316 ARLDALREELDELEAQIR---GNGG-DRLEQLEREIERLERELEERERRRARLEallaalglplpasaEEFAALRAEAAA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8958 LTQALNLVWGDIDKASSTLDAmgpaggnvtTVKALQEELkgfvkstmEPLQKQFESVSRQG------QALIKTAVAGSnt 9031
Cdd:COG4913 392 LLEALEEELEALEEALAEAEA---------ALRDLRREL--------RELEAEIASLERRKsniparLLALRDALAEA-- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9032 TGL-ETDLESLAE---------RWAGLVEKVaeheknldsalLRTGKF-----QDAMASLLDWLAET--EELVAMQKAPS 9094
Cdd:COG4913 453 LGLdEAELPFVGElievrpeeeRWRGAIERV-----------LGGFALtllvpPEHYAAALRWVNRLhlRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9095 PEQRVVRAQLQEQKLVQKMVTDRTP-------SM-------------------KAVQDSG------------------NQ 9130
Cdd:COG4913 522 GLPDPERPRLDPDSLAGKLDFKPHPfrawleaELgrrfdyvcvdspeelrrhpRAITRAGqvkgngtrhekddrrrirSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9131 LITGLDPAER-KHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAAnkrftALEphspdaEGI 9209
Cdd:COG4913 602 YVLGFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-----SAE------REI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9210 EHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQE 9289
Cdd:COG4913 671 AELEAELERLDASSDDLAALEEQLEELEAELEE---------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9290 AHAEFLSW----------ASKVEPELRA-LELGVPDEETNIEELANQLTEEMQpllDIINSEGAELAEVAPGDAGLRved 9358
Cdd:COG4913 742 LARLELRAlleerfaaalGDAVERELREnLEERIDALRARLNRAEEELERAMR---AFNREWPAETADLDADLESLP--- 815
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1397727989 9359 iinrdnkRFDNLRDQIEKR---AQKVQLARQRSSEVVNELGDLVDWF 9402
Cdd:COG4913 816 -------EYLALLDRLEEDglpEYEERFKELLNENSIEFVADLLSKL 855
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8633-8734 |
3.22e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 55.41 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8633 QQFTERLDKMAMWLQMTEEKLEKMKPEDvDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQV 8712
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGK-DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 8713 AVINERWDAVNKALSERASHLE 8734
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7553-7801 |
7.45e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 57.46 E-value: 7.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7553 ELAKFEEESKKFRTWMGAAFSELTnQEDYLKRFEDLKVLGEKHRELASDISSHQAdhrfmsmAVQKYMEEAKlyklemds 7632
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLS-STDYGDDLESVEALLKKHEALEAELAAHEE-------RVEALNELGE-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7633 fradrarparhSLISMECVAADNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDvAFKLLTWLTDMEGQLSSv 7712
Cdd:cd00176 65 -----------QLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALAS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7713 kQDAGlSEPQQLQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNSLSGQAAEQqqvakLQSTMNDLSVRYSTLTKDINS 7792
Cdd:cd00176 132 -EDLG-KDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE-----IEEKLEELNERWEELLELAEE 204
|
....*....
gi 1397727989 7793 HVTQLQAAV 7801
Cdd:cd00176 205 RQKKLEEAL 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9667-10094 |
7.63e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9667 AAEELLRQAGDEQDEaVKDVRQKLEELTKLYKDIQERGRGRQRALE--ETLAVAEKFWDELHALNSSLKDLQEALssvdq 9744
Cdd:COG4717 75 ELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERL----- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9745 palepEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAIsdqyskrsQELESAL 9824
Cdd:COG4717 149 -----EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL--------AELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9825 AQAvhfQDQLMKllvwLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRvepknVEIESLNQHVTELTKSSTPEQASVL 9904
Cdd:COG4717 216 EEA---QEELEE----LEEELEQLENELEAAALEERLKEARLLLLIAAAL-----LALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9905 REPMTQLNIRWNNLLtnigDRQRELQMALLTAGQFDHAHKELKNWMDLVDVtLDEITPVYGDPKLVEIELAKLRIVQNDI 9984
Cdd:COG4717 284 GLLALLFLLLAREKA----SLGKEAEELQALPALEELEEEELEELLAALGL-PPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9985 TAHQESVESISKEAQRLMTSEGIAQAQGLKTKMEDMEKtWENIQAKSRAKQDMLE--DGLREAQGFTGELQDILAKINDI 10062
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEelLGELEELLEALDEEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|..
gi 1397727989 10063 EGQLiiskpvgglpETAKEQLEKFMDVYAELE 10094
Cdd:COG4717 438 EEEL----------EELEEELEELREELAELE 459
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
391-618 |
7.81e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 57.07 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 391 AEKIQRESKQAGESLHDLERQIQEAEVRGDKQHPYEAKHNCDAMDRALHTIEENLRAMFRDVQTLQDNHFPQSQQLYTRI 470
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 471 SELQSRVSSLRTRLysgvvqpllsrayveegrtVTRRTEIMTEVRLVDTnpaFRHVQDCLDWIEAQQQMIVGQDYSSDLQ 550
Cdd:cd00176 82 EELNQRWEELRELA-------------------EERRQRLEEALDLQQF---FRDADDLEQWLEEKEAALASEDLGKDLE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 551 QVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAEEQ----KLYTQKLSSVEVAYSLLLNTSSRRLKFLES 618
Cdd:cd00176 140 SVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHpdadEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
8991-9720 |
1.28e-07 |
|
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: 59.68 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8991 ALQEELKGFVKSTMEPLQ-KQFESVSRQGQALiKTAVAGSNTTGLeTDLESLAERWAglvEKVAEHEKNLDSAL-LRTGK 9068
Cdd:TIGR00606 374 ATRLELDGFERGPFSERQiKNFHTLVIERQED-EAKTAAQLCADL-QSKERLKQEQA---DEIRDEKKGLGRTIeLKKEI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9069 FQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLitGLDPAERKHIEsELQ 9148
Cdd:TIGR00606 449 LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA--DLDRKLRKLDQ-EME 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9149 QLNSRWEALTKRVV---DRTAILEEVQGLAGEFQDVLDPLTTwlDAANKRFTALEPHSPDAEgIEHLIQELKKLQKEV-- 9223
Cdd:TIGR00606 526 QLNHHTTTRTQMEMltkDKMDKDEQIRKIKSRHSDELTSLLG--YFPNKKQLEDWLHSKSKE-INQTRDRLAKLNKELas 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9224 ---------NEHEPAMKQLATAGKKLQDYCKGED--VIMIQLK--IDGVQKQNGELR-------SHIEDCLEQMEEALPL 9283
Cdd:TIGR00606 603 leqnknhinNELESKEEQLSSYEDKLFDVCGSQDeeSDLERLKeeIEKSSKQRAMLAgatavysQFITQLTDENQSCCPV 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9284 AKHFQEAHAEFLSWASKVEPELRALelgvPDEETNIEELANQLTEEMQPLLDIINSEGAELAEVAPGDAGLRVED-IINR 9362
Cdd:TIGR00606 683 CQRVFQTEAELQEFISDLQSKLRLA----PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNR 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9363 DNKRFDNLRDQIEKRAQKVqLARQRSSEV----VNELGDLVDWFVDADSRLQNQ--QPIASDLDLLQQQLAEQKvmnEEI 9436
Cdd:TIGR00606 759 DIQRLKNDIEEQETLLGTI-MPEEESAKVcltdVTIMERFQMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEK---QEK 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9437 NNQKVKARDTLSASKKLLSDSaMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHTELVVWLDDVEP 9516
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9517 VLSELDvlsvdadqvKKQQEKAKVLKQEVADRKPIVDRLNktgtalvamcgskgaeQVQSMLDDDNRRMDNVRTKVRDRS 9596
Cdd:TIGR00606 914 LETFLE---------KDQQEKEELISSKETSNKKAQDKVN----------------DIKEKVKNIHGYMKDIENKIQDGK 968
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9597 NsiDQAMQQsaeftdklENMLDTLTVTAEQV-RSAEPISAQPDKLREQIEENKAMEEDLE------MRHNALESVKNAAE 9669
Cdd:TIGR00606 969 D--DYLKQK--------ETELNTVNAQLEECeKHQEKINEDMRLMRQDIDTQKIQERWLQdnltlrKRENELKEVEEELK 1038
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 9670 ELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEK 9720
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10157-10258 |
1.30e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 53.86 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10157 FHGELNKFISWLTDTEKTLNNlQPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKYfSQKQDVVLIKNLLS 10236
Cdd:pfam00435 6 FFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLID-EGHYASEEIQERLE 83
|
90 100
....*....|....*....|..
gi 1397727989 10237 SIQHRWEKIVSRSAERTRHLER 10258
Cdd:pfam00435 84 ELNERWEQLLELAAERKQKLEE 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9571-9827 |
1.95e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9571 AEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEP----ISAQPDKLREQIEE 9646
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleeLEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9647 NKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELH 9726
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9727 ALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTgdtllgmvGTTEQPEVQKNVDDAGASL 9806
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--------LLEEAALLEAALAELLEEL 486
|
250 260
....*....|....*....|.
gi 1397727989 9807 AAISDQYSKRSQELESALAQA 9827
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFL 507
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9358-10050 |
2.09e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9358 DIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNelgdlvdwfvDADSRLQNQQPIASDLDLLQQQLAEQKVMNEEIN 9437
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLE----------DSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9438 NQKVKARDTLSASKkllsdsamednsaIRNKmdelkqwvdtvsGSAnerqslleqavpFARHFHEAHTELVVWLDDVEPV 9517
Cdd:pfam15921 201 GKKIYEHDSMSTMH-------------FRSL------------GSA------------ISKILRELDTEISYLKGRIFPV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9518 LSELDVLSVDAdqvkkqQEKAKVLKQEVADRkpivdrlnktgtalvamcgskgAEQVQSMLDDDNRRMDNVRTKVRDRSN 9597
Cdd:pfam15921 244 EDQLEALKSES------QNKIELLLQQHQDR----------------------IEQLISEHEVEITGLTEKASSARSQAN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9598 SI--------DQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPIsaqpdkLREQIEEnkaMEEDLEMRHNALESVKNAAE 9669
Cdd:pfam15921 296 SIqsqleiiqEQARNQNSMYMRQLSDLESTVSQLRSELREAKRM------YEDKIEE---LEKQLVLANSELTEARTERD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9670 ELLRQAGDEQDEAVK---DVRQKLEELTkLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPA 9746
Cdd:pfam15921 367 QFSQESGNLDDQLQKllaDLHKREKELS-LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9747 LEPE--AIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEvqKNVDDAGASLaaisdqySKRSQELESAL 9824
Cdd:pfam15921 446 MERQmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE--RTVSDLTASL-------QEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9825 AQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASEFETIKKQWDElknfktrvepKNVEIESLNQHVTELTK--SSTPEQAS 9902
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAE----------KDKVIEILRQQIENMTQlvGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9903 VLREPMTQLNirwnnllTNIGDRQRELQmalltagqfdhahkELKNWMDLVDVTLDEItpvygDPKLVEIELAKLRIVqN 9982
Cdd:pfam15921 587 AMQVEKAQLE-------KEINDRRLELQ--------------EFKILKDKKDAKIREL-----EARVSDLELEKVKLV-N 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9983 DITAHQESVESISKEAQRL-------------MTSEGIAQAQGLKTKMEDMEKTWENIQAKSRAKQDMLE---DGLREAQ 10046
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLlnevktsrnelnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEqtrNTLKSME 719
|
....
gi 1397727989 10047 GFTG 10050
Cdd:pfam15921 720 GSDG 723
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10043-10149 |
2.68e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 52.71 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10043 REAQGFTGELQDILAKINDIEgQLIISKPVGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLgGKSKGPALANL 10122
Cdd:pfam00435 1 LLLQQFFRDADDLESWIEEKE-ALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKL-IDEGHYASEEI 78
|
90 100
....*....|....*....|....*..
gi 1397727989 10123 RQNLQHLNQRCDYIRSRACDRKKKLED 10149
Cdd:pfam00435 79 QERLEELNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9608-9712 |
2.94e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 52.72 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9608 EFTDKLENMLDTLTvTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLrqagDEQDEAVKDVR 9687
Cdd:smart00150 2 QFLRDADELEAWLE-EKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI----EEGHPDAEEIE 76
|
90 100
....*....|....*....|....*
gi 1397727989 9688 QKLEELTKLYKDIQERGRGRQRALE 9712
Cdd:smart00150 77 ERLEELNERWEELKELAEERRQKLE 101
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1084-1275 |
4.58e-07 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 55.14 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 1084 LDDVKQMIHDYQHTLASQDNAtSDLSSLKLAHTELTDVQTSMKQQQPRIEHLKSDVSSLRVLveksrsgvtSHHDLDAVE 1163
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE---------GHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 1164 REVINLASQWATVSSQAAERLQMVRSIQDLLSMYEHGLgAEEQWLEQIQKTVASQPPlTGDVVDAKNQLQTTMAIYNRLV 1243
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDAD-DLEQWLEEKEAALASEDL-GKDLESVEELLKKHKELEEELE 156
|
170 180 190
....*....|....*....|....*....|..
gi 1397727989 1244 ERKHQIEAVNRLGGQYIREAKIFEKKQTKYRQ 1275
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
9938-10040 |
5.67e-07 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 51.94 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9938 QFDHAHKELKNWMDLVDVTLDEiTPVYGDPKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTSEGIAQAQgLKTKM 10017
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE-IQERL 82
|
90 100
....*....|....*....|...
gi 1397727989 10018 EDMEKTWENIQAKSRAKQDMLED 10040
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
151-256 |
6.12e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.02 E-value: 6.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21313 8 TPKQRLLGWIQNKI---PYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVIT 84
|
90 100
....*....|....*....|....*..
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSlydvFPQ 256
Cdd:cd21313 85 PEEIIHPDVDEHSVMTYLSQ----FPK 107
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7436-8089 |
6.29e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.42 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7436 RLADSFDSIVQELMTEQEhLGDLEQILKHDSQMGDEASKVK---LQLEAHKSTHEKIQSQQQPILSLVYKAEQLTENYQE 7512
Cdd:pfam05483 52 QVANSGDCHYQEGLKDSD-FENSEGLSRLYSKLYKEAEKIKkwkVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7513 ELTPEQVTQLTTQASLLKatlekvSKTSERRLSHLTK-----AADELAKFEEESKKFRTwmgaAFSELTNQ-EDYLKRFE 7586
Cdd:pfam05483 131 KVSLKLEEEIQENKDLIK------ENNATRHLCNLLKetcarSAEKTKKYEYEREETRQ----VYMDLNNNiEKMILAFE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7587 DLKVlgekhrelasdisshQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRARPARHSLISMECVAADNVKDKLTDLTEE 7666
Cdd:pfam05483 201 ELRV---------------QAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7667 YHDlsnRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLS-SVKQDAGLSEpqQLQVHLDRLKSLSMDALSQkllL 7745
Cdd:pfam05483 266 SRD---KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrSMSTQKALEE--DLQIATKTICQLTEEKEAQ---M 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7746 DEMQKrgqdltnslsGQAAEQQQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAVTHSQDITQAMNELVSWMDSAEqvv 7825
Cdd:pfam05483 338 EELNK----------AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE--- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7826 ttqlpislrrpelnAQLQSFSAVDADVTNHQSALDAVKALANELVKTCE--LDIARAVEQRLTSLDEKFSSLQAKCRQRD 7903
Cdd:pfam05483 405 --------------VELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQelIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7904 RDLEEVDSSLRefQEKLEQTNLWVHDGILQLDSKELSKLSSD---DMKQQLEKLAREKHNRLRTIQEIQVAAEQLLQdpr 7980
Cdd:pfam05483 471 KEVEDLKTELE--KEKLKNIELTAHCDKLLLENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMN--- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7981 tgegeavknlvsdLKKNLEAFDSLLAAKENEASDKEQQGAdfENAKTIALLWLSQMEARLDEFQPVAIDVGIVEQQKMEL 8060
Cdd:pfam05483 546 -------------LRDELESVREEFIQKGDEVKCKLDKSE--ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
650 660
....*....|....*....|....*....
gi 1397727989 8061 QPMLQEYEDYAPKIDEVNDLGNAYEAMIN 8089
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVN 639
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
168-248 |
6.99e-07 |
|
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: 52.09 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 168 PGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLDPEDVDVPNPDEKSILTY 246
Cdd:cd21315 30 PDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIKPEEMVNPKVDELSMMTY 109
|
..
gi 1397727989 247 VS 248
Cdd:cd21315 110 LS 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7743-8614 |
7.17e-07 |
|
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: 57.37 E-value: 7.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7743 LLLDEMQKRGQDLTNSLSGQAAEQQQVAKLQSTMNDLSVRYSTLtkdiNSHVTQLQAAVTHSQDITQAMNELVSWMDSAE 7822
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL----RLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7823 QVvttqlpISLRRPELNAQLQsfsAVDADVTNHQSALDAVKALANELvktceldiaravEQRLTSLDEKFSSLQAKCRQR 7902
Cdd:TIGR02168 305 QI------LRERLANLERQLE---ELEAQLEELESKLDELAEELAEL------------EEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7903 DRDLEEVDSSLREFQEKLEQTNLWVHDGILQLDS--KELSKLSSDdmKQQLEklarekHNRLRTIQEIqvaaEQLLQDPR 7980
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASlnNEIERLEAR--LERLE------DRRERLQQEI----EELLKKLE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7981 TGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWLSQMEARLDEfqpvaidvgiveqqkmeL 8060
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS-----------------L 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8061 QPMLQEYEDYAPKIDEV----NDLG-------------NAYEAMI----------------NPGDRPISPIR--RIGRSR 8105
Cdd:TIGR02168 495 ERLQENLEGFSEGVKALlknqSGLSgilgvlselisvdEGYEAAIeaalggrlqavvvenlNAAKKAIAFLKqnELGRVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8106 RLPgilsprLRSPSPTFPTSPSTQRAsplssessGVSSRKSSADNLLLDDLSEVQQQLLDITQRYEIVgERLADRQQELQ 8185
Cdd:TIGR02168 575 FLP------LDSIKGTEIQGNDREIL--------KNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV-DDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8186 LMLTSIRTFMQDMQDIL-QWLDLKDHETDSAQPLPTnekdaKKRLKEHEvfhREILSKEGLVEDIRKKAQDLLKtrhgvp 8264
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLVRpGGVITGGSAKTNSSILER-----RREIEELE---EKIEELEEKIAELEKALAELRK------ 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8265 geemlqqQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQQLtlwlaqkdrmldvlgpvamepnmlASQMEQVKV 8344
Cdd:TIGR02168 706 -------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL------------------------EERIAQLSK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8345 LREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaVSRRLDTVSKAWNKLQSRLNERSKNLSSVegiSVEFASLTRGLAD 8424
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEE---LEAQIEQLKEELKALREALDELRAELTLL---NEEAANLRERLES 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8425 WLSDFSDKldgqgkvssqpdkqHKQLQELKQLESELIVQQPRLARARDlcrqlcdkakdastktDLRSKLTALEKDMNDT 8504
Cdd:TIGR02168 829 LERRIAAT--------------ERRLEDLEEQIEELSEDIESLAAEIE----------------ELEELIEELESELEAL 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8505 TRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLdilreQMRQNRTLQQELSLKEpeirQLLEKG 8584
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL-----ELRLEGLEVRIDNLQE----RLSEEY 949
|
890 900 910
....*....|....*....|....*....|....*
gi 1397727989 8585 -----DKLVKESSPTTEVRAIADKVGELQGEWTRL 8614
Cdd:TIGR02168 950 sltleEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8155-8908 |
7.65e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8155 DLSEVQQQLLDITQRYEIVGERLADRQQELQLMLTSIRTFMQDMQDILQwLDLKDHETDSAQ------PLPTNEKDAKKR 8228
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK-EKIGELEAEIASlersiaEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8229 LKEHEVFHREILSK-EGLVEDIRKKAQDL--LKTRHGVPGEEM--LQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRD 8303
Cdd:TIGR02169 324 LAKLEAEIDKLLAEiEELEREIEEERKRRdkLTEEYAELKEELedLRAELEEVDKEFAETRDELKDYREKLEKLKREINE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8304 MREHEQQLTLWLAQKD-RMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEptydhflncahGILERCgdkSQDGIAVSR 8382
Cdd:TIGR02169 404 LKRELDRLQEELQRLSeELADLNAAIAGIEAKINELEEEKEDKALEIKKQE-----------WKLEQL---AADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8383 RLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGqgkvssqpdkQHKQLQELKQLESELIV 8462
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG----------VHGTVAQLGSVGERYAT 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8463 QQPRLARAR--------DLCRQLCD---KAKDASTKTDLrskltALEKdMNDTTRKLEIC--KAAVEEASQQAE---KFE 8526
Cdd:TIGR02169 540 AIEVAAGNRlnnvvvedDAVAKEAIellKRRKAGRATFL-----PLNK-MRDERRDLSILseDGVIGFAVDLVEfdpKYE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8527 ADCKELLtwiseaannlqESEPLSSDLDILREQMRQNR--TLQQELSLKEPEIR--QLLEKGDKLVKESSPtTEVRAIAD 8602
Cdd:TIGR02169 614 PAFKYVF-----------GDTLVVEDIEAARRLMGKYRmvTLEGELFEKSGAMTggSRAPRGGILFSRSEP-AELQRLRE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8603 KVGELQGEWTRLQQEVTVQDSRL---------------------TMAGSHAQQFTERLDKMAMWLQMTEEKLEKMKPEdv 8661
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLdelsqelsdasrkigeiekeiEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE-- 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8662 dQNTVVHKLKELQGVQNEMMKKSHDRERlnSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLG 8741
Cdd:TIGR02169 760 -LKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8742 EVQDSLAEATSalNKWENKLAVHNSLGLSAKdpkhinrikdlledtgwLASQLNNTETMLNSIEvdgGETSNLRDELNKL 8821
Cdd:TIGR02169 837 ELQEQRIDLKE--QIKSIEKEIENLNGKKEE-----------------LEEELEELEAALRDLE---SRLGDLKKERDEL 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8822 RGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGsqlaDMKDFLTRLGEKVETL 8901
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----DVQAELQRVEEEIRAL 970
|
....*..
gi 1397727989 8902 KDLEQQA 8908
Cdd:TIGR02169 971 EPVNMLA 977
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
9144-9671 |
8.62e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9144 ESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEPHSPDAEGIEHLIQELKK----L 9219
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereeL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9220 QKEVNEHEPAMKQLATAGKKLQDYCKGE--DVIMIQLKIDGVQKQNGELRSHIEDC-------LEQMEEALPLAKHFQEA 9290
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDdaDAEAVEARREELEDRDEELRDRLEECrvaaqahNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9291 HAEFLSWASKVEPELRALELGVPDEETNIEELANQLTEemqplldiiNSEGAELAEVAPGDAGLRVEDIinRDNKrfDNL 9370
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEE---------LRERFGDAPVDLGNAEDFLEEL--REER--DEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9371 RDQIEKRAQKVQLARQRSSEVVN--------ELGDLVDWFVDADSRLQNQQPIASdldlLQQQLAEQKVMNEEINNQKVK 9442
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEAlleagkcpECGQPVEGSPHVETIEEDRERVEE----LEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9443 ARDTLSASKKLlsdsamednSAIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhFHEAHTELVVWLDDVEPVLSELd 9522
Cdd:PRK02224 501 AEDLVEAEDRI---------ERLEERREDLEELIAERRETIEEKRERAEE-------LRERAAELEAEAEEKREAAAEA- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9523 vlsvdADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGT--ALVAMCGSKgAEQVQSMLDDDNRRMDNVRTKVRDRS---- 9596
Cdd:PRK02224 564 -----EEEAEEAREEVAELNSKLAELKERIESLERIRTllAAIADAEDE-IERLREKREALAELNDERRERLAEKRerkr 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9597 --------NSIDQAMQQSAEFTDKLENMLDTLTVTAEQ---VRSAepISAQPDKLrEQIEENKAMEEDLEMRHNALESVK 9665
Cdd:PRK02224 638 eleaefdeARIEEAREDKERAEEYLEQVEEKLDELREErddLQAE--IGAVENEL-EELEELRERREALENRVEALEALY 714
|
....*.
gi 1397727989 9666 NAAEEL 9671
Cdd:PRK02224 715 DEAEEL 720
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
9389-9899 |
8.82e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.65 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9389 SEVVNELGDLVDWFVDADSRL-QNQQPIASDLDLLQqqlAEQKVMNE-EINNQKV--KARDTLSASKKLLsdsamEDNSA 9464
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELkQKENKLQENRKIIE---AQRKAIQElQFENEKVslKLEEEIQENKDLI-----KENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9465 IRNKMDELKQwvdTVSGSAnERQSLLEqavpfarhfHEAHTELVVWLD---DVEPVLSELDVLSVDAD--------QVKK 9533
Cdd:pfam05483 153 TRHLCNLLKE---TCARSA-EKTKKYE---------YEREETRQVYMDlnnNIEKMILAFEELRVQAEnarlemhfKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9534 QQEKAKVLKQEVadRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNR-RMDNVRTKVRDRSNSIDQAMQQSAEFTDK 9612
Cdd:pfam05483 220 DHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRdKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9613 LENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENK--AMEEDLEMR--HN----ALESVKNAAEELLRQAgdeqdeavk 9684
Cdd:pfam05483 298 LEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKeaQMEELNKAKaaHSfvvtEFEATTCSLEELLRTE--------- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9685 dvRQKLE-----------ELTKLYKDIQERGR---GRQRALEE---TLAVAEKFWDElhalNSSLKDLQEALSSVDQPAL 9747
Cdd:pfam05483 369 --QQRLEknedqlkiitmELQKKSSELEEMTKfknNKEVELEElkkILAEDEKLLDE----KKQFEKIAEELKGKEQELI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9748 EPEAIREQQ-------------------EELEALKEDIEASQADFEEVQQTGDTLLgmvgtTEQPEVQKNVDDAGASLAA 9808
Cdd:pfam05483 443 FLLQAREKEihdleiqltaiktseehylKEVEDLKTELEKEKLKNIELTAHCDKLL-----LENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9809 ISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEF-------------SEFEPVASEFETIKKQ------WDELK 9869
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgdevkckldkSEENARSIEYEVLKKEkqmkilENKCN 597
|
570 580 590
....*....|....*....|....*....|
gi 1397727989 9870 NFKTRVEPKNVEIESLNQHVTELTKSSTPE 9899
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
15-250 |
9.25e-07 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 56.49 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 15 PKTPFVQYEEARLRDTDERDAVQKKTFTKWVNKHLMKAglRIIDLFDDLRDGhnlISLLEVLAHDILPRERGH------- 87
Cdd:COG5069 358 GQEPLEEEEKPEIEEFDAEGEFEARVFTFWLNSLDVSP--EITNLFGDLRDQ---LILLQALSKKLMPMTVTHklvkkqp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 88 ------MRFHKIQNVQIALDYLRLKGIRLVNIRSDEIVDGNpKLTLGLIW-------TIILHFQISDVVVPGQEDISARE 154
Cdd:COG5069 433 asgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGCGLSDSDLCAWL 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 155 ALLLWSRRTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSN----SNKQNLELAFTVAEKEFGVTRLLdP 230
Cdd:COG5069 512 GSLGLKGDKEEGIRSFGDPAGSVSGVFYLDVLKGIHSELVDYDLVTRGFTEfddiADARSLAISSKILRSLGAIIKFL-P 590
|
250 260
....*....|....*....|
gi 1397727989 231 EDVDVPNPdEKSILTYVSSL 250
Cdd:COG5069 591 EDINGVRP-RLDVLTFIESL 609
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8425-8962 |
1.16e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8425 WLSDFSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDT 8504
Cdd:TIGR00618 244 YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8505 TRKLEICKAAV------EEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLKEPEIR 8578
Cdd:TIGR00618 324 AKLLMKRAAHVkqqssiEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8579 QLLE---KGDKLVKESSPTTEVRAIADKVGELQGEWTRLQQE-VTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKLE 8654
Cdd:TIGR00618 404 ILQReqaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8655 KmkpEDVDQNTVVHKLKELQGVQNEMMKK-SHDRERLNSEGTSLVECvdSGKEAIKQQVAVINERWDAVNKALSERASHL 8733
Cdd:TIGR00618 484 Q---ETRKKAVVLARLLELQEEPCPLCGScIHPNPARQDIDNPGPLT--RRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8734 EDLGQRLGEVQDSLAEATSALNKwenklavhnslgLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEVDGGETSN 8813
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNR------------SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8814 LRDELNKLRGQHQTLQGELSELVAEMETGAQiVEQFQGLLKIVGGQFLELESELGSKTPVSRDDAELGSQLADMKDFLTR 8893
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQLTLTQ-ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 8894 LGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVVANQHSIQHLTQAL 8962
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAAL 774
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9529-10046 |
1.24e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9529 DQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAmcgskgAEQVQSMLDDDNRRMDNVRtKVRDRSNSIDQAMQQSAE 9608
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEE------LEAELEELREELEKLEKLL-QLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9609 FTDKLEnmldtltvtaeqvrsaepisaqpdKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQ 9688
Cdd:COG4717 144 LPERLE------------------------ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9689 KLEELtklykdiqergRGRQRALEETLAVAEkfwDELHALNSSLKDLQEalssvdqpALEPEAIREQQEELEALKEdIEA 9768
Cdd:COG4717 200 ELEEL-----------QQRLAELEEELEEAQ---EELEELEEELEQLEN--------ELEAAALEERLKEARLLLL-IAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9769 SQADFEEVQQTGDTLLGMVGtteqpevqkNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKL--LVWLQEAED 9846
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIA---------GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELeeEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9847 EFSEFEPVASEFETIKKQWDELKNFKTRVEPKN--VEIESLNQHVTELTKSSTPEQASVLREPMTQLNiRWNNLLtnigD 9924
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEeeLQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELK----E 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9925 RQRELQMALLTAGQFDHAhkelknwmDLVDVTLDEItpvygDPKLVEIElAKLRIVQNDITAHQESVESISKEAQRLMTS 10004
Cdd:COG4717 403 ELEELEEQLEELLGELEE--------LLEALDEEEL-----EEELEELE-EELEELEEELEELREELAELEAELEQLEED 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1397727989 10005 EGIAQA----QGLKTKMEDMEKTWeniqAKSRAKQDMLEDGLREAQ 10046
Cdd:COG4717 469 GELAELlqelEELKAELRELAEEW----AALKLALELLEEAREEYR 510
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9829-9930 |
1.89e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.41 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9829 HFQDQLMKLLVWLQEAEdEFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSStPEQASVLREPM 9908
Cdd:smart00150 2 QFLRDADELEAWLEEKE-QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG-HPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 9909 TQLNIRWNNLLTNIGDRQRELQ 9930
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
8392-8907 |
2.98e-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: 55.11 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8392 NKLQSRLNERSKNLSSvegiSVEFAS-LTRGLADWlsdfsdKLDGQGKVSSQpdkqhKQLQELKQLESELIVQqprLARA 8470
Cdd:pfam05483 271 NQLEEKTKLQDENLKE----LIEKKDhLTKELEDI------KMSLQRSMSTQ-----KALEEDLQIATKTICQ---LTEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8471 RDLCRQLCDKAKDAST--KTDLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEP 8548
Cdd:pfam05483 333 KEAQMEELNKAKAAHSfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8549 LSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEKGDKLVKE-----SSPTTEVRAIADKVGELQGEWTRLQQEVTVQDS 8623
Cdd:pfam05483 413 ILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDleiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8624 RLTMAGSHAQQFTERLDKMAMWLQMTEEKL-------EKM-KPEDVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGT 8695
Cdd:pfam05483 493 HCDKLLLENKELTQEASDMTLELKKHQEDIinckkqeERMlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8696 SLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLavhNSLGLSAKDPK 8775
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKV---NKLELELASAK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8776 H-----INRIKDLLEDtgwlasQLNNTETMLNSIE---VDGGETSNLRDELNKlRGQHQtlqgeLSELVAEMETGAQive 8847
Cdd:pfam05483 650 QkfeeiIDNYQKEIED------KKISEEKLLEEVEkakAIADEAVKLQKEIDK-RCQHK-----IAEMVALMEKHKH--- 714
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 8848 QFQGLLKivggqflELESELG----SKTPVSRDDAELGSQLADMKDFLTRLGEKVETLKDLEQQ 8907
Cdd:pfam05483 715 QYDKIIE-------ERDSELGlyknKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9374-10069 |
3.02e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9374 IEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTL-SASKK 9452
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAhIKAVT 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9453 LLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAvPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDADQVK 9532
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQR-RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9533 KQQEKAKVLKQEVADRKPIVDRLNktgtalvamcgskgAEQVQSMldddnrrmdnvrtkVRDRSNSIDQAMQQSAEFTDK 9612
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSLCKELDILQ--------------REQATID--------------TRTSAFRDLQGQLAHAKKQQE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9613 LENMLDTLTVTAEQVRSAEPISAQP--DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKL 9690
Cdd:TIGR00618 435 LQQRYAELCAAAITCTAQCEKLEKIhlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9691 EELTKLYkdIQERGRGRQRALEETLAVAEKFWDEL-HALNSSLKDLQEalssvdqpaLEPEAIREQQEEL------EALK 9763
Cdd:TIGR00618 515 PARQDID--NPGPLTRRMQRGEQTYAQLETSEEDVyHQLTSERKQRAS---------LKEQMQEIQQSFSiltqcdNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9764 EDIEASQADFEEVQQTGDTLL----GMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLV 9839
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSeaedMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9840 WLQEAEDEFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTpEQASVLREPMTQLNIRwNNLL 9919
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFN-EIENASSSLGSDLAAR-EDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9920 TNIGDRQRELQMALLTAGQFDHAHKELKNWMDLvdVTLDEITPVYGDPKLvEIELAKLRIVQNDITAHQESVESISKEAQ 9999
Cdd:TIGR00618 742 NQSLKELMHQARTVLKARTEAHFNNNEEVTAAL--QTGAELSHLAAEIQF-FNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 10000 RLMTSEGIAQA-QGLKTKMEDMEKTWENIQ------AKSRAKQDMLEDGLREAQGFTGELQDILAKINDIEGQLIIS 10069
Cdd:TIGR00618 819 LNLQCETLVQEeEQFLSRLEEKSATLGEIThqllkyEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIK 895
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9032-9689 |
3.06e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9032 TGLEtDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVamqKAPSPEQRVVRAQLQeqklvq 9111
Cdd:PRK03918 155 LGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI---NEISSELPELREELE------ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9112 kMVTDRTPSMKAVQDSGNQL--ITGLDPAERKHIESELQQLNSRWEALTKRVVD---RTAILEEVQGLAGEFQDVLDPLT 9186
Cdd:PRK03918 225 -KLEKEVKELEELKEEIEELekELESLEGSKRKLEEKIRELEERIEELKKEIEEleeKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9187 TWLDAANKRFTALEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYCKG-EDVIMIQLKIDGVQKQNGE 9265
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLKKRLTG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9266 LRshIEDCLEQMEEAlplakhfQEAHAEFLSWASKVEPELRALELGVPDEETNIEEL----------ANQLTEEMQplLD 9335
Cdd:PRK03918 384 LT--PEKLEKELEEL-------EKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcGRELTEEHR--KE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9336 IINSEGAELAEvapgdaglrvediINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELgDLVDWFVDADSRLQnqqpi 9415
Cdd:PRK03918 453 LLEEYTAELKR-------------IEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLK----- 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9416 ASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKL--LSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQA 9493
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeeLKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9494 VPFARHFHEAHTELVVWLDDVEPVLSELdvlsvdadqvKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQ 9573
Cdd:PRK03918 594 LKELEPFYNEYLELKDAEKELEREEKEL----------KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9574 VQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQsaefTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEED 9653
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEELEKRREEIKKT----LEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
650 660 670
....*....|....*....|....*....|....*.
gi 1397727989 9654 lemrhNALESVKNAAEELLRQAGDEQDEAVKDVRQK 9689
Cdd:PRK03918 740 -----RALSKVGEIASEIFEELTEGKYSGVRVKAEE 770
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
35-137 |
3.65e-06 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. 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: 409155 Cd Length: 121 Bit Score: 50.11 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMRF----HKIQNVQIALDYLRLKGIRL 110
Cdd:cd21306 15 NVVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPK 94
|
90 100
....*....|....*....|....*..
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHF 137
Cdd:cd21306 95 PKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8154-8943 |
3.67e-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: 55.06 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8154 DDLSEVQQQLLdiTQRYEIVGERLADRQQEL---QLMLTSIRTFMQDMQDILQWLDLKDHETDSAQplptneKDAKKRLK 8230
Cdd:TIGR02168 220 AELRELELALL--VLRLEELREELEELQEELkeaEEELEELTAELQELEEKLEELRLEVSELEEEI------EELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8231 EHEvfhREILSKEGLVEDIRKKAQDLLKTRHGVPGE-EMLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQ 8309
Cdd:TIGR02168 292 ALA---NEISRLEQQKQILRERLANLERQLEELEAQlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8310 QL-TLWLAQKDRMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCgdKSQDGIAVSRRLDTVS 8388
Cdd:TIGR02168 369 ELeSRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8389 KAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRLA 8468
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLS 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8469 rarDLCRqlCDKAKDASTKTDLRSKLTALekdmndTTRKLEICKAAVEEASQQAekfeadcKELLTWIseAANNLQESEP 8548
Cdd:TIGR02168 527 ---ELIS--VDEGYEAAIEAALGGRLQAV------VVENLNAAKKAIAFLKQNE-------LGRVTFL--PLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8549 LSSDLDILrEQMRQNRTLQQELSLKEPEIRQLLEKgdkLVKESSPTTEVRAIADKVGELQGEWTRlqqeVTVQDSRLT-- 8626
Cdd:TIGR02168 587 QGNDREIL-KNIEGFLGVAKDLVKFDPKLRKALSY---LLGGVLVVDDLDNALELAKKLRPGYRI----VTLDGDLVRpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8627 --MAGSHAQQFTERLDKMAMwLQMTEEKLEKMKPEDVDQNTvvhKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSG 8704
Cdd:TIGR02168 659 gvITGGSAKTNSSILERRRE-IEELEEKIEELEEKIAELEK---ALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8705 KEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNSLGLSAKDpkhinRIKDLL 8784
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-----ALDELR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8785 EDTGWLASQLNNTETMLNSIEVDGGETsnlRDELNKLRGQHQTLQGELSELVAEME----TGAQIVEQFQGLLKIVGGQF 8860
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAAT---ERRLEDLEEQIEELSEDIESLAAEIEeleeLIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8861 LELESELGSKTPVSRDDAELGSQLADMKDFLTRLGEKVETLK--------DLEQQASSLcNAGYVSDPELLKSQVEALSN 8932
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEELREKLAQLElrleglevRIDNLQERL-SEEYSLTLEEAEALENKIED 965
|
810
....*....|.
gi 1397727989 8933 QHASLTERATQ 8943
Cdd:TIGR02168 966 DEEEARRRLKR 976
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9635-9829 |
4.39e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9635 AQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDeaVKDVRQKLEELTKLYKDIqERGRGRQRALEET 9714
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERL-DASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9715 LAVAEKfwdELHALNSSLKDLQEALSSVDQpalEPEAIREQQEELEALKEDIEASQAdfEEVQQTGDTLLgmvgttEQPE 9794
Cdd:COG4913 694 LEELEA---ELEELEEELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAEDLAR--LELRALLEERF------AAAL 759
|
170 180 190
....*....|....*....|....*....|....*
gi 1397727989 9795 VQKNVDDAGASLAAISDQYSKRSQELESALAQAVH 9829
Cdd:COG4913 760 GDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
10596-10651 |
5.36e-06 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 49.24 E-value: 5.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 10596 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 10651
Cdd:pfam00435 10 ADDLESWIEEKEALLSSED---YGKDLESVQALLKKHKALEAELAAHQDRVEALNE 62
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8544-9768 |
5.48e-06 |
|
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: 54.41 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8544 QESEPLSSDLDILREQMRQnrtLQQELSLKEPEIR--QLLEKGDKLVKESSPTTEVRAIADKV-GELQGEWTRLQQEVTV 8620
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQ---QKAESELKELEKKhqQLCEEKNALQEQLQAETELCAEAEEMrARLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8621 QDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKLEKmkPEDVDQntvvhKLkELQGVQNEMMKKSHDRERLNSEgtslvec 8700
Cdd:pfam01576 80 LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQ-----KL-QLEKVTTEAKIKKLEEDILLLE------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8701 vdsgkeaikqqvavinerwDAVNKALSERaSHLEDlgqRLGEVQDSLA---EATSALNKWENKlavHNSLglsakdpkhI 8777
Cdd:pfam01576 145 -------------------DQNSKLSKER-KLLEE---RISEFTSNLAeeeEKAKSLSKLKNK---HEAM---------I 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8778 NRIKDLL--EDTGWLasqlnntETMLNSIEVDGgetsnlrdELNKLRGQHQTLQGELSELVAEMetgAQIVEQFQGLLki 8855
Cdd:pfam01576 190 SDLEERLkkEEKGRQ-------ELEKAKRKLEG--------ESTDLQEQIAELQAQIAELRAQL---AKKEEELQAAL-- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8856 vggqfLELESELGSKTPVSRDDAELGSQLADMKDFLTR---LGEKVETLK-DLEQQAsslcnagyvsdpELLKSQVEALS 8931
Cdd:pfam01576 250 -----ARLEEETAQKNNALKKIRELEAQISELQEDLESeraARNKAEKQRrDLGEEL------------EALKTELEDTL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8932 NQHASLTERATQRQSDVVANQHSIQHLTQALNLVWGDIDKASSTldamgpaggnvtTVKALQEELKGF--VKSTMEPLQK 9009
Cdd:pfam01576 313 DTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQ------------ALEELTEQLEQAkrNKANLEKAKQ 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9010 QFESVSRQGQALIKTAVAGSNTTglETDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETE-ELVA 9088
Cdd:pfam01576 381 ALESENAELQAELRTLQQAKQDS--EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgKNIK 458
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9089 MQKAPSPeqrvVRAQLQE-QKLVQKMVTDR---TPSMKAVQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVV 9162
Cdd:pfam01576 459 LSKDVSS----LESQLQDtQELLQEETRQKlnlSTRLRQLEDERNSLQEQLEEEEeaKRNVERQLSTLQAQLSDMKKKLE 534
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9163 DRTAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTALEphspdaEGIEHLIQELKKLQKEVNEHepamKQLATAGKKLQd 9242
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE------KTKNRLQQELDDLLVDLDHQ----RQLVSNLEKKQ- 603
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9243 ycKGEDVIMIQLKidGVQKQNGELRSHIE-DCLEQMEEALPLAKHFQEA--HAEFLSWASK-VEPELRALELGVPDEETN 9318
Cdd:pfam01576 604 --KKFDQMLAEEK--AISARYAEERDRAEaEAREKETRALSLARALEEAleAKEELERTNKqLRAEMEDLVSSKDDVGKN 679
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9319 IEEL------ANQLTEEMQPLLDIINSE--GAElaevapgDAGLRVEdiinrdnkrfdnlrdqIEKRAQKVQLARQRSSE 9390
Cdd:pfam01576 680 VHELerskraLEQQVEEMKTQLEELEDElqATE-------DAKLRLE----------------VNMQALKAQFERDLQAR 736
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9391 vvNELGDlvdwfvdaDSRLQnqqpiasdldlLQQQLAEQKVMNEEINNQKVKArdtLSASKKL---LSDSAMEDNSAIRN 9467
Cdd:pfam01576 737 --DEQGE--------EKRRQ-----------LVKQVRELEAELEDERKQRAQA---VAAKKKLeldLKELEAQIDAANKG 792
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9468 KMDELKQwVDTVSGSANERQSLLEQAvpfarhfHEAHTELVVWLDDVEPVLSELDvlsvdADQVKKQQEKA---KVLKQE 9544
Cdd:pfam01576 793 REEAVKQ-LKKLQAQMKDLQRELEEA-------RASRDEILAQSKESEKKLKNLE-----AELLQLQEDLAaseRARRQA 859
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9545 VADRKPIVDRLNKtgtalvamcGSKGaeqvQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTA 9624
Cdd:pfam01576 860 QQERDELADEIAS---------GASG----KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTEL 926
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9625 EQVRSAepiSAQPDKLREQIE-ENK-------AMEEDLEMRHN----ALESVKNAAEELLRQAGDEQDEAVKDVRQKLEE 9692
Cdd:pfam01576 927 AAERST---SQKSESARQQLErQNKelkaklqEMEGTVKSKFKssiaALEAKIAQLEEQLEQESRERQAANKLVRRTEKK 1003
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 9693 LTKLYKDIQERGRgrqraleetlaVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQ-QEELEALKEDIEA 9768
Cdd:pfam01576 1004 LKEVLLQVEDERR-----------HADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKlQRELDDATESNES 1069
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
10596-10651 |
6.44e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.87 E-value: 6.44e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 10596 LEDLLAWLNNAEMTLADVDrqtIPQDMAIIQQLIKEHQDFQNEMSSRQPDVDRLTK 10651
Cdd:smart00150 7 ADELEAWLEEKEQLLASED---LGKDLESVEALLKKHEAFEAELEAHEERVEALNE 59
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7455-7606 |
7.92e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 51.29 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7455 LGDLEQILKHDsQMGDEASKVKLQLEAHKSTHEKIQSQQQPILSLVYKAEQLTENYQEEltpeqVTQLTTQASLLKATLE 7534
Cdd:cd00176 16 LSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-----AEEIQERLEELNQRWE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 7535 KVSKTSERRLSHLTKAADeLAKFEEESKKFRTWMGAAFSELtNQEDYLKRFEDLKVLGEKHRELASDISSHQ 7606
Cdd:cd00176 90 ELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAAL-ASEDLGKDLESVEELLKKHKELEEELEAHE 159
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8702-9181 |
9.80e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8702 DSGKEAIKQQVAVINERWDAVNKALSER----------ASHLEDLGQRLGEVQDSLAEATSALNKWENKLavhNSLGLSA 8771
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAglddadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEA---ESLREDA 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8772 KDpkHINRIKDLLEDTGWLASQLNNTETML----------------NSIEVDGGETS--NLRDELNKLRGQHQTLQGELS 8833
Cdd:PRK02224 352 DD--LEERAEELREEAAELESELEEAREAVedrreeieeleeeieeLRERFGDAPVDlgNAEDFLEELREERDELREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8834 ELVAEMETGAQIVEQFQGLLKiVG-----GQFLElESELGSKTPVSRDD-AELGSQLADMKDFLTRLGEKVETLKDLEQQ 8907
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLE-AGkcpecGQPVE-GSPHVETIEEDRERvEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8908 ASslcnagyvsdpellksQVEALSNQHASLTERATQRQSDVVANQHSIQHL-TQALNLVWGDIDKASSTLDAMGPAGGNV 8986
Cdd:PRK02224 508 ED----------------RIERLEERREDLEELIAERRETIEEKRERAEELrERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8987 TTVKALQEELkGFVKSTMEPLQKQFESVSRqgqaliktavagsnTTGLETDLESLAERWAGLVEKVAEHEKNLDSalLRT 9066
Cdd:PRK02224 572 EEVAELNSKL-AELKERIESLERIRTLLAA--------------IADAEDEIERLREKREALAELNDERRERLAE--KRE 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9067 GKFQdamaslldwLAETEELVAMQKAPSPEQRVVRAQLQeqklvqkmVTDRTPSMKAVQDSGNQLITGldpaerkhIESE 9146
Cdd:PRK02224 635 RKRE---------LEAEFDEARIEEAREDKERAEEYLEQ--------VEEKLDELREERDDLQAEIGA--------VENE 689
|
490 500 510
....*....|....*....|....*....|....*...
gi 1397727989 9147 LQQLNS---RWEALTKRVVDRTAILEEVQGLAGEFQDV 9181
Cdd:PRK02224 690 LEELEElreRREALENRVEALEALYDEAEELESMYGDL 727
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
8266-8694 |
1.06e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8266 EEML---QQQLQELDDKWHGLRALSEQQRKGLEDMvSDLRDMREHE-QQLTLWLAQKDRMLDvlgpvamepnmlasQMEQ 8341
Cdd:pfam05483 362 EELLrteQQRLEKNEDQLKIITMELQKKSSELEEM-TKFKNNKEVElEELKKILAEDEKLLD--------------EKKQ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8342 VKVLREELSAQEPTYDHFLNCAHgilERCGDKSQDGIAVSRRLDTVSKAWNKLQSRL-NERSKNL---SSVEGISVEFAS 8417
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQARE---KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELeKEKLKNIeltAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8418 LTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQELK----QLESELIVQQPRLARARDLCRQLCDKAKDasTKTDLRSK 8493
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEekemNLRDELESVREEFIQKGDEVKCKLDKSEE--NARSIEYE 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8494 LTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLK 8573
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8574 EPEIRQLLEkgDKLVKEsspTTEVRAIADKVGELQGEW-TRLQQEVTvqdSRLTMAGSHAQQFTERLDKMAMWLQMTEEK 8652
Cdd:pfam05483 662 EIEDKKISE--EKLLEE---VEKAKAIADEAVKLQKEIdKRCQHKIA---EMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1397727989 8653 LEKMKPEDVDQNTVVHKLK-ELQGVQNEMMKKSHDRERLNSEG 8694
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKaELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
29-134 |
1.16e-05 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 48.60 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 29 DTDERdavqkKTFTKWVNKHLM---KAGLRI------IDLFDDLRDGHNLISLLEVLAHDILPRERGHMR---------F 90
Cdd:cd21294 4 NEDER-----REFTKHINAVLAgdpDVGSRLpfptdtFQLFDECKDGLVLSKLINDSVPDTIDERVLNKPprknkplnnF 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1397727989 91 HKIQNVQIALDYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21294 79 QMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
10804-10852 |
1.22e-05 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 46.77 E-value: 1.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727989 10804 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 10852
Cdd:cd00051 15 GTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
9620-9892 |
1.25e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9620 LTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESV---KNAAEELLRQAGDEQDEAvkdvRQKLEELTKL 9696
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAreeLEQLEEELEQARSELEQL----EEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9697 YKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEA-IREQQEELEALKEDIEASQadfEE 9775
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSeIAEREEELKELEEQLESLQ---EE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9776 VQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLvwLQEAEDEFSEFEPVA 9855
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE--AKLGLALSALLDALE 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1397727989 9856 SEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTEL 9892
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8514-9187 |
1.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8514 AVEEASQQAEkfeadckeLLTWISEAANNLQEsepLSSDLDILREQMRQNR--TLQQELSLKEPEIRQLLEKGDKLvkes 8591
Cdd:COG4913 243 ALEDAREQIE--------LLEPIRELAERYAA---ARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARL---- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8592 spTTEVRAIADKVGELQGEWTRLQQEvtvqdsrltmagsHAQQFTERLdkmamwlqmteEKLEKmkpedvdqntvvhklk 8671
Cdd:COG4913 308 --EAELERLEARLDALREELDELEAQ-------------IRGNGGDRL-----------EQLER---------------- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8672 ELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERwdavnkaLSERASHLEDLGQRLGEVQDSLAEAT 8751
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL-------LEALEEELEALEEALAEAEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8752 SALNKWENKLAvhnSLGLSAKD-PKHINRIKDLLedtgwlASQLNNTETML----NSIEVDGGEtSNLRDELNK-LRGQH 8825
Cdd:COG4913 419 RELRELEAEIA---SLERRKSNiPARLLALRDAL------AEALGLDEAELpfvgELIEVRPEE-ERWRGAIERvLGGFA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8826 QTLqgelseLVAEmetgaqivEQFQGLLKIV-----GG--QFLELESELGSKTPVSRDDAELGSQLA----DMKDFL-TR 8893
Cdd:COG4913 489 LTL------LVPP--------EHYAAALRWVnrlhlRGrlVYERVRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLeAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8894 LGE-----KVETLKDLEQQASSLCNAGYVSDP--------------------------ELLKSQVEALSNQHASLTERAT 8942
Cdd:COG4913 555 LGRrfdyvCVDSPEELRRHPRAITRAGQVKGNgtrhekddrrrirsryvlgfdnraklAALEAELAELEEELAEAEERLE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8943 QRQSDVVANQHSIQHLTQALNLVWGDIDkasstldamgpaggnvttVKALQEELkgfvkstmeplqkqfesvsRQGQALI 9022
Cdd:COG4913 635 ALEAELDALQERREALQRLAEYSWDEID------------------VASAEREI-------------------AELEAEL 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9023 KTAVAGSNttgletDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVamQKAPSPEQRVVRA 9102
Cdd:COG4913 678 ERLDASSD------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRA 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9103 QLqEQKLVQKMVTDRTPSM-KAVQDSGNQLITGLDPAERKhIESELQQLNSRWEALTkrvVDRTAILEEvqglAGEFQDV 9181
Cdd:COG4913 750 LL-EERFAAALGDAVERELrENLEERIDALRARLNRAEEE-LERAMRAFNREWPAET---ADLDADLES----LPEYLAL 820
|
....*.
gi 1397727989 9182 LDPLTT 9187
Cdd:COG4913 821 LDRLEE 826
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9644-10528 |
1.27e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9644 IEENKAMEEDLEMRHNALESVKnaAEELLRQAGDEQDEAVKDVR---QKLEELTKLYKDIQERGRGRQRALEETLAVAEK 9720
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIK--ALETLRQVRQTQGQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9721 FWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQadfEEVQQTGDTLLGMVGTTEQPEVQknvd 9800
Cdd:TIGR00606 243 YENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKM---EKVFQGTDEQLNDLYHNHQRTVR---- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9801 DAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQE------AEDEFSEFEPVASEFETIKKQWD---ELKNF 9871
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirARDSLIQSLATRLELDGFERGPFserQIKNF 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9872 KTRV-EPKNVEIESLNQHVTELTKSST--PEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHKELKN 9948
Cdd:TIGR00606 396 HTLViERQEDEAKTAAQLCADLQSKERlkQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9949 WMDLVDVTLDEItPVYGDPKLVEIELAKLRIVQNDitaHQESVESISKEAQRLmtsegiAQAQGLKTKMEDMEKTwenIQ 10028
Cdd:TIGR00606 476 LDQELRKAEREL-SKAEKNSLTETLKKEVKSLQNE---KADLDRKLRKLDQEM------EQLNHHTTTRTQMEML---TK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10029 AKSRAKQDMLEDGLREAQGFTGELQDILAKindiegqLIISKPVGGLPETAKEQLEKFMDVYAELEKLEpqvQSLNVMGE 10108
Cdd:TIGR00606 543 DKMDKDEQIRKIKSRHSDELTSLLGYFPNK-------KQLEDWLHSKSKEINQTRDRLAKLNKELASLE---QNKNHINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10109 KLggKSKGPALANLRQNLQHLNQrCDYIRSRACDRKKKLEDAEGMATNFHGELNKFISWLTDTEKTLNNLQPVSRLVERV 10188
Cdd:TIGR00606 613 EL--ESKEEQLSSYEDKLFDVCG-SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10189 TSQIED-HRDLQkdiSKHREAMVALEKMGTHLKYFSQKQDVVLIK-NLLSSIQHRWEKIVSRSAERTRHLERGYKEAK-- 10264
Cdd:TIGR00606 690 EAELQEfISDLQ---SKLRLAPDKLKSTESELKKKEKRRDEMLGLaPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKnd 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10265 -QFNDTWKDLITWLIEAEKTLETETSVANE--------PDKIKAQISK---------HKEFQRRLGAKQPVYDGVNKAGR 10326
Cdd:TIGR00606 767 iEEQETLLGTIMPEEESAKVCLTDVTIMERfqmelkdvERKIAQQAAKlqgsdldrtVQQVNQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10327 LLKeRCPSD---DVPTIQAMLTELKSHWNNVCSKSVDRQRKLEEGLLLSGQFTEALDALLDWLAKVEP---ALADDAPVH 10400
Cdd:TIGR00606 847 LNR-KLIQDqqeQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPletFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10401 GDI------------DTVNgflDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLIELNaawdrvcklsvS 10468
Cdd:TIGR00606 926 EELissketsnkkaqDKVN---DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECE-----------K 991
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 10469 KQDRLEHAQRLAEEFHKKAQQLLSWLADAERQLHYRGPIPD--EEPL----------ILQQMEEHKKFEESL 10528
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEveEELKqhlkemgqmqVLQMKQEHQKLEENI 1063
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
7913-8094 |
1.30e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.52 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7913 LREFQEKLEQTNLWVHDGILQLDSKELSKLSSD--DMKQQLEKLAREKHNRLRTIQEIQVAAEQLLQDpRTGEGEAVKNL 7990
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESveALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7991 VSDLKKNLEAFDSLLAAKEN---EASDKEQQGADFENaktiALLWLSQMEARLDEFQPVAiDVGIVEQQKMELQPMLQEY 8067
Cdd:cd00176 81 LEELNQRWEELRELAEERRQrleEALDLQQFFRDADD----LEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEEL 155
|
170 180
....*....|....*....|....*..
gi 1397727989 8068 EDYAPKIDEVNDLGNAYEAMINPGDRP 8094
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADE 182
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
8242-8931 |
1.44e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8242 KEGLVEDIR-----KKAQDLLKTRHGvpgeemLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMREHEQQLTLWLA 8316
Cdd:PRK02224 185 QRGSLDQLKaqieeKEEKDLHERLNG------LESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8317 QKDRMLDVLGPVAMEPNMLAsqmEQVKVLREELSAQEPTYDHflncahgILERCGDKSQDGIAVSRRLDTVSKAWNKLQS 8396
Cdd:PRK02224 259 EIEDLRETIAETEREREELA---EEVRDLRERLEELEEERDD-------LLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8397 RLNERSKNlssvegisvefASLTRGLADWLSDFSDKLDGQGKvssqpDKQhkqlQELKQLESELivqqprlarardlcrq 8476
Cdd:PRK02224 329 RLEECRVA-----------AQAHNEEAESLREDADDLEERAE-----ELR----EEAAELESEL---------------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8477 lcdkAKDASTKTDLRSKLTALEKDMNDTtrkleicKAAVEEASQQAEKFEADCKELLTWISEAANNLQEsepLSSDLDIL 8556
Cdd:PRK02224 373 ----EEAREAVEDRREEIEELEEEIEEL-------RERFGDAPVDLGNAEDFLEELREERDELREREAE---LEATLRTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8557 REQMRQNRTLQQElsLKEPEIRQllekgdkLVKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGShAQQFT 8636
Cdd:PRK02224 439 RERVEEAEALLEA--GKCPECGQ-------PVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8637 ERLDKMAMWLQMTEEKLEKMKPE-DVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDsgkeAIKQQVAVI 8715
Cdd:PRK02224 509 DRIERLEERREDLEELIAERRETiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA----ELNSKLAEL 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8716 NERWDAVNKaLSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNslglsakdpkhiNRIKDLLEdtgwlasqln 8795
Cdd:PRK02224 585 KERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR------------ERKRELEA---------- 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8796 ntetmlnsiEVDGgetsnlrDELNKLRGQHQTLQGELSELVAEMEtgaQIVEQFQGLLKIVGGqfleLESELgsktpvsr 8875
Cdd:PRK02224 642 ---------EFDE-------ARIEEAREDKERAEEYLEQVEEKLD---ELREERDDLQAEIGA----VENEL-------- 690
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 8876 ddaelgSQLADMKDFLTRLGEKVETLKDLEQQASSLCNAGYVSDPELLKSQVEALS 8931
Cdd:PRK02224 691 ------EELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8176-8755 |
1.53e-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: 52.87 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8176 RLADRQQELQLMLTSI------------------RTFMQDMQDILQWLdlkDHETDSAQPLPTNEKDAKKRLKEHEvfhR 8237
Cdd:pfam01576 65 RLAARKQELEEILHELesrleeeeersqqlqnekKKMQQHIQDLEEQL---DEEEAARQKLQLEKVTTEAKIKKLE---E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8238 EILskegLVEDIRKKaqdLLKTRHGVpgEEMLQQ---QLQELDDKWHGLRALSEQQrkglEDMVSDLRDMREHEQQLTLW 8314
Cdd:pfam01576 139 DIL----LLEDQNSK---LSKERKLL--EERISEftsNLAEEEEKAKSLSKLKNKH----EAMISDLEERLKKEEKGRQE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8315 LAQKDRMLDVlgpvamEPNMLASQMEQVKVLREELSAQeptydhflncahgiLERCGDKSQDGIAvsrRLDTVSKAWNKL 8394
Cdd:pfam01576 206 LEKAKRKLEG------ESTDLQEQIAELQAQIAELRAQ--------------LAKKEEELQAALA---RLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8395 QSRLNErsknlssvegisvefasltrgLADWLSDFSDKLDGQGKVSSQPDKQHKQL-QELKQLESEL--------IVQQP 8465
Cdd:pfam01576 263 LKKIRE---------------------LEAQISELQEDLESERAARNKAEKQRRDLgEELEALKTELedtldttaAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8466 RLARARDLcrQLCDKAKDASTKT------DLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEA 8539
Cdd:pfam01576 322 RSKREQEV--TELKKALEEETRSheaqlqEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8540 AnnlQESeplssdldilrEQMRQNRTLQ-QELSLKEPEI-RQLLEKGDKLVKessPTTEVRAIADKVGELQGEWTRLQQE 8617
Cdd:pfam01576 400 K---QDS-----------EHKRKKLEGQlQELQARLSESeRQRAELAEKLSK---LQSELESVSSLLNEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8618 VTVQDSRLTMAGSHAQQFTERLDKMAMWL-QMTEEK---LEKMKPEDVDQNTVVHKLKELQGVQNEMMKKShdrerlnSE 8693
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLSTRLrQLEDERnslQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-------EE 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 8694 GTSLVECVDSGKEAIKQQVavinerwDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALN 8755
Cdd:pfam01576 536 DAGTLEALEEGKKRLQREL-------EALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLD 590
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
9189-9778 |
1.56e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9189 LDAANKRftaLEPH---SPDAEGIEHLIQELKK-----------LQKEVNEHEPAMKQLATAGKKLQDYCKG-EDVIMIQ 9253
Cdd:pfam05483 204 VQAENAR---LEMHfklKEDHEKIQHLEEEYKKeindkekqvslLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9254 lkiDGVQKQNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKV------EPELRALELG---------VPDEETN 9318
Cdd:pfam05483 281 ---DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTicqlteEKEAQMEELNkakaahsfvVTEFEAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9319 IEELANQLTEEMQPL------LDIINSE----GAELAEVAPGDAGLRVE-----DIINRDNKRFDNlRDQIEKRAQKVQL 9383
Cdd:pfam05483 358 TCSLEELLRTEQQRLeknedqLKIITMElqkkSSELEEMTKFKNNKEVEleelkKILAEDEKLLDE-KKQFEKIAEELKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9384 ARQrssevvnELGDLvdwfvdadsrLQNQQPIASDLDLL--------QQQLAEQKVMNEEINNQKVKARDTLSASKKLLs 9455
Cdd:pfam05483 437 KEQ-------ELIFL----------LQAREKEIHDLEIQltaiktseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9456 dsaMEDNSAIRNKMD---ELKQWVDTVSGSANERQSLLEQavpfARHFHEAHTELvvwLDDVEPVLSELdvlsvdadQVK 9532
Cdd:pfam05483 499 ---LENKELTQEASDmtlELKKHQEDIINCKKQEERMLKQ----IENLEEKEMNL---RDELESVREEF--------IQK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9533 KQQEKAKVLKQEVADRKPIVDRLNKtgtalvamcgskgaeqvQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDK 9612
Cdd:pfam05483 561 GDEVKCKLDKSEENARSIEYEVLKK-----------------EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9613 lenmldtLTVTAEQVRSAEpisAQPDKLREQIEENK-AMEEDLEMRHNALESVKNAAEELLrqagdeqdEAVKDVRQKLE 9691
Cdd:pfam05483 624 -------GSAENKQLNAYE---IKVNKLELELASAKqKFEEIIDNYQKEIEDKKISEEKLL--------EEVEKAKAIAD 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9692 ELTKLYKDIQERGrgrQRALEETLAVAEKF---WDELHALNSS---LKDLQEALSSVDQPALEPEaIREQQEELEALKED 9765
Cdd:pfam05483 686 EAVKLQKEIDKRC---QHKIAEMVALMEKHkhqYDKIIEERDSelgLYKNKEQEQSSAKAALEIE-LSNIKAELLSLKKQ 761
|
650
....*....|...
gi 1397727989 9766 IEASQADFEEVQQ 9778
Cdd:pfam05483 762 LEIEKEEKEKLKM 774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9356-9961 |
1.66e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.72 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9356 VEDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQN--QQPIASDLDL--LQQQLAEQKV 9431
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKikNKLLKLELLLsnLKKKIQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9432 MNEEINNQKvKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDT---VSGSANERQSLLEQAvpfarhfHEAHTELV 9508
Cdd:TIGR04523 216 LESQISELK-KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQN-------NKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9509 VWLDDVEPVLSEL------DVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLN-------KTGTALVAMCGSKGAE--- 9572
Cdd:TIGR04523 288 KQLNQLKSEISDLnnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNeqisqlkKELTNSESENSEKQRElee 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9573 ---QVQSMLDDDNRRMDNVrTKVRDRSNSIDQAMQQSaeftDKLENMLDTLTVTAEQvrSAEPISAQPDKLREQIEENKA 9649
Cdd:TIGR04523 368 kqnEIEKLKKENQSYKQEI-KNLESQINDLESKIQNQ----EKLNQQKDEQIKKLQQ--EKELLEKEIERLKETIIKNNS 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9650 MEEDLEMRHNALE----SVKNAAEEL-------------LRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALE 9712
Cdd:TIGR04523 441 EIKDLTNQDSVKEliikNLDNTRESLetqlkvlsrsinkIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9713 ETLAVAEKFWDELHALNSSLKDLQEALSSVDQ----PALEPEaIREQQEELEALKEDIEASQADFEEVQQTGDtllgmvg 9788
Cdd:TIGR04523 521 SLKEKIEKLESEKKEKESKISDLEDELNKDDFelkkENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELID------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9789 tteqpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLvwlqeaedefSEFEPVASEFETIKKQWDEL 9868
Cdd:TIGR04523 593 -----QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK----------SKKNKLKQEVKQIKETIKEI 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9869 KNFKTRVEPKNVEIESLNQHVTELTKSSTPEqASVLREPMTQLNIRwNNLLTNIGDRQRELQMALLTAGQFDhahKELKN 9948
Cdd:TIGR04523 658 RNKWPEIIKKIKESKTKIDDIIELMKDWLKE-LSLHYKKYITRMIR-IKDLPKLEEKYKEIEKELKKLDEFS---KELEN 732
|
650
....*....|...
gi 1397727989 9949 WMDLVDVTLDEIT 9961
Cdd:TIGR04523 733 IIKNFNKKFDDAF 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9647-9838 |
1.77e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9647 NKAMEEDLEMRHNALESVKNAAEELLRQAGDEQD--EAVKDVRQKLEELTKLYKDIQERGRgRQRALEETLAVAEKFWDE 9724
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9725 LHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAG- 9803
Cdd:COG4913 687 LAALEEQLEELEAELEELE------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALg 760
|
170 180 190
....*....|....*....|....*....|....*.
gi 1397727989 9804 -ASLAAISDQYSKRSQELESALAQAvhfQDQLMKLL 9838
Cdd:COG4913 761 dAVERELRENLEERIDALRARLNRA---EEELERAM 793
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
619-712 |
2.05e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 47.31 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 619 LSEFLQGATAELTWLAEREEvEVTRDWVSKDL-NLADLDDHHKNLIRQVEARERHFNAVQEKGGAMILDRHPAASMVEVL 697
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEA-LLSSEDYGKDLeSVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQER 81
|
90
....*....|....*
gi 1397727989 698 MASLQARWSWLLQLV 712
Cdd:pfam00435 82 LEELNERWEQLLELA 96
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8444-8841 |
2.08e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8444 DKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDTTRKLEICKAAVEE------ 8517
Cdd:COG4717 84 EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelee 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8518 ----ASQQAEKFEADCKELLTWISEAAnnLQESEPLSSDLDILREQMRQnrtLQQELSLKEPEIRQLLEKGDKLVKESSP 8593
Cdd:COG4717 164 eleeLEAELAELQEELEELLEQLSLAT--EEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8594 TTEVRAIADKVGELQGEWTRL---QQEVTVQDSRLTMAGshAQQFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKL 8670
Cdd:COG4717 239 AALEERLKEARLLLLIAAALLallGLGGSLLSLILTIAG--VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8671 KElQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERwdAVNKALSERASHLEDLGQRLGEVQDSLAEA 8750
Cdd:COG4717 317 EE-EELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8751 TSALNKWENKLAVHNSLgLSAKDPKHINRIKDLLEDTgwLASQLNNTETMLNSIEvdgGETSNLRDELNKLRGQHQTL-- 8828
Cdd:COG4717 394 AEEYQELKEELEELEEQ-LEELLGELEELLEALDEEE--LEEELEELEEELEELE---EELEELREELAELEAELEQLee 467
|
410
....*....|...
gi 1397727989 8829 QGELSELVAEMET 8841
Cdd:COG4717 468 DGELAELLQELEE 480
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
9629-9834 |
2.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9629 SAEPISAQPD--KLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrg 9706
Cdd:COG3883 8 APTPAFADPQiqAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9707 RQRALEETLAVAEK------FWDELhaLNSslKDLQEALSSVDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTG 9780
Cdd:COG3883 84 RREELGERARALYRsggsvsYLDVL--LGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9781 DTLLGMVGTTEQpEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQL 9834
Cdd:COG3883 160 EALKAELEAAKA-ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7494-7978 |
2.24e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7494 QPILSLVYKAEQLTE--NYQEELTPEQ--VTQ----LTTQASLLKATLEKVSKTSERR--LSHLTKAADELAKFEEESKK 7563
Cdd:TIGR02168 619 SYLLGGVLVVDDLDNalELAKKLRPGYriVTLdgdlVRPGGVITGGSAKTNSSILERRreIEELEEKIEELEEKIAELEK 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7564 FRTWMGAAFSELTNQEDYLKRFEDlkvlgekhrELASDISSHQADHRFMSMAVQKYMEEAKLYKLEMDSFRADRArpARH 7643
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELE---------ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE--ELE 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7644 SLISMECVAADNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDVAFKLLTWLTDMEGQLSSVKQDAGLSEpQQ 7723
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE-EQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7724 LQVHLDRLKSLSMDALSQKLLLDEMQKRGQDLTNslsgqaaeqqQVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAAvth 7803
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLN----------ERASLEEALALLRSELEELSEELRELESKRSEL--- 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7804 sqdiTQAMNELvswMDSAEQVVTTQLPISLRRPELNAQLQSfsavdadvtNHQSALDAVKALANELvktcELDIARAvEQ 7883
Cdd:TIGR02168 914 ----RRELEEL---REKLAQLELRLEGLEVRIDNLQERLSE---------EYSLTLEEAEALENKI----EDDEEEA-RR 972
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7884 RLTSLDEKFSSLQakcrqrdrdleEVD-SSLREFQEKLEQTnlwvhdgilqldskelsklssDDMKQQLEKLAREKHNRL 7962
Cdd:TIGR02168 973 RLKRLENKIKELG-----------PVNlAAIEEYEELKERY---------------------DFLTAQKEDLTEAKETLE 1020
|
490
....*....|....*.
gi 1397727989 7963 RTIQEIQVAAEQLLQD 7978
Cdd:TIGR02168 1021 EAIEEIDREARERFKD 1036
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
155-250 |
2.57e-05 |
|
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: 46.91 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 155 ALLLWSRRTTegyPGVKIKDFSSSWRDGKAFLSIIHRNRPDLIDFRQARSNSNKQNLELAFTvAEKEFGVTRLLDPEDVD 234
Cdd:cd21185 5 ATLRWVRQLL---PDVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMA 80
|
90
....*....|....*.
gi 1397727989 235 VPNPDEKSILTYVSSL 250
Cdd:cd21185 81 DPEVEHLGIMAYAAQL 96
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
523-617 |
3.15e-05 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 46.93 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 523 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 599
Cdd:pfam00435 7 FRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEghyASEEIQERLEELN 86
|
90
....*....|....*...
gi 1397727989 600 VAYSLLLNTSSRRLKFLE 617
Cdd:pfam00435 87 ERWEQLLELAAERKQKLE 104
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
34-136 |
3.19e-05 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, 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. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 47.11 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 34 DAVQKKTFTKWVNKhlMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGH-----MRFHKIQNVQIALDYLRLKGI 108
Cdd:cd21299 2 TSREERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHANkppikMPFKKVENCNQVVKIGKQLKF 79
|
90 100
....*....|....*....|....*...
gi 1397727989 109 RLVNIRSDEIVDGNPKLTLGLIWTIILH 136
Cdd:cd21299 80 SLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9719-9821 |
4.18e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9719 EKFWDELHALNSSLKDLQEALSSvDQPALEPEAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMvGTTEQPEVQKN 9798
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEE-GHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1397727989 9799 VDDAGASLAAISDQYSKRSQELE 9821
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
9356-9780 |
4.33e-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: 51.49 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9356 VEDIINRDNKRFDNLRDQIEKRAQKVQLARQ------RSSEVVNELGDLVDWFVDADSRLQNQQPIA---SDLDLLQQQL 9426
Cdd:COG3096 284 SERALELRRELFGARRQLAEEQYRLVEMAREleelsaRESDLEQDYQAASDHLNLVQTALRQQEKIEryqEDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9427 AEQKVMNEEINNQKVKARDTLSASkkllsdsamednsaiRNKMDELKqwvdtvSGSANERQSLLEQAVPfARHFHEAhte 9506
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAA---------------EEEVDSLK------SQLADYQQALDVQQTR-AIQYQQA--- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9507 lVVWLDDVEpVLSELDVLSvdADQVKKQQEKAKVLKQEVADRkpivdRLnktgtalvamcgskGAEQVQSMLDDDNRRMD 9586
Cdd:COG3096 419 -VQALEKAR-ALCGLPDLT--PENAEDYLAAFRAKEQQATEE-----VL--------------ELEQKLSVADAARRQFE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9587 NVRTKVR------DRSNSIDQAMQQSAEFTDkLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEE-NKAMEEDLEMRHN 9659
Cdd:COG3096 476 KAYELVCkiagevERSQAWQTARELLRRYRS-QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9660 aLESVKNAAEELLRQAGDEQDEAVKD---VRQKLEELTKLYKDIqergrgRQRALE--ETLAVAEKFWDELHAlnsSLKD 9734
Cdd:COG3096 555 -LEELLAELEAQLEELEEQAAEAVEQrseLRQQLEQLRARIKEL------AARAPAwlAAQDALERLREQSGE---ALAD 624
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1397727989 9735 LQEaLSSVDQPALEPEAIREQQE-ELEALKEDIEaSQAdfEEVQQTG 9780
Cdd:COG3096 625 SQE-VTAAMQQLLEREREATVERdELAARKQALE-SQI--ERLSQPG 667
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
43-133 |
4.55e-05 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 46.91 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 43 KWVNKHLMKAGL---RIIDLFDDLRDGHNLISLLEVLA-HDILPRERGHM--RFHKIQNVQIALDYLRLKGIRLVnIRSD 116
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLApELCDKELVLEVlsEEDLEKRAEKVLQAAEKLGCKYF-LTPE 95
|
90
....*....|....*..
gi 1397727989 117 EIVDGNPKLTLGLIWTI 133
Cdd:cd21218 96 DIVSGNPRLNLAFVATL 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9206-9899 |
4.68e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9206 AEGIEHLIQELKKLQKEVNEHEPAMKQLA--------TAGKKLQDYCKGEDVIMIQLKIDGVQKQNGELRSHIEDCLEQM 9277
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfarrQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9278 EE---ALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEETNIEELanQLTEEMQPLLDIINSEGAELAEVAPGDAgl 9354
Cdd:PTZ00121 1312 EEakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA--EAAEEKAEAAEKKKEEAKKKADAAKKKA-- 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9355 rvediinRDNKRFDNLRDQIEKRAQKVQLARQRSSEV--VNELGDLVDWFVDADsRLQNQQPIASDLDLLQQQlAEQKVM 9432
Cdd:PTZ00121 1388 -------EEKKKADEAKKKAEEDKKKADELKKAAAAKkkADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKK-AEEAKK 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9433 NEEINNQKVKARDTLSASKKL----LSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHTelV 9508
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK--A 1536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9509 VWLDDVEPVLSELDVLSvdADQVKKQQEKAKVLKQEVADRkpivDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNV 9588
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKK--AEELKKAEEKKKAEEAKKAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9589 RTKVRDRSNSIDQAMQQSAEFTDKLENMLDTltvTAEQVRSAEPI--SAQPDKLREQIEENKAMEE--DLEMRHNALESV 9664
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK---EAEEKKKAEELkkAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDE 1687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9665 KNAAEELLRQAgdEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAE---KFWDELHALNSSLKDLQEALSS 9741
Cdd:PTZ00121 1688 KKAAEALKKEA--EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEKKKIAHLKKE 1765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9742 VDQPALEPEAIREQQEELEALKED----------IEASQADFEEVQQTGDTLLGMVGTTEQPEVQ--KNVDDAGASLAAI 9809
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDekrrmevdkkIKDIFDNFANIIEGGKEGNLVINDSKEMEDSaiKEVADSKNMQLEE 1845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9810 SDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEfepvASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHV 9889
Cdd:PTZ00121 1846 ADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE----ADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDK 1921
|
730
....*....|
gi 1397727989 9890 TELTKSSTPE 9899
Cdd:PTZ00121 1922 DEYIKRDAEE 1931
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
9569-9850 |
4.93e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9569 KGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMldtltvTAEQVRSAEPISAQPDKLREQIEENK 9648
Cdd:pfam07888 55 RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEK------YKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9649 A----MEEDLEM-------RHNALESVKNAAEELLRQAGDEQDEAvKDVRQKLE----ELTKLYKDIQE-RGRGRQRAle 9712
Cdd:pfam07888 129 ArireLEEDIKTltqrvleRETELERMKERAKKAGAQRKEEEAER-KQLQAKLQqteeELRSLSKEFQElRNSLAQRD-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9713 etlavaekfwDELHALNSSLKDLQEALSSVDQPALEPEAIREQ----QEELEALKEDIEASQADFEEVQQTGDTLLGMVG 9788
Cdd:pfam07888 206 ----------TQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslQERLNASERKVEGLGEELSSMAAQRDRTQAELH 275
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 9789 TTEQPEVQKNVDDAGASLAAISDQySKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSE 9850
Cdd:pfam07888 276 QARLQAAQLTLQLADASLALREGR-ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8516-9157 |
4.96e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8516 EEASQQAEKF-----EADCKELLTWISEAANNLQESEPLSSDLDILREQMRQnrtLQQELSLKEPEIRQLLEKGDKLvke 8590
Cdd:COG1196 206 ERQAEKAERYrelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEEL--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8591 sspTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKL 8670
Cdd:COG1196 280 ---ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8671 KELQGVQNEmmkkshdrERLNSEgtslvecvdsgkEAIKQQVAVINERWDAVNKALSERASHLEDLGQRLGEVQDSLAEA 8750
Cdd:COG1196 357 EAELAEAEE--------ALLEAE------------AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8751 TSALNKWENKLAvhnslGLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEvdggetsNLRDELNKLRGQHQTLQG 8830
Cdd:COG1196 417 ERLEEELEELEE-----ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA-------ELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8831 ELSELVAEMETGAQIVEQFQGLLKIVGGQFLEleselgsktPVSRDDAELGSQLADmkdfltrLGEKVETlkDLEQQASS 8910
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLL---------AGLRGLAGAVAVLIG-------VEAAYEA--ALEAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8911 LCNAGYVSDPELLKSQVEALSNQHASlteRATQRQSDVVANQHSIQHLTQALNLVWGDIDKASS--TLDAMGPAGGNVTT 8988
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAG---RATFLPLDKIRARAALAAALARGAIGAAVDLVASDlrEADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8989 VKALQEELKGFVKSTMEPLQKQFESVSRQGQALI-KTAVAGSNTTGLETDLESLAERWAGLVEKVAEHEKNLDSALLRtg 9067
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSaGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA-- 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9068 kfqdamaslldwLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRTPSMKAVQDSGNQLITGLDPAERKHIESEL 9147
Cdd:COG1196 702 ------------EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
650
....*....|
gi 1397727989 9148 QQLNSRWEAL 9157
Cdd:COG1196 770 ERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8223-8756 |
5.04e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8223 KDAKKRLKEHEVFHREILSKEGLVEDIRKKAQDLLKTRhgvpgeEMLQQQLQELDDKWHGLRALsEQQRKGLEDMVSDLR 8302
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8303 DMREHEQQLTLWLAQKDRMLDVLGPVAMEPNMLASQMEQVKVLREELSAQEPtydhflncaHGILERCGDKSQDGIAVSR 8382
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP---------EKLEKELEELEKAKEEIEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8383 RLDTVSKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGL-----ADWLSDFSDKLDGQGKVSSQPDKQHKQLQ-ELKQL 8456
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrKELLEEYTAELKRIEKELKEIEEKERKLRkELREL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8457 ESELiVQQPRLARARDLCRQLcdkakdastkTDLRSKLTALEkdmndttrkleickaaVEEASQQAEKFEADCKELLTWI 8536
Cdd:PRK03918 486 EKVL-KKESELIKLKELAEQL----------KELEEKLKKYN----------------LEELEKKAEEYEKLKEKLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8537 SEAANnlqesepLSSDLDILREQMRQNRTLQQELSLKEPE----IRQLLEKGDKLVKE-SSPTTEVRAIADKVGELQGEW 8611
Cdd:PRK03918 539 GEIKS-------LKKELEKLEELKKKLAELEKKLDELEEElaelLKELEELGFESVEElEERLKELEPFYNEYLELKDAE 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8612 TRLQQEVTVQDSrltmagshaqqFTERLDKMAMWLQMTEEKLEKMKPEdVDQNTVVHKLKELQGVQNEMMKKSHDRERLN 8691
Cdd:PRK03918 612 KELEREEKELKK-----------LEEELDKAFEELAETEKRLEELRKE-LEELEKKYSEEEYEELREEYLELSRELAGLR 679
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 8692 SEGTSLVECVDSGK---EAIKQQVAVINE---RWDAVNKALSErashLEDLGQRLGEVQDSLAEAtsALNK 8756
Cdd:PRK03918 680 AELEELEKRREEIKktlEKLKEELEEREKakkELEKLEKALER----VEELREKVKKYKALLKER--ALSK 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8451-9293 |
5.44e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8451 QELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRskltaLEKDMNDTTRKLEICKAAVEEASQQAEKFEADCK 8530
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-----VKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8531 ELLTWISEAANNLQESEPLSSDLDILREQ-MRQNRTLQQELSLKEPEIRQLLEKGDKLVKE-SSPTTEVRAIADKVGELQ 8608
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDElKDYREKLEKLKREINELK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8609 GEWTRLQQEVTVQDSRLT-----MAGSHAQ--QFTERLDKMAMWLQMTEEKLEKMKPEDVDQNTVVHKLK-ELQGVQNEM 8680
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlnaaIAGIEAKinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeEYDRVEKEL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8681 MKKSHDRERLNSEGTSLVECVDSGKEAikqqVAVINERWDAVNKALSERASHLED--------LGQRLGEV---QDSLAE 8749
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAV----EEVLKASIQGVHGTVAQLGSVGERyataievaAGNRLNNVvveDDAVAK 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8750 ATSALNKWE----------NKLAV-HNSLGLSAK-------------DPKHINRIKDLLEDTGwlasqlnntetMLNSIE 8805
Cdd:TIGR02169 562 EAIELLKRRkagratflplNKMRDeRRDLSILSEdgvigfavdlvefDPKYEPAFKYVFGDTL-----------VVEDIE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8806 VDggetsnlRDELNKLRgqHQTLQGELSElvaemETGAqiveqfqgllkIVGGqFLELESELGSKTPVSRDDAELGSQLA 8885
Cdd:TIGR02169 631 AA-------RRLMGKYR--MVTLEGELFE-----KSGA-----------MTGG-SRAPRGGILFSRSEPAELQRLRERLE 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8886 DMKDFLTRLGEKVETLKDLEQQASSLcnagyVSDPE----LLKSQVEALSNQHASLTERATQRQSDvvanqhsIQHLTQA 8961
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQE-----LSDASrkigEIEKEIEQLEQEEEKLKERLEELEED-------LSSLEQE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8962 LNLVWGDIDKASSTLDAMgpaggnvttvkalQEELkgfvkstmEPLQKQFESvsrqgqalIKTAVAGSNTTGLETDLESL 9041
Cdd:TIGR02169 753 IENVKSELKELEARIEEL-------------EEDL--------HKLEEALND--------LEARLSHSRIPEIQAELSKL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9042 AERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQklvqkmvtdrtpsM 9121
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE-------------L 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9122 KAVQDSGNQLItgldpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEfqdvldpLTTWLDAANKRFTALEP 9201
Cdd:TIGR02169 871 EELEAALRDLE-----SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-------LKAKLEALEEELSEIED 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9202 HSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAG-KKLQDYckgEDVIM----IQLKIDGVQKQNGELRSHIEDCLEQ 9276
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNmLAIQEY---EEVLKrldeLKEKRAKLEEERKAILERIEEYEKK 1015
|
890 900
....*....|....*....|..
gi 1397727989 9277 -----MEEALPLAKHFQEAHAE 9293
Cdd:TIGR02169 1016 krevfMEAFEAINENFNEIFAE 1037
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9633-9906 |
5.97e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9633 ISAQPDKLREQIEE---------------NK--AMEEDLEmRHNALES-VKNAAEELLRQAgdEQDEAVKDVRQKLEELt 9694
Cdd:COG1196 150 IEAKPEERRAIIEEaagiskykerkeeaeRKleATEENLE-RLEDILGeLERQLEPLERQA--EKAERYRELKEELKEL- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9695 klykDIQERGRgRQRALEETLAVAEKfwdELHALNSSLKDLQEALSSVDqpalepEAIREQQEELEALKEDIEASQADFE 9774
Cdd:COG1196 226 ----EAELLLL-KLRELEAELEELEA---ELEELEAELEELEAELAELE------AELEELRLELEELELELEEAQAEEY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9775 EVQQTGDTLLG--MVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFE 9852
Cdd:COG1196 292 ELLAELARLEQdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9853 pvaSEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTPEQASVLRE 9906
Cdd:COG1196 372 ---AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
8154-8850 |
6.11e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.82 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8154 DDLSEVQQQLL---DITQRYEIVGERLADRQQELQLMLTSIrtfmQDMQDILQWLDL--KDHETDSAQPLPTNEK---DA 8225
Cdd:TIGR00606 224 DQITSKEAQLEssrEIVKSYENELDPLKNRLKEIEHNLSKI----MKLDNEIKALKSrkKQMEKDNSELELKMEKvfqGT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8226 KKRLKEHEVFH-REILSKEGLVEDIRKKAQDLLKTRHGVPGE----EMLQQQLQELDDKWH------GLRALSEQQRKGL 8294
Cdd:TIGR00606 300 DEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEktelLVEQGRLQLQADRHQehirarDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8295 EDMVSDLRDMREHEQQLTLwlaQKDRMLDVLGPVAMEPNMLASQM----EQVKVLREELSAQEPTYDH---FLNCAHGIL 8367
Cdd:TIGR00606 380 DGFERGPFSERQIKNFHTL---VIERQEDEAKTAAQLCADLQSKErlkqEQADEIRDEKKGLGRTIELkkeILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8368 ERCGDKSQDGIAVSRRLDTVSKAWNKLQSRLNERSKNlSSVEGISVEFASLTRGLADWLSDFSdkldgqgKVSSQPDKQH 8447
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN-SLTETLKKEVKSLQNEKADLDRKLR-------KLDQEMEQLN 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8448 KQLQELKQLESELIVQQPRLARARDL----CRQLCDKAKDASTKTDLRSKLTALEKDMNDTTRKLEICKAAVEEASQQAE 8523
Cdd:TIGR00606 529 HHTTTRTQMEMLTKDKMDKDEQIRKIksrhSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8524 KFEADCKELLTWISEAANNLQE---SEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLLEkgdKLVKESSPTTEVrai 8600
Cdd:TIGR00606 609 HINNELESKEEQLSSYEDKLFDvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFIT---QLTDENQSCCPV--- 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8601 ADKVGELQGEWtrlqQEVTVQDSRLTMAGSHAQQFTERLDKmamwlQMTEEKLEKMKPEDVDQNTVVHKLKELQGVQNEM 8680
Cdd:TIGR00606 683 CQRVFQTEAEL----QEFISDLQSKLRLAPDKLKSTESELK-----KKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKL 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8681 MKKSHDRERLNS---EGTSLVECVDSGKEAIK---QQVAVIN---ERWDAVNKALSERASHLE--DLGQRLGEVQDSLAE 8749
Cdd:TIGR00606 754 QKVNRDIQRLKNdieEQETLLGTIMPEEESAKvclTDVTIMErfqMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQE 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8750 ATSALNKWENKLAVHNSLglsakdpkhinrIKDLLEDTGWLASQLNNTETMLNSIEVDGGETSNLRDELNKLRGQHQTLQ 8829
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKL------------IQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
730 740
....*....|....*....|.
gi 1397727989 8830 GELSELVAEMETGAQIVEQFQ 8850
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQ 922
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
8272-8962 |
7.98e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8272 QLQELDDKWHGLRALSEQQRKGLEDMVSDLRD--------MREHEQQLtLWLAQKDRmldvlgpvamepnmLASQMEQVK 8343
Cdd:PRK10246 199 ELEKLQAQASGVALLTPEQVQSLTASLQVLTDeekqlltaQQQQQQSL-NWLTRLDE--------------LQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8344 ----VLREELSAQEPTYDHfLNCAHG------ILERCGDKSQDGIAVSRRLDTVSKawnKLQSRLNERSKNLSSVEGISV 8413
Cdd:PRK10246 264 qalqQALAAEEKAQPQLAA-LSLAQParqlrpHWERIQEQSAALAHTRQQIEEVNT---RLQSTMALRARIRHHAAKQSA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8414 EFASLTRGLADWLSD------FSDKLDGQGKVSSQPDKQHKQLQELKQLESELIVQQPRL-ARARDLCRQLCDKAKDAST 8486
Cdd:PRK10246 340 ELQAQQQSLNTWLAEhdrfrqWNNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNALpAITLTLTADEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8487 KTD-LRSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQ------ESEPLSSDLDILREQ 8559
Cdd:PRK10246 420 EQRpLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLAdvkticEQEARIKDLEAQRAQ 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8560 MRQNRTLQQELSLKEPEIR--QLLEKGDKLVKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTE 8637
Cdd:PRK10246 500 LQAGQPCPLCGSTSHPAVEayQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQ 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8638 RLDKMAMWLQMTEEKLEKMKP---EDVDQNTVVHKLKELQGVQNEMmkkshdrerlnsegtslvecvdsgkEAIKQQVAV 8714
Cdd:PRK10246 580 QWQAVCASLNITLQPQDDIQPwldAQEEHERQLRLLSQRHELQGQI-------------------------AAHNQQIIQ 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8715 INERWDAVNKALSERASHLEDLGQRLGEVQDSLAEATSALNKWENKLAVHNSLglsakdPKHINRIKDLLEdtgwLASQL 8794
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTAL------QNRIQQLTPLLE----TLPQS 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8795 NNTETMLNSIEVDggetsNLR---DELNKLRGQHQTLQGELSElvaEMETGAQIVEQFQGLLKivggqfleleselgskt 8871
Cdd:PRK10246 705 DDLPHSEETVALD-----NWRqvhEQCLSLHSQLQTLQQQDVL---EAQRLQKAQAQFDTALQ----------------- 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8872 pvsrddaelGSQLADMKDFLTRLGEKvETLKDLEQQASSLcnagyvsdpELLKSQVEALSNQHASLTERATQRQSDVVAN 8951
Cdd:PRK10246 760 ---------ASVFDDQQAFLAALLDE-ETLTQLEQLKQNL---------ENQRQQAQTLVTQTAQALAQHQQHRPDGLDL 820
|
730
....*....|.
gi 1397727989 8952 QHSIQHLTQAL 8962
Cdd:PRK10246 821 TVTVEQIQQEL 831
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
9210-9753 |
8.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9210 EHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgedvimIQLKIDGVQKQNGELRSHIEDcLEQMEEALPLAKHFQE 9289
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE---------LEEELEELEAELEELREELEK-LEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9290 AHAEFlswaSKVEPELRALElgvpDEETNIEELANQLTEemqpLLDIINSEGAELAEvAPGDAGLRVEDIINRDNKRFDN 9369
Cdd:COG4717 137 LEAEL----AELPERLEELE----ERLEELRELEEELEE----LEAELAELQEELEE-LLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9370 LRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDAD--SRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTL 9447
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9448 SASKKLLSDSAMEdNSAIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhfheahtelvVWLDDVEPVlSELDVLSVD 9527
Cdd:COG4717 284 GLLALLFLLLARE-KASLGKEAEELQALPALEELEEEELEELLAA----------------LGLPPDLSP-EELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9528 ADQVKKQQEKAKVLKQEVAdrkpiVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRmdnvrtkvrdrsnsiDQAMQQSA 9607
Cdd:COG4717 346 IEELQELLREAEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEY---------------QELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9608 EFTDKLENMLDTLTVTAEQvrsaepisAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAVKDVR 9687
Cdd:COG4717 406 ELEEQLEELLGELEELLEA--------LDEEELEEELEELEEELEELEEELEELREELAELEAELEQL--EEDGELAELL 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 9688 QKLEELtklykdiqergrgrqralEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIR 9753
Cdd:COG4717 476 QELEEL------------------KAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
523-617 |
8.84e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 523 FRHVQDCLDWIEAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE---EQKLYTQKLSSVE 599
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEghpDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1397727989 600 VAYSLLLNTSSRRLKFLE 617
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8983-9060 |
1.12e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 1.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 8983 GGNVTTVKALQEELKGFvKSTMEPLQKQFESVSRQGQALIKTAVAGSNTtgLETDLESLAERWAGLVEKVAEHEKNLD 9060
Cdd:smart00150 27 GKDLESVEALLKKHEAF-EAELEAHEERVEALNELGEQLIEEGHPDAEE--IEERLEELNERWEELKELAEERRQKLE 101
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
151-256 |
1.19e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 45.57 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 151 SAREALLLWSRRTtegYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLI-DFRQARSNSNKQNLELAFTVAEKEFGVTRLLD 229
Cdd:cd21312 12 TPKQRLLGWIQNK---LPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQVIT 88
|
90 100
....*....|....*....|....*..
gi 1397727989 230 PEDVDVPNPDEKSILTYVSSlydvFPQ 256
Cdd:cd21312 89 PEEIVDPNVDEHSVMTYLSQ----FPK 111
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
10804-10852 |
1.28e-04 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 45.94 E-value: 1.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1397727989 10804 GRVTRKEFIEGIISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 10852
Cdd:COG5126 48 GRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT 96
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9631-10268 |
1.34e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9631 EPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAgdEQDEAV-KDVRQKLEELTKLYKDIQERGRGRQR 9709
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI--ADDEKShSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9710 ALEETLAVAekfwDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEALKedieasqadfeevqqtgdtllgmvgt 9789
Cdd:PRK01156 240 ALNELSSLE----DMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDP-------------------------- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9790 teqpeVQKNVDDAGASLAAISDQYSKRsQELESALAQAVHFQDQLMKLlvwlQEAEDEFSEFEPVASEFETIKKQWDELK 9869
Cdd:PRK01156 290 -----VYKNRNYINDYFKYKNDIENKK-QILSNIDAEINKYHAIIKKL----SVLQKDYNDYIKKKSRYDDLNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9870 NFKTRVEPKNVEIESLNQHVTELTKSSTPEQASVlrepmtqlnirwnnlltnigdrQRELQMALLTAgqfdhahKELKNW 9949
Cdd:PRK01156 360 GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI----------------------SEILKIQEIDP-------DAIKKE 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9950 MDLVDVTLDEITpvygdpklveielAKLRIVQNDITAHQESVESISKEAQrLMTSEGIAQAQGL---KTKMEDMEKTWEN 10026
Cdd:PRK01156 411 LNEINVKLQDIS-------------SKVSSLNQRIRALRENLDELSRNME-MLNGQSVCPVCGTtlgEEKSNHIINHYNE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10027 IQAKSRAKQDMLEdglREAQGFTGELQDILAKINDIEGQLI-ISKPVGGLPETAKEQLEKFMDVYAEL-------EKLEP 10098
Cdd:PRK01156 477 KKSRLEEKIREIE---IEVKDIDEKIVDLKKRKEYLESEEInKSINEYNKIESARADLEDIKIKINELkdkhdkyEEIKN 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10099 QVQSLNVmgEKLGGKSKgpalANLRQNLQHLNQRCDYIRSRACDRKKKLEDAEG----MATNFHGELNKFISWLTDTEKT 10174
Cdd:PRK01156 554 RYKSLKL--EDLDSKRT----SWLNALAVISLIDIETNRSRSNEIKKQLNDLESrlqeIEIGFPDDKSYIDKSIREIENE 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10175 LNNLQPVSRLVERVTSQIEDHR----DLQKDISK-------HREAMVALEKMGTHLKYFSQKQDVVLI-----KNLLSSI 10238
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRgkidNYKKQIAEidsiipdLKEITSRINDIEDNLKKSRKALDDAKAnrarlESTIEIL 707
|
650 660 670
....*....|....*....|....*....|
gi 1397727989 10239 QHRWEKIVSRSAERTRHLERGYKEAKQFND 10268
Cdd:PRK01156 708 RTRINELSDRINDINETLESMKKIKKAIGD 737
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
9586-9779 |
1.35e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9586 DNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLtvtaeqVRSAEPISAQPDKLREQIEEnkaMEEDLEMRHNALESVK 9665
Cdd:PHA02562 191 DHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL------VEEAKTIKAEIEELTDELLN---LVMDIEDPSAALNKLN 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9666 NAA-------------EELLRQAG---------DEQDEAVKDVRQKLEELTKLYKDIQErgrgRQRALEETLAVAEKFWD 9723
Cdd:PHA02562 262 TAAakikskieqfqkvIKMYEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDT----AIDELEEIMDEFNEQSK 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 9724 ELHALNSSLKDLQEALSSVDQPALEPEA-IREQQEELEALKEDIEASQADFEEVQQT 9779
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAaIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9638-9870 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9638 DKLREQIEENKAMEEDLEmrhNALESVKnaAEELLRQAGDEQDEAVKDVR--QKLEELTKLYKDIQERG--RGRQRALEE 9713
Cdd:COG4913 228 DALVEHFDDLERAHEALE---DAREQIE--LLEPIRELAERYAAARERLAelEYLRAALRLWFAQRRLEllEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9714 TLAVAEkfwDELHALNSSLKDLQEALSsvdqpALEpEAIREQQ-EELEALKEDIEASQADFEEVQQTGDTLlgmvgtteq 9792
Cdd:COG4913 303 ELARLE---AELERLEARLDALREELD-----ELE-AQIRGNGgDRLEQLEREIERLERELEERERRRARL--------- 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 9793 pevQKNVDDAGASLAAISDqyskrsqELESALAQAVHFQDQLMKLLVWLQEAEDE-FSEFEPVASEFETIKKQWDELKN 9870
Cdd:COG4913 365 ---EALLAALGLPLPASAE-------EFAALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLER 433
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9177-9272 |
1.48e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.01 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9177 EFQDVLDPLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyCKGEDVIMIQLKI 9256
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90
....*....|....*.
gi 1397727989 9257 DGVQKQNGELRSHIED 9272
Cdd:smart00150 80 EELNERWEELKELAEE 95
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
37-134 |
1.51e-04 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 46.19 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNK---------HLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPrERGHMR-----FHKIQNVQIALDY 102
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTID-ERAINKkkltpFTISENLNLALNS 103
|
90 100 110
....*....|....*....|....*....|..
gi 1397727989 103 LRLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQII 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9685-9834 |
1.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9685 DVRQKLEELTKlykdiqergrgRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEAL-- 9762
Cdd:COG4913 607 DNRAKLAALEA-----------ELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELea 675
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397727989 9763 -KEDIEASQADFEEVQQtgdtllgmvgttEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQL 9834
Cdd:COG4913 676 eLERLDASSDDLAALEE------------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8892-9492 |
1.72e-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: 49.45 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8892 TRLGEKVETLKDLEQQASSLcNAGYVSDPELLKSQVEALSNQHASLTERATQRQSDVvanQHSIQHLTQALNLVWGDIDK 8971
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHL-HFGYKSDETLIASRQEERQETSAELNQLLRTLDDQW---KEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8972 ASSTLDAMGPAGG-----NVTTVKALQEELKGFvKSTMEPLQKQFE-------SVSRQGQALIKTAVAGSNT--TGLETD 9037
Cdd:pfam12128 320 DRSELEALEDQHGafldaDIETAAADQEQLPSW-QSELENLEERLKaltgkhqDVTAKYNRRRSKIKEQNNRdiAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9038 LESLAERWAGLVEKVAEHEKNLDSALlrtgkfQDAMASLLDWLAETEELVAmQKAPSPEQRVVRAQLQEQKLVQKMVTD- 9116
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESEL------REQLEAGKLEFNEEEYRLK-SRLGELKLRLNQATATPELLLQLENFDe 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9117 RTPSMKAVQDSGNqlitgldpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDP--------LTT- 9187
Cdd:pfam12128 472 RIERAREEQEAAN--------AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagtllhfLRKe 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9188 ---WLDAANKRF-------TALEPHSPDAEG---------------IEH-----LIQELKK--------LQKEVNEHEPA 9229
Cdd:pfam12128 544 apdWEQSIGKVIspellhrTDLDPEVWDGSVggelnlygvkldlkrIDVpewaaSEEELRErldkaeeaLQSAREKQAAA 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9230 MKQLATAGKKLQDYCKGEDVIMIQLK--IDGVQKQNGELRSHIEDCLEQMEEalplakHFQEAHAEFlswaSKVEPELRA 9307
Cdd:pfam12128 624 EEQLVQANGELEKASREETFARTALKnaRLDLRRLFDEKQSEKDKKNKALAE------RKDSANERL----NSLEAQLKQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9308 LELGVPDEETNIEELANQLTEEMQP-LLDIINSEGAELAEVAPGDAGLRVE-----DIINRDNKR-----------FDNL 9370
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGakaelKALETWYKRdlaslgvdpdvIAKL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9371 RDQIEKRAQKVQLARQRSSEVvnelgdlVDWFVDADSRLQNQQP--------IASDLDLLQQQLAEQKVMNEEINNQKVK 9442
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEV-------LRYFDWYQETWLQRRPrlatqlsnIERAISELQQQLARLIADTKLRRAKLEM 846
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1397727989 9443 ARDTLSASKKLLSDSAMEDNSAIRnKMDELK--QWVDTVSGSANERQSLLEQ 9492
Cdd:pfam12128 847 ERKASEKQQVRLSENLRGLRCEMS-KLATLKedANSEQAQGSIGERLAQLED 897
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
9679-9915 |
2.04e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9679 QDEAVKDVRQKLEELtklykdiQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQpalepeAIREQQEE 9758
Cdd:COG4942 18 QADAAAEAEAELEQL-------QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ------ELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9759 LEALKEDIEASQADFEEVQQTGDTLLG---MVGTTEQPEV---QKNVDDAGASLAAIS----------DQYSKRSQELES 9822
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRalyRLGRQPPLALllsPEDFLDAVRRLQYLKylaparreqaEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9823 ALAQAVHFQDQLMKLLVWLQEAEDEFSEFEpvASEFETIKKQWDELKNFKTRVEPKNVEIESLNQHVTELTKSSTPEQAS 9902
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALK--AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|...
gi 1397727989 9903 VLREPMTQLNIRW 9915
Cdd:COG4942 243 TPAAGFAALKGKL 255
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9121-9708 |
2.07e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9121 MKAVQDSGNQLITGLDpaerkHIESELQQLNSRWEALTKRVVDRTA----ILEEVQGLAGEFQDVLDPLTTwLDAANKRF 9196
Cdd:PRK01156 171 LKDVIDMLRAEISNID-----YLEEKLKSSNLELENIKKQIADDEKshsiTLKEIERLSIEYNNAMDDYNN-LKSALNEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9197 TALEphspdaEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQD------YCKGEDVI-MIQLKIDGVQKQngELRSH 9269
Cdd:PRK01156 245 SSLE------DMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvYKNRNYINdYFKYKNDIENKK--QILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9270 IEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEP------ELRALELGVPDEETNIEELANQLTEEM--QPLLDIINSEG 9341
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDlnnqilELEGYEMDYNSYLKSIESLKKKIEEYSknIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9342 AELAEVAPGDAGLRVEDIiNRD-----------NKRFDNLRDQIEKRAQKVQLARQRSSEVV--NELGD-----LVDWFV 9403
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEI-NVKlqdisskvsslNQRIRALRENLDELSRNMEMLNGQSVCPVcgTTLGEeksnhIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9404 DADSRLQNQ-QPIASDLDLLQQQLAEQKVMNEEINNQKVKardTLSASKKLLSdSAMEDNSAIRNKMDELKQWVDTVSGS 9482
Cdd:PRK01156 476 EKKSRLEEKiREIEIEVKDIDEKIVDLKKRKEYLESEEIN---KSINEYNKIE-SARADLEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9483 ANERQSLleqavpfarHFHEAHTELVVWLDdvepVLSELDVLSVDADQVKKQQEKAKVlkqevadrKPIVDRLNKTGTal 9562
Cdd:PRK01156 552 KNRYKSL---------KLEDLDSKRTSWLN----ALAVISLIDIETNRSRSNEIKKQL--------NDLESRLQEIEI-- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9563 vamcgskGAEQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDklre 9642
Cdd:PRK01156 609 -------GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN---- 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 9643 QIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQ 9708
Cdd:PRK01156 678 DIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
9630-9870 |
2.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9630 AEPISAQPDKLREQIEENKAMEEDLEMRHNALESV------------KNAAEELLRQAGDEQDEAVKDVRQKLEELTKLY 9697
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafeadPEAELRQLNRRRVELERALADHESQEQQQRSQL 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9698 KDIQERGRGRQRALEE-TLAVAEKFWDELHALNSSLKDLQEALSSVDQ-----PALEPEA--IREQQEELEALKEDIEAS 9769
Cdd:PRK04863 868 EQAKEGLSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRFVQQhgnalAQLEPIVsvLQSDPEQFEQLKQDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9770 QADFEEVQQTGDTLLGMVgtteQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQlmkllvwLQEAEDEFS 9849
Cdd:PRK04863 948 QQTQRDAKQQAFALTEVV----QRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ-------LRQAQAQLA 1016
|
250 260
....*....|....*....|....*
gi 1397727989 9850 EFEPV----ASEFETIKKQWDELKN 9870
Cdd:PRK04863 1017 QYNQVlaslKSSYDAKRQMLQELKQ 1041
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
8175-8758 |
2.19e-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: 49.07 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8175 ERLADRQQELQLMLTSIRTFMQDMQDILQW---------LDLKDHETDSAQPLpTNEKDAKKRLKEHEVFHREILS---K 8242
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKynrrrskikEQNNRDIAGIKDKL-AKIREARDRQLAVAEDDLQALEselR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8243 EGLVEDIR--KKAQDLLKTRHG--------VPGEEMLQQQLQELDDKWHGLRALSEQQRKGLEDMVSDLRDMReheqqlt 8312
Cdd:pfam12128 426 EQLEAGKLefNEEEYRLKSRLGelklrlnqATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR------- 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8313 lwlAQKDRMLDVLGPVAMEPNMLASQMEQVKvlrEELSAQEPTYDHFLN-------------CAHGILERC--------- 8370
Cdd:pfam12128 499 ---KRRDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRkeapdweqsigkvISPELLHRTdldpevwdg 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8371 ---GDKSQDGI-----------------AVSRRLDTVSKAWNKLQSRLNERSKNLSSvegISVEFASLTRGLADWLSDFS 8430
Cdd:pfam12128 573 svgGELNLYGVkldlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQ---ANGELEKASREETFARTALK 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8431 DKLDGQGKVS----SQPDKQHKQLQELKQLESELIVQQPRLARARDLCRQLCDKAKDASTKTDLRSKLTALEKDMNDTTR 8506
Cdd:pfam12128 650 NARLDLRRLFdekqSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDA 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8507 KLEICKAAVEEASQQAEkfeADCKELLTWiseaanNLQESEPLSSDLDILREQMRQNRTLQQELS---LKEPEIRQ---- 8579
Cdd:pfam12128 730 QLALLKAAIAARRSGAK---AELKALETW------YKRDLASLGVDPDVIAKLKREIRTLERKIEriaVRRQEVLRyfdw 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8580 -----LLEKgDKLVkessptTEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMaGSHAQQFTE-RLDKMAMWLQMTEEKL 8653
Cdd:pfam12128 801 yqetwLQRR-PRLA------TQLSNIERAISELQQQLARLIADTKLRRAKLEM-ERKASEKQQvRLSENLRGLRCEMSKL 872
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8654 EKMKpEDVDQNTVVHKLKELQGvQNEMMKKSHDRErlnsegtslvecvdsgKEAIKQQVavinERWDAVNKALSerASHL 8733
Cdd:pfam12128 873 ATLK-EDANSEQAQGSIGERLA-QLEDLKLKRDYL----------------SESVKKYV----EHFKNVIADHS--GSGL 928
|
650 660
....*....|....*....|....*.
gi 1397727989 8734 EDLGQRLGEVQDSL-AEATSALNKWE 8758
Cdd:pfam12128 929 AETWESLREEDHYQnDKGIRLLDYRK 954
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9599-10297 |
2.38e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9599 IDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDE 9678
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9679 QDEAVKDVRqklEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNsslKDLQEALSSVDQPALEPEAIREQ--- 9755
Cdd:TIGR00606 292 MEKVFQGTD---EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN---QEKTELLVEQGRLQLQADRHQEHira 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9756 ----------QEELEALKED--IEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISDQYSKRSQELE-- 9821
Cdd:TIGR00606 366 rdsliqslatRLELDGFERGpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIElk 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9822 ---------------SALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVASeFETIKKQWDELKNFKTRVEPK----NVEI 9882
Cdd:TIGR00606 446 keilekkqeelkfviKELQQLEGSSDRILELDQELRKAERELSKAEKNSL-TETLKKEVKSLQNEKADLDRKlrklDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9883 ESLNQHVTELTKSStpeqaSVLREPMTQLN-IRWNNlltnigdrQRELQMALLTAGQFDHAhKELKNWMDLVDvtlDEIT 9961
Cdd:TIGR00606 525 EQLNHHTTTRTQME-----MLTKDKMDKDEqIRKIK--------SRHSDELTSLLGYFPNK-KQLEDWLHSKS---KEIN 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9962 PVYGDPKLVEIELAKLRIVQNDITAHQEsvesiSKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQaKSRAKQDMLEDG 10041
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELE-----SKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIE-KSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10042 LREAQGFTGELQDILAKINDIEGQLIISKpvGGLPETAKEQLEKFMDVYAELEKLEPQVQSLNVMGEKLGGKSKGPA--- 10118
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTE--AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQsii 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10119 ------LANLRQNLQHLNQRCDYIRSRACDRKK-------KLEDAEGMATNFhGELNKFISWLTDTEKTLNNL------- 10178
Cdd:TIGR00606 740 dlkekeIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpEEESAKVCLTDV-TIMERFQMELKDVERKIAQQaaklqgs 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10179 ---QPVSRLVERVTSQIEDHRDLQKDISKHREAMVALEKMGTHLKyfSQKQDVVLIKNLLSSIQHRWEKIVSRSAERTRH 10255
Cdd:TIGR00606 819 dldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK--SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE 896
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1397727989 10256 LERGYKEAKQFNDTWKDLITWLIEAEKTLETETSVANEPDKI 10297
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
8301-8405 |
2.87e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.24 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8301 LRDMREHEQqltlWLAQKDRMLDVLgPVAMEPNMLASQMEQVKVLREELSAQEPTYDHFLNCAHGILERCGDKSQDgiaV 8380
Cdd:smart00150 4 LRDADELEA----WLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEE---I 75
|
90 100
....*....|....*....|....*
gi 1397727989 8381 SRRLDTVSKAWNKLQSRLNERSKNL 8405
Cdd:smart00150 76 EERLEELNERWEELKELAEERRQKL 100
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
9209-9699 |
3.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9209 IEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDyckgeDVIMIQLKIDGVQKQNGELRSHIEDCLEQMEEA-------- 9280
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-----EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeleqnn 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9281 ---LPLAKHFQEAHAEFLS--------WASKVEPELRalelgvpDEETNIEELANQLTEEMQplldIINSEGAELAEvap 9349
Cdd:TIGR04523 281 kkiKELEKQLNQLKSEISDlnnqkeqdWNKELKSELK-------NQEKKLEEIQNQISQNNK----IISQLNEQISQ--- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9350 gdagLRVEdiinRDNKRFDN--LRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQNQQPIASDLDLLQQQLA 9427
Cdd:TIGR04523 347 ----LKKE----LTNSESENseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9428 EQK-VMNEEINN---QKVKARDTLSASKKLLSDSAMEDNSaIRNKMDELKQWVDTVSGSANERQSLLEQavpfarhfhea 9503
Cdd:TIGR04523 419 QEKeLLEKEIERlkeTIIKNNSEIKDLTNQDSVKELIIKN-LDNTRESLETQLKVLSRSINKIKQNLEQ----------- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9504 hteLVVWLDDVEPVLSELDvlsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALvamcgskgaEQVQSMLDDDNR 9583
Cdd:TIGR04523 487 ---KQKELKSKEKELKKLN------EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK---------ESKISDLEDELN 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9584 RMDNVRTK--VRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSA--------EPISAQPDKLREQIEENKAMEED 9653
Cdd:TIGR04523 549 KDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEkkdlikeiEEKEKKISSLEKELEKAKKENEK 628
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 9654 LEMRHNALESVKNAAEELLRQAGDEQDEAV----------KDVRQKLEELTKLYKD 9699
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRnkwpeiikkiKESKTKIDDIIELMKD 684
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
9515-9759 |
3.85e-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: 47.76 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9515 EPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAM-----------------CGSKGAEQ---- 9573
Cdd:pfam05622 228 ERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAeireklirlqhenkmlrLGQEGSYRerlt 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9574 -VQSMLDDDNRRMDNVRTKVRdrsnsidQAMQQSAEFTDKLENMLDTLTvtaEQVRSAEPISAQPDKLREQIEENKAMEE 9652
Cdd:pfam05622 308 eLQQLLEDANRRKNELETQNR-------LANQRILELQQQVEELQKALQ---EQGSKAEDSSLLKQKLEEHLEKLHEAQS 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9653 DLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwDELHALNSSL 9732
Cdd:pfam05622 378 ELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASP--PEIQALKNQL 455
|
250 260
....*....|....*....|....*..
gi 1397727989 9733 KDLQEALSSVDQPALEPEAIREQQEEL 9759
Cdd:pfam05622 456 LEKDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9034-9702 |
4.15e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9034 LETDLESL------AERWAGLVEKVAEHEKNLdsALLRTGKFQDAMASLLDWLAETEELVAMQKApspEQRVVRAQLQEQ 9107
Cdd:COG1196 198 LERQLEPLerqaekAERYRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9108 KLVQKMVTDRTPSMKA----VQDSGNQLITGLDPAE--RKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDV 9181
Cdd:COG1196 273 RLELEELELELEEAQAeeyeLLAELARLEQDIARLEerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9182 LDPLTTWLDAANKRFTALEphspdaEGIEHLIQELKKLQKEVNEhepAMKQLATAGKKLQDyckgedvimIQLKIDGVQK 9261
Cdd:COG1196 353 LEEAEAELAEAEEALLEAE------AELAEAEEELEELAEELLE---ALRAAAELAAQLEE---------LEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9262 QNGELRSHIEDCLEQMEEALPLAKHFQEAHAEFLSWASKVEPELRALELGVPDEETNIEELANQLTEEMQPLLDIINSEG 9341
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9342 AELAEVAPgdaglrvediinrdnkrfDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFVDADSRLQN--QQPIASDL 9419
Cdd:COG1196 495 LLLEAEAD------------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9420 DLLQQQLAEQKvmneeinnQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDElkqwvdtvsgsANERQSLLEQAVPFARH 9499
Cdd:COG1196 557 EVAAAAIEYLK--------AAKAGRATFLPLDKIRARAALAAALARGAIGAA-----------VDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9500 FHEAHTELVVWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLD 9579
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9580 DDNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHN 9659
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1397727989 9660 ALESVKNAAEEllrqagdEQDEavkdVRQKLEELTKLYKDIQE 9702
Cdd:COG1196 778 ALGPVNLLAIE-------EYEE----LEERYDFLSEQREDLEE 809
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
32-140 |
4.19e-04 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 44.21 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 32 ERDAVQKKTFTKWVNKhlMKAGLRIIDLFDDLRDGHNLISLLEVLAHDI---------LPRERGHMRfhKIQNVQIALDY 102
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMTRVPVdwghvnkppYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1397727989 103 LRLKG-IRLVNIRSDEIVDGNPKLTLGLIWTIILHFQIS 140
Cdd:cd21329 78 GKNKAkFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9243-9894 |
4.19e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9243 YCKGEDVI-MIQLKIDGVQKQNGELRSHIEDcLEQMEEALplakhfqeahAEFLSWASKVEPELRALElgvpdEETNIEE 9321
Cdd:PRK01156 168 YDKLKDVIdMLRAEISNIDYLEEKLKSSNLE-LENIKKQI----------ADDEKSHSITLKEIERLS-----IEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9322 ----LANQLTEEMQPLLDIINSEGAELAEVapgDAGLRVEDIINRDNKRFDNLRDQIEKraQKVQLARQRSSEVVNELGD 9397
Cdd:PRK01156 232 ddynNLKSALNELSSLEDMKNRYESEIKTA---ESDLSMELEKNNYYKELEERHMKIIN--DPVYKNRNYINDYFKYKND 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9398 LVDW---FVDADSRLQNQQPIASDLDLLQQ---QLAEQKVMNEEINNQKVKardtlsaskklLSDSAMEDNSAIRNkMDE 9471
Cdd:PRK01156 307 IENKkqiLSNIDAEINKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQILE-----------LEGYEMDYNSYLKS-IES 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9472 LKQWVDtvsgsanerqsllEQAVPFARHFHEAHTELVVWLDDVEPVLSELDVLSVDADQVKKQ----QEKAKVLKQEVAD 9547
Cdd:PRK01156 375 LKKKIE-------------EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKvsslNQRIRALRENLDE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9548 RKPIVDRLNktGTALVAMCGSK-GAEQVQSMLDDDNRRMDNVRTKVRDRSN---SIDQAMQQSAEFTDKLE--------- 9614
Cdd:PRK01156 442 LSRNMEMLN--GQSVCPVCGTTlGEEKSNHIINHYNEKKSRLEEKIREIEIevkDIDEKIVDLKKRKEYLEseeinksin 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9615 --NMLDTLTVTAEQVRSAEP-ISAQPDKLREQIEENKAME-EDLEMRH----NALESVKNAAEELLRQAGDEQDEAVKDV 9686
Cdd:PRK01156 520 eyNKIESARADLEDIKIKINeLKDKHDKYEEIKNRYKSLKlEDLDSKRtswlNALAVISLIDIETNRSRSNEIKKQLNDL 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9687 RQKLEELTKLYKDIQERGRGRQRALEetlavaekfwDELHALNSSLKDLQEalssvdqpalEPEAIREQQEELEALKEDI 9766
Cdd:PRK01156 600 ESRLQEIEIGFPDDKSYIDKSIREIE----------NEANNLNNKYNEIQE----------NKILIEKLRGKIDNYKKQI 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9767 easqadfeevqqtgdtllgmvgtTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQAVHFQDQLMKLLVWLQEAED 9846
Cdd:PRK01156 660 -----------------------AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSD 716
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 9847 EFSEFEPVASEFETIKKQWDELKNFKTRVEPKNVEI---ESLNQHVTELTK 9894
Cdd:PRK01156 717 RINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAmirKSASQAMTSLTR 767
|
|
| EFh |
smart00054 |
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ... |
10826-10852 |
4.84e-04 |
|
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.
Pssm-ID: 197492 [Multi-domain] Cd Length: 29 Bit Score: 41.21 E-value: 4.84e-04
10 20
....*....|....*....|....*..
gi 1397727989 10826 EMEKVADIFDKDGDGFINYKEFVAALR 10852
Cdd:smart00054 1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9140-9850 |
4.93e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9140 RKHIESELQQLnsrwEALTkRVVDRTAILEEVQGLAGEFQDVLDPLTTWldAANKRFTALEPHspdaegIEHLIQELKKL 9219
Cdd:COG4913 241 HEALEDAREQI----ELLE-PIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAE------LEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9220 QKEVNEHEpamKQLATAGKKLQDYckgEDVImiqLKIDGVQKQngELRSHIEDCLEQMEEALPLAKHFQEAhaeflswas 9299
Cdd:COG4913 308 EAELERLE---ARLDALREELDEL---EAQI---RGNGGDRLE--QLEREIERLERELEERERRRARLEAL--------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9300 kvepeLRALELGVPDEETNIEELANQLTEemqpLLDIINSEGAELAEVApgdAGLRVEdiINRDNKRFDNLRDQI---EK 9376
Cdd:COG4913 368 -----LAALGLPLPASAEEFAALRAEAAA----LLEALEEELEALEEAL---AEAEAA--LRDLRRELRELEAEIaslER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9377 RA----QKVQLARQRSSEVVNE-------LGDLVDwfVDADSR---------LQNQQpiasdLDLL--QQQLA------E 9428
Cdd:COG4913 434 RKsnipARLLALRDALAEALGLdeaelpfVGELIE--VRPEEErwrgaiervLGGFA-----LTLLvpPEHYAaalrwvN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9429 QKVMNEEINNQKVKARDTLSASKKLLSDSamednsaIRNKMD----ELKQW-------------VDTVSGSANERQSLLE 9491
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPRLDPDS-------LAGKLDfkphPFRAWleaelgrrfdyvcVDSPEELRRHPRAITR 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9492 QAVpfARHFHEAHTelvvwLDDVEPVLSELdVLSVDAdqvkkqQEKAKVLKQEVADrkpIVDRLNKTGTALvamcgskga 9571
Cdd:COG4913 580 AGQ--VKGNGTRHE-----KDDRRRIRSRY-VLGFDN------RAKLAALEAELAE---LEEELAEAEERL--------- 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9572 EQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSAEftDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKAME 9651
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDEIDVASAEREI--AELEAELERLDASSDDLAALE---EQLEELEAELEELEEEL 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9652 EDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKL-EELTKLYKDIQERGRGRQ--RALEETLAVAEKfwdELHAL 9728
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERElrENLEERIDALRA---RLNRA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9729 NSSLKDLQEALSSVDQPAL-----EPEAIREQQEELEALKED-IEASQADFEEV--QQTGDTLLGMVGTTEQP--EVQKN 9798
Cdd:COG4913 786 EEELERAMRAFNREWPAETadldaDLESLPEYLALLDRLEEDgLPEYEERFKELlnENSIEFVADLLSKLRRAirEIKER 865
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 9799 VDDAGASLAAIsDQYSKRSQELE---SALAQAVHFQDQLMKLLVWLQEAEDEFSE 9850
Cdd:COG4913 866 IDPLNDSLKRI-PFGPGRYLRLEarpRPDPEVREFRQELRAVTSGASLFDEELSE 919
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
162-233 |
5.17e-04 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 42.67 E-value: 5.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 162 RTTEGYPGVKIKDFSSSWRDGKAFLSIIHRNRPDLID-----FRQARSNSNKQ-NLELAFTVAEKEFGVTRL-LDPEDV 233
Cdd:pfam11971 3 SQRSLPLSPPVEDLLRDLSDGCALAALIHFYCPQLIDledicLKESMSLADSLyNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
8631-8735 |
5.24e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.46 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8631 HAQQFTERLDKMAMWLQMTEEKLEKM-KPEDVDqnTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIK 8709
Cdd:pfam00435 2 LLQQFFRDADDLESWIEEKEALLSSEdYGKDLE--SVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQ 79
|
90 100
....*....|....*....|....*.
gi 1397727989 8710 QQVAVINERWDAVNKALSERASHLED 8735
Cdd:pfam00435 80 ERLEELNERWEQLLELAAERKQKLEE 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7446-8025 |
6.28e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7446 QELMTEQEHLGDLEQILKHDSQMGDEASKVKLQLEAHKSTHEKIQSQQQPILSLVYKaEQLTENYQEELTPEQVTQLTTQ 7525
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK-LQSLCKELDILQREQATIDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7526 AS-----LLKATLEKVSKTSERRLSHLTKAADELAKFEEESKKFRTWMGAAFSELTNQEDYLKRFedLKVLGEKHRELAS 7600
Cdd:TIGR00618 417 SAfrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--HLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7601 DISSHQADHRFMSMAVQKYMEEA-KLYKLEMDSFRADRARPARHSLISMEcvaaDNVKDKLTDLTEEYHDLSNRCNLLGD 7679
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLETSE----EDVYHQLTSERKQRASLKEQMQEIQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7680 RLADLSGKHRQFNDVAFKLLTWLTDM----EGQLSSVKQDAGLSEPQ--QLQVHLDRL-KSLSMDALSQKLLLDEMQKRG 7752
Cdd:TIGR00618 571 SFSILTQCDNRSKEDIPNLQNITVRLqdltEKLSEAEDMLACEQHALlrKLQPEQDLQdVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7753 QDLT--------NSLSGQAAEQQQVAKLQSTMNDLSVRYSTLTKD---INSHVTQLQAAVTHSQDITQAMNELvswmdsa 7821
Cdd:TIGR00618 651 LQLTltqervreHALSIRVLPKELLASRQLALQKMQSEKEQLTYWkemLAQCQTLLRELETHIEEYDREFNEI------- 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7822 eqvvttQLPISLRRPELNAQLQSfsavdadvtnHQSALDAVKALANELVKTCELDIARAVE------QRLTSLDEKFSSL 7895
Cdd:TIGR00618 724 ------ENASSSLGSDLAAREDA----------LNQSLKELMHQARTVLKARTEAHFNNNEevtaalQTGAELSHLAAEI 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7896 QAKCRQRDRDLEEVDSSLREFQEKLEqtnlwvHDGilqlDSKELSKLSSDDMKQQLEKLAREKHNRLRTIQEIQVAAEQL 7975
Cdd:TIGR00618 788 QFFNRLREEDTHLLKTLEAEIGQEIP------SDE----DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEEC 857
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7976 LQDPRTGEGEAVKnlVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENA 8025
Cdd:TIGR00618 858 SKQLAQLTQEQAK--IIQLSDKLNGINQIKIQFDGDALIKFLHEITLYAN 905
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
9624-9713 |
6.74e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 43.08 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9624 AEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELLrqagDEQDEAVKDVRQKLEELTKLYKDIQER 9703
Cdd:pfam00435 20 KEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI----DEGHYASEEIQERLEELNERWEQLLEL 95
|
90
....*....|
gi 1397727989 9704 GRGRQRALEE 9713
Cdd:pfam00435 96 AAERKQKLEE 105
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
10826-10852 |
6.85e-04 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 40.85 E-value: 6.85e-04
10 20
....*....|....*....|....*..
gi 1397727989 10826 EMEKVADIFDKDGDGFINYKEFVAALR 10852
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLK 27
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
37-134 |
7.04e-04 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 44.28 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNK---------HLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMR----FHKIQNVQIALDYL 103
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKkltpFIIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 104 RLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
9656-9778 |
7.12e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 44.13 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9656 MRHNALESVKNAAEELLRQAGDEQDEAVK---DVRQKLEELTKLYKDIQERgrgRQRALEETLAVAEkfwdelhalnssL 9732
Cdd:COG2882 2 KRSFRLQTLLDLAEKEEDEAARELGQAQQaleQAEEQLEQLEQYREEYEQR---LQQKLQQGLSAAQ------------L 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1397727989 9733 KDLQEALSSVDQpalepeAIREQQEELEALKEDIEASQADFEEVQQ 9778
Cdd:COG2882 67 RNYQQFIARLDE------AIEQQQQQVAQAEQQVEQARQAWLEARQ 106
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
9390-9491 |
9.61e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9390 EVVNELGDLVDWFVDADSRLQnQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAmEDNSAIRNKM 9469
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGH-PDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1397727989 9470 DELKQWVDTVSGSANERQSLLE 9491
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
8673-9241 |
9.89e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8673 LQGVQNEMMKK--SHDRERLNSEgtslvecvdSGKEAIKQQVAVINERwdavNKALSERASHLEDlgqrlgevQDSLAEA 8750
Cdd:pfam05557 11 LSQLQNEKKQMelEHKRARIELE---------KKASALKRQLDRESDR----NQELQKRIRLLEK--------REAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8751 TSALNKWENKLAVHNSLGLSakdpKHINRIKDLLEDTGWLASQLNN-TETMLNSIEVDGGETSNLRDELNKLRGQHQTLQ 8829
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALN----KKLNEKESQLADAREVISCLKNeLSELRRQIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8830 GELSelvaEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpvsrDDAELgsqLADMKDFLTRLGEKVETLKDLEQQAS 8909
Cdd:pfam05557 146 AKAS----EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQE----QDSEI---VKNSKSELARIPELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8910 SLCNAgyVSDPELLKSQVEALSNQhaslTERATQRQSDVVANQHSIQHLTQALNlVWGDIDKaSSTLDAMGPAGGNVTTV 8989
Cdd:pfam05557 215 HLNEN--IENKLLLKEEVEDLKRK----LEREEKYREEAATLELEKEKLEQELQ-SWVKLAQ-DTGLNLRSPEDLSRRIE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8990 KALQEELK-GFVKSTMEPLQKQFESVSRQGQalIKTAVAGSNTTGLETDLESLAERWAGLVEKV--AEHEKNLDSALLrt 9066
Cdd:pfam05557 287 QLQQREIVlKEENSSLTSSARQLEKARRELE--QELAQYLKKIEDLNKKLKRHKALVRRLQRRVllLTKERDGYRAIL-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9067 GKFQDAMA------SLLDWLAETEELVAMQKAPSPEQRVVRAQLQE----QKLVQKMVTDRTPSMKAVQDSGNQLIT--G 9134
Cdd:pfam05557 363 ESYDKELTmsnyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEelggYKQQAQTLERELQALRQQESLADPSYSkeE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9135 LDPAERK--HIESELQQLNSRWEALTKRVVDR----------TAILEEVQGLAGEFQDVLDPLTTWLDAANKRFTAL-EP 9201
Cdd:pfam05557 443 VDSLRRKleTLELERQRLREQKNELEMELERRclqgdydpkkTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLlKK 522
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1397727989 9202 HSPDAEGIEHL-IQELKKLQKEVNEHEpamKQLATAGKKLQ 9241
Cdd:pfam05557 523 LEDDLEQVLRLpETTSTMNFKEVLDLR---KELESAELKNQ 560
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
10804-10852 |
1.05e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 41.47 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1397727989 10804 GRVTRKEFIEGI--ISSKFPTSKLEMEKVADIFDKDGDGFINYKEFVAALR 10852
Cdd:pfam13499 17 GYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9422-9911 |
1.13e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9422 LQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDTVSGSANERQSlLEQAVPFARHFH 9501
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA-RNKAEKQRRDLG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9502 EahtelvvwldDVEPVLSEL-DVLsvdaDQVKKQQEKAKVLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLD- 9579
Cdd:pfam01576 299 E----------ELEALKTELeDTL----DTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEq 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9580 -DDNRRMDNVRTKVR-----DRSN------SIDQAMQQSAEFTDKLENMLDTLTVTA-EQVRSAEPISAQPDKLREQIEE 9646
Cdd:pfam01576 365 lEQAKRNKANLEKAKqalesENAElqaelrTLQQAKQDSEHKRKKLEGQLQELQARLsESERQRAELAEKLSKLQSELES 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9647 NKAMEEDLEMRhnALESVKNAAeELLRQAGDEQDEAVKDVRQKLEELTKLyKDIQERGRGRQRALEETLAVAEKFWDELH 9726
Cdd:pfam01576 445 VSSLLNEAEGK--NIKLSKDVS-SLESQLQDTQELLQEETRQKLNLSTRL-RQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9727 ALNSSLKD----LQEALSSVDqpALEpEAIREQQEELEALKEDIEASQADFEE-------VQQTGDTLLGMVGTTEQ--- 9792
Cdd:pfam01576 521 TLQAQLSDmkkkLEEDAGTLE--ALE-EGKKRLQRELEALTQQLEEKAAAYDKlektknrLQQELDDLLVDLDHQRQlvs 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9793 --PEVQKNVDDAGASLAAISDQYskrSQELESALAQAVHFQDQLMKLLVWLQEAEDEFSEFEPVAsefETIKKQWDELKN 9870
Cdd:pfam01576 598 nlEKKQKKFDQMLAEEKAISARY---AEERDRAEAEAREKETRALSLARALEEALEAKEELERTN---KQLRAEMEDLVS 671
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1397727989 9871 FKTRVePKNVeieslnqHVTELTKSSTPEQASVLREPMTQL 9911
Cdd:pfam01576 672 SKDDV-GKNV-------HELERSKRALEQQVEEMKTQLEEL 704
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
35-138 |
1.29e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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: 409186 Cd Length: 129 Bit Score: 43.06 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMR----FHKIQNVQIALDYLRLKGIRL 110
Cdd:cd21337 19 NVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEK 98
|
90 100
....*....|....*....|....*...
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHFQ 138
Cdd:cd21337 99 PKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7412-8044 |
1.33e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7412 QRLTDILFKLNLKTGSTARERRKgrlADSFDSIVQELMTEQEHL--GDLEQILKHDSQMGDEASKVKLQLEAHKSTHEKI 7489
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEK---AERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7490 QSQQQPILSLVYKAEQLTENYQEEL--TPEQVTQLTTQASLLKATLEKVSKTSERR-------LSHLTKAADELAKFEEE 7560
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELyaLANEISRLEQQKQILRERLANLERQLEELeaqleelESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7561 SKKFRTWMGAAFSELTNQEDYLKRFEDLKV-LGEKHRELASDISSH-----QADHRFMSMAVQKYMEEAKLYKLEMD-SF 7633
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLelqiaSLNNEIERLEARLERLEDRRERLQQEiEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7634 RADRARPARHSLISMECvaaDNVKDKLTDLTEEYHDLSNRCNLLGDRLADLSGKHRQFNDVAFKL---LTWLTDMEGQLS 7710
Cdd:TIGR02168 426 LLKKLEEAELKELQAEL---EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7711 S----VKQ--DAGLSEPQQLQVHLDRLK-----SLSMDAL----SQKLLLD--EMQKRGQD-LTNSLSGQAA-------- 7764
Cdd:TIGR02168 503 GfsegVKAllKNQSGLSGILGVLSELISvdegyEAAIEAAlggrLQAVVVEnlNAAKKAIAfLKQNELGRVTflpldsik 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7765 -EQQQVAKLQSTMNDLSVRysTLTKDINSHVTQLQAAVTH-------SQDITQAMNELVSwMDSAEQVVTTQLPISLRRp 7836
Cdd:TIGR02168 583 gTEIQGNDREILKNIEGFL--GVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKK-LRPGYRIVTLDGDLVRPG- 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7837 elnaqlqsFSAVDADVTNHQSALDAVKALAnELVKTCEL--DIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLR 7914
Cdd:TIGR02168 659 --------GVITGGSAKTNSSILERRREIE-ELEEKIEEleEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7915 EFQEKLEQTNLWVHDGILQLDSKELSKLSSDDMK----QQLEKLAREKHNRLRTIQEIQVAAEQLLQDPRTGE--GEAVK 7988
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIeeleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALReaLDELR 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 7989 NLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWLSQMEARLDEFQ 8044
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
9141-9477 |
1.59e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9141 KHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDplttwldaANKRFTALEPHSPDAEgiEHLIQELKKLQ 9220
Cdd:pfam05483 380 KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD--------EKKQFEKIAEELKGKE--QELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9221 KEVNEHEpamKQLATAGKKLQDYCKgeDVIMIQLKIDGVQKQNGELRSHIEDCL----EQMEEALPLAKHFQEAHAEFLS 9296
Cdd:pfam05483 450 KEIHDLE---IQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNIELTAHCDKLLlenkELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9297 WASKVEPELRALElGVPDEETNIEELANQLTEEMQPLLDIINS--EGAELAEVAPGDAGLRVEDIINRDNKRFDNLRDQI 9374
Cdd:pfam05483 525 CKKQEERMLKQIE-NLEEKEMNLRDELESVREEFIQKGDEVKCklDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9375 EKRAQKVQLARQRSSEVVNElgdlvdwfVDADSRLQNQQPIASDLDLLQQQLAEQKvMNEEINNQKVKARDTLSASKKLL 9454
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKK--------GSAENKQLNAYEIKVNKLELELASAKQK-FEEIIDNYQKEIEDKKISEEKLL 674
|
330 340
....*....|....*....|...
gi 1397727989 9455 SDsaMEDNSAIRNKMDELKQWVD 9477
Cdd:pfam05483 675 EE--VEKAKAIADEAVKLQKEID 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
8388-8629 |
1.61e-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: 45.53 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8388 SKAWNKLQSRLNERSKNLSSVEGISVEFASLTRGLADWLSDFSDKLDGQGKVSSQPDKQHKQLQ-ELKQLESELIVQQPR 8466
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8467 LARARDLCRQLCDKAKDASTKTDLRSKLTAleKDMNDTTRKLEICKAAVEEASQQAEKFEADCKELLTWISEAANNLQEs 8546
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8547 eplssdldiLREQMRQNRTLQQELSLKEPEIRQLLEKGDKlvKESSPTTEVRAIADKVGELQGEWTRLQQEVTVQDSRLT 8626
Cdd:COG4942 176 ---------LEALLAELEEERAALEALKAERQKLLARLEK--ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 1397727989 8627 MAG 8629
Cdd:COG4942 245 AAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
9483-9828 |
1.66e-03 |
|
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: 46.10 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9483 ANERQSLLEQAVPFARHfheahtelvvWLDDVEPVLSELDVLSVDADQVKKQQEKAKVLKQEVadrKPIVDRLNKTGTAL 9562
Cdd:COG3096 277 ANERRELSERALELRRE----------LFGARRQLAEEQYRLVEMARELEELSARESDLEQDY---QAASDHLNLVQTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9563 vamcgsKGAEQVQSMLDDdnrrmdnvrtkVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVrsaepisaqpDKLRE 9642
Cdd:COG3096 344 ------RQQEKIERYQED-----------LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV----------DSLKS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9643 QIEEnkaMEEDLEMRH----------NALE-----------SVKNAAEEL--LRQAGDEQDEAVKDVRQKL--------- 9690
Cdd:COG3096 397 QLAD---YQQALDVQQtraiqyqqavQALEkaralcglpdlTPENAEDYLaaFRAKEQQATEEVLELEQKLsvadaarrq 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9691 -----EELTKLYKDIqERGRGRQRALE------ETLAVAEKfwdeLHALNSSLKDLQEALS--------------SVDQP 9745
Cdd:COG3096 474 fekayELVCKIAGEV-ERSQAWQTAREllrryrSQQALAQR----LQQLRAQLAELEQRLRqqqnaerlleefcqRIGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9746 ALEPEAIREQQEELEALKEDIEASQADFEE----VQQTGDTLLGMVGTTEQPE-VQKNVDDAGASLAAISDQYSKRSQEL 9820
Cdd:COG3096 549 LDAAEELEELLAELEAQLEELEEQAAEAVEqrseLRQQLEQLRARIKELAARApAWLAAQDALERLREQSGEALADSQEV 628
|
....*...
gi 1397727989 9821 ESALAQAV 9828
Cdd:COG3096 629 TAAMQQLL 636
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
9649-9824 |
1.79e-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: 44.53 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9649 AMEEDLEM------RHNALESVKNAAEELLRQAGDEQDEaVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFW 9722
Cdd:COG1579 1 AMPEDLRAlldlqeLDSELDRLEHRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9723 D---------ELHALNSSLKDLQEALSsvdqpALEpEAIREQQEELEALKEDIEASQADFEEVQQTGDtllgmvgtteqp 9793
Cdd:COG1579 80 EqlgnvrnnkEYEALQKEIESLKRRIS-----DLE-DEILELMERIEELEEELAELEAELAELEAELE------------ 141
|
170 180 190
....*....|....*....|....*....|.
gi 1397727989 9794 EVQKNVDDAGASLAAISDQYSKRSQELESAL 9824
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8659-9228 |
2.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8659 EDVDQNTVVHKLKELQGVQNEMMKKSHDRERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSERASHLEDLGQ 8738
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8739 -------RLGEVQDSLAEATSALNKWENKLAvhnslGLSAKDPKHINRIKDLLEDTGWLASQLNNTETMLNSIEvdgGET 8811
Cdd:COG1196 303 diarleeRRRELEERLEELEEELAELEEELE-----ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE---AEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8812 SNLRDELNKLRGQHQTLQGELSELVAEMETGAQIVEQFQGLLKIVGGQFLELESELGSKTpvSRDDAELGSQLADMKDFL 8891
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8892 TRLGEKVETLKDLEQQASSLcnAGYVSDPELLKSQVEALSNQHASLTERATQRQSDvvANQHSIQHLTQALNLVWGDIDK 8971
Cdd:COG1196 453 ELEEEEEALLELLAELLEEA--ALLEAALAELLEELAEAAARLLLLLEAEADYEGF--LEGVKAALLLAGLRGLAGAVAV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8972 ASST--------LDAMGPAGGNV-----TTVKALQEELKGFVKSTMEPLQKQFESVSRQGQALIKTAVAGSNTTGLETDL 9038
Cdd:COG1196 529 LIGVeaayeaalEAALAAALQNIvveddEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9039 ESLAERWAGLVEKVAEHekNLDSALLRTGKFQdAMASLLDWLAETEELVAMQKAPSPEQRVVRAQLQEQKLVQKMVTDRT 9118
Cdd:COG1196 609 READARYYVLGDTLLGR--TLVAARLEAALRR-AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9119 PSMKAVQDSGNQLITGLDPAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQGLAGEFQDVLDplttwldaankrftA 9198
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE--------------E 751
|
570 580 590
....*....|....*....|....*....|
gi 1397727989 9199 LEPHSPDAEGIEHLIQELKKLQKEVNEHEP 9228
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGP 781
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
37-134 |
2.16e-03 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that 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-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 42.69 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNK---------HLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMR----FHKIQNVQIALDYL 103
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDERTINKKkltpFTIQENLNLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 104 RLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVI 135
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9992-10643 |
2.24e-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: 45.73 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9992 ESISKEAQRLMTSEGIAQAQGLKTKMEDMEKTWENIQAKSRAKQDMLEDGLREAQGFTGE----LQDILAKINDIEGQLI 10067
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHErkqvLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10068 ISKP-VGGLPETAKEQLEK---FMDVYAELEKLEPQVQSLNVMGEKLGGKSKGPALANLRQNLQHLNQRCDYIRSRACDR 10143
Cdd:TIGR00618 240 QSHAyLTQKREAQEEQLKKqqlLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10144 KKKLEDAEGMATNfhgeLNKFISWLTDTEKTLNNLQPVSRLVERVTSQ---IEDHRDLQKDISKHreaMVALEKMGTHLK 10220
Cdd:TIGR00618 320 MRSRAKLLMKRAA----HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVatsIREISCQQHTLTQH---IHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10221 YFSQkqdvvLIKNLLSSIQHRWEKIVSRSAERTrhLERGYKEAKQFNDTWKDLITWLIEAEKTLETETSVANEPDKIKAQ 10300
Cdd:TIGR00618 393 QKLQ-----SLCKELDILQREQATIDTRTSAFR--DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10301 iSKHKEFQRRLGAKQPVYDGVNKAGRLLKERcpsddvptiqamLTELKSHWNNVCSKSVDRQRKLEEgLLLSGQFTEALD 10380
Cdd:TIGR00618 466 -QSLKEREQQLQTKEQIHLQETRKKAVVLAR------------LLELQEEPCPLCGSCIHPNPARQD-IDNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10381 ALLDWLAKVEPALADdapVHGDIDTVNGFLDIHKAFQQELGARTTTIAFLQKSAKEIISRAEGDVCSLQSDLIELNAAWD 10460
Cdd:TIGR00618 532 RGEQTYAQLETSEED---VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10461 RVCKLSVSKQDRLEHAQRLAE------EFHKKAQQLLSWLADA------ERQLHYRGPIPDEEPLILQQMEEHKKFEESL 10528
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDvrlhlqQCSQELALKLTALHALqltltqERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10529 LRQEANLRETLNIGQDIMKRCHP---DSVPIMKQWLSVIRARWEELtalgRQRSARLSNGLTDLRH--NNVLLEDLLAWL 10603
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDL----AAREDALNQSLKELMHqaRTVLKARTEAHF 764
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1397727989 10604 NNAEMTLADVdrqtipQDMAIIQQLIKEHQDFQNEMSSRQ 10643
Cdd:TIGR00618 765 NNNEEVTAAL------QTGAELSHLAAEIQFFNRLREEDT 798
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
9590-9827 |
2.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9590 TKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKA----MEEDLEMRHNALESVK 9665
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ---AELEALQAEIDKLQAeiaeAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9666 NAA---------EELLRQAGDEQD-----EAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKfwdelhalnsS 9731
Cdd:COG3883 93 RALyrsggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA----------L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9732 LKDLQEALSSVDQpalepeAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQKNVDDAGASLAAISD 9811
Cdd:COG3883 163 KAELEAAKAELEA------QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|....*.
gi 1397727989 9812 QYSKRSQELESALAQA 9827
Cdd:COG3883 237 AAAAAAAASAAGAGAA 252
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
365-1001 |
2.91e-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: 45.34 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 365 RFMQAQQERDMALQAEIVRLER---LARMAEKIQRESKQAGESLhDLERQIQEAEVRGDKQHPYEAKHNCDAMDRALHTI 441
Cdd:TIGR00618 156 QFLKAKSKEKKELLMNLFPLDQytqLALMEFAKKKSLHGKAELL-TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 442 EENLR---AMFRDVQTLQDnhfpQSQQLYTRISELQSRVSSLRTRLYS-GVVQPLLSRA-----YVEEGRTVT----RRT 508
Cdd:TIGR00618 235 LQQTQqshAYLTQKREAQE----EQLKKQQLLKQLRARIEELRAQEAVlEETQERINRArkaapLAAHIKAVTqieqQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 509 EIMTE--VRLVDTNPAFRHVQDcldwieAQQQMIVGQDYSSDLQQVQEQLRTHRKTHQEVTTFRAQIDRCISDRKSLSAE 586
Cdd:TIGR00618 311 RIHTElqSKMRSRAKLLMKRAA------HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 587 EQKLyTQKLSSVEVAYSLLLNTSSRRLKFLESLSEF--LQG--ATAELTWLAEREEVEVTRDWVSKDLNLADLDDHHKNL 662
Cdd:TIGR00618 385 QQQK-TTLTQKLQSLCKELDILQREQATIDTRTSAFrdLQGqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 663 IRQvEARERHFnavQEKGGAMILDRHPAASMVEVLMASLQARWSWLLQlVTCLDAHLKHTIAHNQFFEEARHC--EQWMA 740
Cdd:TIGR00618 464 SAQ-SLKEREQ---QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC-GSCIHPNPARQDIDNPGPLTRRMQrgEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 741 RHTELLQNRFARDNIPMEQAELLIRELQELQEQLREYERRIASLTMSAPSIIPLSLRAQ---PVRSPLRLRTLCSCHLPE 817
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHALL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 818 VNLQRGEECFLISN-----SQLVKWRIKTLKGIETECPsvcllipppnQDAIDYANRLKRQHDHLSN------LWKSQHR 886
Cdd:TIGR00618 619 RKLQPEQDLQDVRLhlqqcSQELALKLTALHALQLTLT----------QERVREHALSIRVLPKELLasrqlaLQKMQSE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 887 KLRFSTIFATIEQIKAwdikKFLAMDPSQRENvWRALKEDGDKLIAESSNLQDRDSRHlQEAMTECQHIFQ---KLSTEA 963
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQT----LLRELETHIEEY-DREFNEIENASSSLGSDLAAREDAL-NQSLKELMHQARtvlKARTEA 762
|
650 660 670
....*....|....*....|....*....|....*...
gi 1397727989 964 AAKEGKRSMTAAQTmLQQLETANRELTICDQQISALVH 1001
Cdd:TIGR00618 763 HFNNNEEVTAALQT-GAELSHLAAEIQFFNRLREEDTH 799
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
9177-9279 |
3.04e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 41.15 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9177 EFQDVLDPLTTWLDAANKRFTAlEPHSPDAEGIEHLIQELKKLQKEVNEHEPAMKQLATAGKKLQDYcKGEDVIMIQLKI 9256
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSS-EDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDE-GHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1397727989 9257 DGVQKQNGELRSHIEDCLEQMEE 9279
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2188-2217 |
3.19e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.00 E-value: 3.19e-03
10 20 30
....*....|....*....|....*....|
gi 1397727989 2188 SITGIVHPKSGARLTVSQAIQNGILDQEKG 2217
Cdd:smart00250 9 AIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
9536-10193 |
3.26e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.07 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9536 EKAKVLKQ---EVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVR-TKVRDRSNSIDQAMQQSAEFTD 9611
Cdd:COG5022 842 LKAEVLIQkfgRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKlVNLELESEIIELKKSLSSDLIE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9612 KLE---NMLDTLTVTAEQVRSAEPISAQPDKLREQI---EENKAMEEDLEMRHNALESvknaaEELLRQAGDEQDEAVKD 9685
Cdd:COG5022 922 NLEfktELIARLKKLLNNIDLEEGPSIEYVKLPELNklhEVESKLKETSEEYEDLLKK-----STILVREGNKANSELKN 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9686 VRQKLEELTKLYKDIQERGRG---RQRALEEtLAVAEKFWDELHALNSSLKDLQEalssvdQPALEPEAIREQQEELEAL 9762
Cdd:COG5022 997 FKKELAELSKQYGALQESTKQlkeLPVEVAE-LQSASKIISSESTELSILKPLQK------LKGLLLLENNQLQARYKAL 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9763 KEDIEASQADFEEVQQTGDT--LLGMVGTTEQPEVQKNVDDAGASLAAISDQYSK--RSQELESALAQAVHF-QDQLMKL 9837
Cdd:COG5022 1070 KLRRENSLLDDKQLYQLESTenLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKlnLLQEISKFLSQLVNTlEPVFQKL 1149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9838 LVWLQEAEDEFsefePVASEFETIKKQWdelknFKTrvepkNVEIESLNQHVTELTKSSTPEQASVLREPMTQLNIRWNN 9917
Cdd:COG5022 1150 SVLQLELDGLF----WEANLEALPSPPP-----FAA-----LSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFS 1215
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9918 LLtNIGDRQRELQMALLTAGQFDHAHKELKNWMDLVDVtldeiTPVYGDPKLVEIelakLRIVQNDITAHQESVESISKE 9997
Cdd:COG5022 1216 GW-PRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT-----PASMSNEKLLSL----LNSIDNLLSSYKLEEEVLPAT 1285
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9998 AQRLMTSEGIAQAQGLKTKMEDMEktWENIQAKSRaKQDMLEDGLREAQgftgelqdilakINDIEGQLIISKPVGGLPE 10077
Cdd:COG5022 1286 INSLLQYINVGLFNALRTKASSLR--WKSATEVNY-NSEELDDWCREFE------------ISDVDEELEELIQAVKVLQ 1350
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10078 TAKEQLEKFMDVYAELEKLEP-QVQSLNVMGEKLGGKskgpalANLRQnlQHLNQrcdyIRSRACDRKKKLEDAEgmatn 10156
Cdd:COG5022 1351 LLKDDLNKLDELLDACYSLNPaEIQNLKSRYDPADKE------NNLPK--EILKK----IEALLIKQELQLSLEG----- 1413
|
650 660 670
....*....|....*....|....*....|....*..
gi 1397727989 10157 fHGELNKFISWLTDTEKTLNNLQPVSRLVERVTSQIE 10193
Cdd:COG5022 1414 -KDETEVHLSEIFSEEKSLISLDRNSIYKEEVLSSLS 1449
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4572-4596 |
3.59e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.85 E-value: 3.59e-03
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
35-141 |
3.71e-03 |
|
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-parvin 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: 409187 Cd Length: 130 Bit Score: 41.88 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 35 AVQKKTFTKWVNKHLMKAGLRIIDLFDDLRDGHNLISLLEVLAHDILPRERGHMR----FHKIQNVQIALDYLRLKGIRL 110
Cdd:cd21338 20 SVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQDGGLKK 99
|
90 100 110
....*....|....*....|....*....|.
gi 1397727989 111 VNIRSDEIVDGNPKLTLGLIWTIILHFQISD 141
Cdd:cd21338 100 PKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
9357-9852 |
3.79e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.84 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9357 EDIINRDNKRFDNLRDQIEKRAQKVQLarQRSSEVVNELGDLVDwfvDADSRLQNqqpIASDLDLLQQQLAEQKVMNEEI 9436
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEELNDKYRF--KKAKKALDEIEELLD---DIEEDIKQ---ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9437 NNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVD-TVSGSANERQSLLEQAvpfarhfHEahtelvvwlddve 9515
Cdd:pfam06160 127 KDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEElTESGDYLEAREVLEKL-------EE------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9516 pvlsELDVLSVDADQVKKQQEKAK-VLKQEVADRKPIVDRLNKTGTALVAMCGSKGAEQVQSMLDDDNRRMDNVRtkvrd 9594
Cdd:pfam06160 187 ----ETDALEELMEDIPPLYEELKtELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLE----- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9595 rsnsIDQAMQQSAEFTDKLENMLDTLT--VTAEQVrSAEPISAQPDKLREQIEENKAMEEDLE-------MRHNALESVK 9665
Cdd:pfam06160 258 ----LDEAEEALEEIEERIDQLYDLLEkeVDAKKY-VEKNLPEIEDYLEHAEEQNKELKEELErvqqsytLNENELERVR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9666 NAAEELlrqagDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQ- 9744
Cdd:pfam06160 333 GLEKQL-----EELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLe 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9745 -------------PALePEAIREQ----QEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQpEVQKNVDDAGasLA 9807
Cdd:pfam06160 408 lreikrlveksnlPGL-PESYLDYffdvSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYE-KTEELIDNAT--LA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1397727989 9808 AISDQYSKRSQELESALAQAvhfqdqlmkllvwLQEAEDEFSEFE 9852
Cdd:pfam06160 484 EQLIQYANRYRSSNPEVAEA-------------LTEAELLFRNYD 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
7874-8288 |
3.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7874 ELDIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKLEQT----NLWVHDGILQLDSKELSKLSS----- 7944
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllQLLPLYQELEALEAELAELPErleel 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7945 DDMKQQLEKLAREKHNRLRTIQEIQVAAEQLLQDPRTGEGEAVKNL---VSDLKKNLEAFDSLLAAKENEASDKEQQGAD 8021
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeLEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8022 FENAktialLWLSQMEARLDEFQPVAIDVGIVeqqkMELQPMLQEYEDYAPKIDEV------------NDLGNAYEAMIN 8089
Cdd:COG4717 232 LENE-----LEAAALEERLKEARLLLLIAAAL----LALLGLGGSLLSLILTIAGVlflvlgllallfLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8090 PGDRPISPIRRIG-RSRRLPGILSPRlrspspTFPTSPSTQRASPLSSESSGVSSRKSSADN----LLLDDLSEVQQQLL 8164
Cdd:COG4717 303 EAEELQALPALEElEEEELEELLAAL------GLPPDLSPEELLELLDRIEELQELLREAEEleeeLQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8165 ---------DITQRYEIVGER--LADRQQELQLMLTSIRTFMQDMQDILQWLDLKDHETDSAQPLPTNEKDAKKRLKEHE 8233
Cdd:COG4717 377 aeagvedeeELRAALEQAEEYqeLKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1397727989 8234 VFHREI--LSKEGLVEDIRKKaqdllktrhgvpgEEMLQQQLQELDDKWHGLRALSE 8288
Cdd:COG4717 457 ELEAELeqLEEDGELAELLQE-------------LEELKAELRELAEEWAALKLALE 500
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8793-9458 |
4.07e-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: 44.96 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8793 QLNNTETMLNSIEVDGGETSNLRDELNKLRGQHQTLQGELSE----------------LVAEMETGAQIVEQFQGLLKIV 8856
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVleetqerinrarkaapLAAHIKAVTQIEQQAQRIHTEL 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8857 GGQFLELESELGSKTPVSRDDAELGSQladmkdfltrlgekvetlKDLEQQASSLCNAgYVSDPELLKSQVEALSNQHaS 8936
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQ------------------RRLLQTLHSQEIH-IRDAHEVATSIREISCQQH-T 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8937 LTERATQRQSDvvanqhsIQHLTQALNLvwgdidkASSTLDAMGPAGGNVTTVKALQEELKG--FVKSTMEPLQKQFESV 9014
Cdd:TIGR00618 377 LTQHIHTLQQQ-------KTTLTQKLQS-------LCKELDILQREQATIDTRTSAFRDLQGqlAHAKKQQELQQRYAEL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9015 SRQgqaliktavAGSNTTGLETDLESLAERWAGLVEKVAEHEKNLDSALLRTGKFQDAMASLLDWLAETEELVAMQKApS 9094
Cdd:TIGR00618 443 CAA---------AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI-H 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9095 PEQRVVRAQLQE--QKLVQKMVTDRTPSMKAVQDSGNQLItgldpAERKHIESELQQLNSRWEALTKRVVDRTAILEEVQ 9172
Cdd:TIGR00618 513 PNPARQDIDNPGplTRRMQRGEQTYAQLETSEEDVYHQLT-----SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9173 GLAGEFQDVLDplttWLDAAN--KRFTALEPHSPDAEGiEHLIQELKKLQKEVN-EHEPAMKQLATAGkkLQDYCKGEDV 9249
Cdd:TIGR00618 588 NLQNITVRLQD----LTEKLSeaEDMLACEQHALLRKL-QPEQDLQDVRLHLQQcSQELALKLTALHA--LQLTLTQERV 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9250 IMIQLKIDGVQKQNGELRSHIEDCLEQMEEAL----PLAKHFQEAHAEFLSWASKVEPELRALELGVPDEETNIE---EL 9322
Cdd:TIGR00618 661 REHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAareDA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9323 ANQLTEEMQPLLDIINSEGAELAEVapgdAGLRVEDIINRDNKRFD---NLRDQIEKRAQKVQLARQRSSEVVNELGDlv 9399
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEAHFN----NNEEVTAALQTGAELSHlaaEIQFFNRLREEDTHLLKTLEAEIGQEIPS-- 814
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 9400 dwfvDADSRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSA 9458
Cdd:TIGR00618 815 ----DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8491-8786 |
4.36e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8491 RSKLTALEKDMNDTTRKLEICKAAVEEASQQAEKFEAdckelltwISEAANNLQESEplSSDLDIlreqmrqnRTLQQEL 8570
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE--------RREALQRLAEYS--WDEIDV--------ASAEREI 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8571 SLKEPEIRQLLEkgdklvkeSSPttEVRAIADKVGELQGEWTRLQQEVTVQDSRLTMAGSHAQQFTERLDKmamwLQMTE 8650
Cdd:COG4913 671 AELEAELERLDA--------SSD--DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE----LQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8651 EKLEKMKPEDVDQNtvvhkLKELqgVQNEMMKKSHD--RERLNSEGTSLVECVDSGKEAIKQQVAVINERWDAVNKALSE 8728
Cdd:COG4913 737 EAAEDLARLELRAL-----LEER--FAAALGDAVERelRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA 809
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1397727989 8729 RASHLEDLGQRLGE-VQDSLAEATSALNKWENKLAVHNSLGLSAKDPKHINRIKDLLED 8786
Cdd:COG4913 810 DLESLPEYLALLDRlEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
10804-10853 |
4.41e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 41.70 E-value: 4.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1397727989 10804 GRVTRKEFIEGIISSKFPTSklEMEKVADIFDKDGDGFINYKEFVAALRP 10853
Cdd:COG5126 84 GKISADEFRRLLTALGVSEE--EADELFARLDTDGDGKISFEEFVAAVRD 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
9265-9868 |
5.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9265 ELRSHIEDcLEQMEEALPLAK-------HFQEAHAEFLSWASKVEpELRALELGVPDE--ETNIEELANQLT---EEMQP 9332
Cdd:COG4913 229 ALVEHFDD-LERAHEALEDAReqiellePIRELAERYAAARERLA-ELEYLRAALRLWfaQRRLELLEAELEelrAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9333 LLDIINSEGAELAEVAPGDAGLRvEDIINRDNKRFDNLRDQI---EKRAQKVQLARQRSSEVVNELGDLVDW----FVDA 9405
Cdd:COG4913 307 LEAELERLEARLDALREELDELE-AQIRGNGGDRLEQLEREIerlERELEERERRRARLEALLAALGLPLPAsaeeFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9406 DSRLQNQQP-IASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSA--SKKLLSDSAMED-----NSAIRNKMDELK---- 9473
Cdd:COG4913 386 RAEAAALLEaLEEELEALEEALAEAEAALRDLRRELRELEAEIASleRRKSNIPARLLAlrdalAEALGLDEAELPfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9474 ---------QW---VDTVSGSAneRQSLLeqaVP------FARHFHEAHTELVVWLDDVEPVLSELDVLSVDADQV--K- 9532
Cdd:COG4913 466 lievrpeeeRWrgaIERVLGGF--ALTLL---VPpehyaaALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLagKl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9533 --KQQEKAKVLKQEVADRKPIV-----DRLNKTGTALVAMCGSKGAEQVQSMldDDNRRMD-------NVRTKV---RDR 9595
Cdd:COG4913 541 dfKPHPFRAWLEAELGRRFDYVcvdspEELRRHPRAITRAGQVKGNGTRHEK--DDRRRIRsryvlgfDNRAKLaalEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9596 SNSIDQAMQQSAEFTDKLENMLDTLT------VTAEQVRSAE----PISAQPDKLREQIEE----NKAMEEdLEMRHNAL 9661
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQerrealQRLAEYSWDEidvaSAEREIAELEAELERldasSDDLAA-LEEQLEEL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9662 ESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERGRGRQRALEETLavaEKFWDELHALNsSLKDLQEALSs 9741
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL---EERFAAALGDA-VERELRENLE- 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9742 vdqpalepEAIREQQEELEALKEDIEASQADFeevqqtgdtllgmvgtteQPEVQKNVDDAGASLAAISDqYSKRSQELE 9821
Cdd:COG4913 773 --------ERIDALRARLNRAEEELERAMRAF------------------NREWPAETADLDADLESLPE-YLALLDRLE 825
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1397727989 9822 -SALAQavhFQDQLMKLlvwLQEAEDEF-----SEFEpvaSEFETIKKQWDEL 9868
Cdd:COG4913 826 eDGLPE---YEERFKEL---LNENSIEFvadllSKLR---RAIREIKERIDPL 869
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
9638-9776 |
5.31e-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: 42.99 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9638 DKLREQIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEA---VKDVRQKLEELTKL---------YKDIQ---E 9702
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQlgnvrnnkeYEALQkeiE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397727989 9703 RGRGRQRALEETLAvaeKFWDELHALNSSLKDLQEALSSVDQpALEpEAIREQQEELEALKEDIEASQADFEEV 9776
Cdd:COG1579 100 SLKRRISDLEDEIL---ELMERIEELEEELAELEAELAELEA-ELE-EKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
9620-9827 |
5.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9620 LTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVK---NAAEELLRQAGDEQDEAVKDVRQKLEELTKL 9696
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNeeyNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9697 YKDIQERGR-----GRQRALEETLAVAE---KFWDELHALN----SSLKDLQEALSSVDQPALEPEAIREQQEELEALKE 9764
Cdd:COG3883 85 REELGERARalyrsGGSVSYLDVLLGSEsfsDFLDRLSALSkiadADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397727989 9765 DIEASQADFEEVQQTGDTLLgmvgTTEQPEVQKNVDDAGASLAAISDQYSKRSQELESALAQA 9827
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALL----AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| ElaB |
COG4575 |
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ... |
9648-9720 |
5.66e-03 |
|
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443632 [Multi-domain] Cd Length: 108 Bit Score: 40.70 E-value: 5.66e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1397727989 9648 KAMEEDLEmrhNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEEltkLYKDIQERGRGRQRALEETLAVAEK 9720
Cdd:COG4575 11 EDSKEDLE---ADLKALVDDLEELLKSTADDAGEKAAELREKAEA---ALDEARERLSEAEDAAVERAREAAD 77
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
37-134 |
5.95e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 40.59 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNKHL-----MKAGLRII----DLFDDLRDGHNLISLLEVLAHDILPRERGHMR-----FHKIQNVQIALDY 102
Cdd:cd21293 2 EKGSYVDHINRYLgddpfLKQFLPIDpstnDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1397727989 103 LRLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
9442-10097 |
6.18e-03 |
|
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: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9442 KARDTLSASKKLLSDSameDNSAIRNKMDELKQWVDTVSGSANERQSLLEQAVPFARHFHEAHTE--------LVVWLDD 9513
Cdd:pfam12128 279 EERQETSAELNQLLRT---LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIEtaaadqeqLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9514 VEPVLSELDVLSVDADQV--KKQQEKAKVLKQEVADRKPIVDRLNKT--GTALVAMCGSKGAEQVQSMLdddnrrmdnvR 9589
Cdd:pfam12128 356 LENLEERLKALTGKHQDVtaKYNRRRSKIKEQNNRDIAGIKDKLAKIreARDRQLAVAEDDLQALESEL----------R 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9590 TKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRSAEPISAQPDKLREQIEENKAMEEDLEmrhnalesvknAAE 9669
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ-----------SEL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9670 ELLRQAGDEQDEAVKDVRQKLEELtklykdiqergRGRQRALEETLAVAEKfwDELHALNSSLKDLQEALSSVDQPALep 9749
Cdd:pfam12128 495 RQARKRRDQASEALRQASRRLEER-----------QSALDELELQLFPQAG--TLLHFLRKEAPDWEQSIGKVISPEL-- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9750 eaireqqeeleALKEDIEASQADFEEVQqtGDTLLGMVGTTEQPEVQknvddagaSLAAISDQYSKRSQELESALAQAVH 9829
Cdd:pfam12128 560 -----------LHRTDLDPEVWDGSVGG--ELNLYGVKLDLKRIDVP--------EWAASEEELRERLDKAEEALQSARE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9830 FQDQLMKLLVWLQEAEDEfsefepvASEFETIKKQwdELKNFKTRVEPKNVEIESLNQHVTELTKS---STPEQASVLRE 9906
Cdd:pfam12128 619 KQAAAEEQLVQANGELEK-------ASREETFART--ALKNARLDLRRLFDEKQSEKDKKNKALAErkdSANERLNSLEA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9907 PMTQLNIRWNNLLTNIGDRQRELQMALLTAgqfdhahkelknWMDLVDVTLDEITpvygdpkLVEIELAKLRivqndiTA 9986
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREARTEKQAY------------WQVVEGALDAQLA-------LLKAAIAARR------SG 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9987 HQESVESISKEAQRLMTSEGI--AQAQGLKTKMEDMEKTWENIqAKSRAKQDMLEDGLREA-----QGFTGELQDILAKI 10059
Cdd:pfam12128 745 AKAELKALETWYKRDLASLGVdpDVIAKLKREIRTLERKIERI-AVRRQEVLRYFDWYQETwlqrrPRLATQLSNIERAI 823
|
650 660 670
....*....|....*....|....*....|....*...
gi 1397727989 10060 NDIEGQLiiskpvGGLPETAKEQLEKFMDVYAELEKLE 10097
Cdd:pfam12128 824 SELQQQL------ARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
9529-9747 |
6.32e-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: 43.60 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9529 DQVKKQ-QEKAKVLKQEVADRKPIVDRLNKTGTALVamcgskgaeQVQSMLDDDNRRMDNVRTKVRDRSNSIDQAMQQSA 9607
Cdd:COG4942 30 EQLQQEiAELEKELAALKKEEKALLKQLAALERRIA---------ALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9608 EFTDKLENMLDTLTVTAEQ---------------VRSAEPISAQPDKLREQIEENKAMEEDLEMRHNALESVKNAAEELL 9672
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplalllspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 9673 RQAGDEQDEAVKDVRQKLEELTKLYKDIQErgrgRQRALEETLAVAEKFWDELHALNSSLKDLQEALSSVDQPAL 9747
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAE----LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7728-8018 |
6.41e-03 |
|
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: 44.29 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7728 LDRLKSLSMDALSQKLLLDEMQK-RGQDLTNSLsgQAAEQQ------QVAKLQSTMNDLSVRYSTLTKDINSHVTQLQAA 7800
Cdd:TIGR02169 200 LERLRREREKAERYQALLKEKREyEGYELLKEK--EALERQkeaierQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7801 vthsqditqamNELVSWMDSAEQV-VTTQL-----PISLRRPELNAQLQSFSAVDADVTNHQSALDAVKALANELvktce 7874
Cdd:TIGR02169 278 -----------NKKIKDLGEEEQLrVKEKIgeleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL----- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7875 ldiARAVEQ---RLTSLDEKFSSLQAKCRQRDRDLEEVDSSLRE-------FQEKLEQTNLWVHDGILQLDSK--ELSKL 7942
Cdd:TIGR02169 342 ---EREIEEerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdelkdYREKLEKLKREINELKRELDRLqeELQRL 418
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397727989 7943 SSD--DMKQQLEKLaREKHNRLRTiqEIQVAAEQLLQDprTGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQ 8018
Cdd:TIGR02169 419 SEElaDLNAAIAGI-EAKINELEE--EKEDKALEIKKQ--EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9750-10046 |
6.52e-03 |
|
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: 44.29 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9750 EAIREQQEELEALKEDIEASQADFEEVQQTGDTLLGMVGTTEQ-PEVQKNVDDAGASLaaISDQYSKRSQELESALAQAV 9828
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKREYEGYE--LLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9829 HFQDQLMKLLVWLQEAEDEFSEFEPVASEFET--IKKQWDELKNFKTRVEPKNVEIESLNQHV----------------T 9890
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEAEIASLERSIaekereledaeerlakL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9891 ELTKSSTPEQASVLREPMTQLNIRWNNLLTNIGDRQRELQMALLTAGQFDHAHKELKNWMDLVDVTLD----EITPVYGD 9966
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkrEINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9967 PKLVEIELAKLRIVQNDITAHQESVESISKEAQRLMTS--EGIAQAQG-LKTKMEDMEKTWENIQAKsRAKQDMLEDGLR 10043
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDkaLEIKKQEWkLEQLAADLSKYEQELYDL-KEEYDRVEKELS 486
|
...
gi 1397727989 10044 EAQ 10046
Cdd:TIGR02169 487 KLQ 489
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
37-134 |
6.52e-03 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes 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. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 41.50 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 37 QKKTFTKWVNKHL-----------MKAGLRiiDLFDDLRDGHNLISLLEVLAHDILPrERGHMR-----FHKIQNVQIAL 100
Cdd:cd21292 25 EKVAFVNWINKNLgddpdckhllpMDPNTD--DLFEKVKDGILLCKMINLSVPDTID-ERAINKkkltvFTIHENLTLAL 101
|
90 100 110
....*....|....*....|....*....|....
gi 1397727989 101 DYLRLKGIRLVNIRSDEIVDGNPKLTLGLIWTII 134
Cdd:cd21292 102 NSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
7795-8039 |
6.64e-03 |
|
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: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7795 TQLQAAVTHSQDITQAMNELVswmDSAEQVVTtqlpisLRRpeLNAQLQSFSAVDADVTNHQSALDAVKALANELvktce 7874
Cdd:COG4913 225 EAADALVEHFDDLERAHEALE---DAREQIEL------LEP--IRELAERYAAARERLAELEYLRAALRLWFAQR----- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7875 ldIARAVEQRLTSLDEKFSSLQAKCRQRDRDLEEVDSSLREFQEKleqtnlwvhdgILQLDSKELSKLssddmKQQLEKL 7954
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-----------IRGNGGDRLEQL-----EREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 7955 AREKHNRLRTIQEIQVAAEQL-LQDPrtGEGEAVKNLVSDLKKNLEAFDSLLAAKENEASDKEQQGADFENAKTIALLWL 8033
Cdd:COG4913 351 ERELEERERRRARLEALLAALgLPLP--ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
....*.
gi 1397727989 8034 SQMEAR 8039
Cdd:COG4913 429 ASLERR 434
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
9324-9930 |
7.63e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9324 NQLTEEMQPLLDIINSEGAELAEVApgdaglRVEDIINRDNKRFDNLRDQIEKRAQKVQLARQRSSEVVNELGDLVDWFV 9403
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNID------YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9404 DADSRLQNQQPIASDLDLLQQQLAEQKVMNEEINNQKVKARDTLSASKKLLSDSAMEDNSAIRNKMDELKQWVDtvsgsa 9483
Cdd:PRK01156 236 NLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEN------ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9484 neRQSLLEQAVPFARHFHEAHtelvvwlddvepvlSELDVLSVDADQVKKQQEKAKVLKQEVADRKPIVDRLNKTgtalv 9563
Cdd:PRK01156 310 --KKQILSNIDAEINKYHAII--------------KKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSY----- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9564 amcgSKGAEQVqsmldddNRRMDNVRTKVRDRSNSIDQAMQQSAEFTDKLENMLDTLTVTAEQVRS-AEPISAQPDKLRE 9642
Cdd:PRK01156 369 ----LKSIESL-------KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSkVSSLNQRIRALRE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9643 QIEENKAMEEDLEMRHNALESVKNAAEELLRQAGDEQDEAVKDVRQKLEELTKLYKDIQERgRGRQRALEETLAVAE--- 9719
Cdd:PRK01156 438 NLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK-IVDLKKRKEYLESEEink 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9720 --KFWDELHALNSSLKDLQEALSSVDQPALEPEAIREQQEELEAlkEDIEASQADFEEVQQTGDTLLGMVGTTEQPEVQK 9797
Cdd:PRK01156 517 siNEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL--EDLDSKRTSWLNALAVISLIDIETNRSRSNEIKK 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9798 NVDDAgaslaaisdqySKRSQELESALAQAVHFQDQLMKllvwlqEAEDEFSEFEPVASEFETIKKQWDEL----KNFKT 9873
Cdd:PRK01156 595 QLNDL-----------ESRLQEIEIGFPDDKSYIDKSIR------EIENEANNLNNKYNEIQENKILIEKLrgkiDNYKK 657
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1397727989 9874 RV------EPKNVEIES-LNQHVTELTKSSTPEQAS------------VLREPMTQLNIRwnnlltnIGDRQRELQ 9930
Cdd:PRK01156 658 QIaeidsiIPDLKEITSrINDIEDNLKKSRKALDDAkanrarlestieILRTRINELSDR-------INDINETLE 726
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
9607-9780 |
8.87e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9607 AEFTDKLENMLDTLTVTAEQVRSAEpisAQPDKLREQIEENKAMEEDLEMRHNAL----ESVKNAAEELLRQAGDEQDEA 9682
Cdd:pfam04012 11 ANIHEGLDKAEDPEKMLEQAIRDMQ---SELVKARQALAQTIARQKQLERRLEQQteqaKKLEEKAQAALTKGNEELARE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 9683 VKDVRQKLEELTKLYKDIQERGR----GRQRALEETLAVAEKFWDELHALNSSLK------DLQEALSSVDQPALEP--E 9750
Cdd:pfam04012 88 ALAEKKSLEKQAEALETQLAQQRsaveQLRKQLAALETKIQQLKAKKNLLKARLKaakaqeAVQTSLGSLSTSSATDsfE 167
|
170 180 190
....*....|....*....|....*....|...
gi 1397727989 9751 AIREQQEELEA---LKEDIEASQADFEEVQQTG 9780
Cdd:pfam04012 168 RIEEKIEEREAradAAAELASAVDLDAKLEQAG 200
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
8523-9053 |
9.88e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8523 EKFEADCKELLT-WISEAANNLQESEPLSSDLDILREQMRQNRTLQQELSLKEPEIRQLlekgdklvkesspttevraiA 8601
Cdd:COG4717 49 ERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--------------------E 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8602 DKVGELQGEWTRLQQEVTVQDSRLTMagshaQQFTERLDKMamwlqmtEEKLEKMKpedvdqntvvHKLKELQGVQNEMM 8681
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQEL-----EALEAELAEL-------PERLEELE----------ERLEELRELEEELE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8682 KKSHDRERLNSEgtsLVECVDSGKEAIKQQVAVINERWDAvnkaLSERASHLEdlgQRLGEVQDSLAEATSALNKWENKL 8761
Cdd:COG4717 167 ELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEE----LQQRLAELE---EELEEAQEELEELEEELEQLENEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8762 avhnslgLSAKDPKHINRIKDLLEDT-------GWLASQLNNTETMLNSIEVDGGETSNLRDELNKLRGQHQTLQGELSE 8834
Cdd:COG4717 237 -------EAAALEERLKEARLLLLIAaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8835 LVAEMETGAQIVEqfqgllkivggqflELESELGSKTPVSRDDA-ELGSQLADMKDFLTRLGEKVETLK--DLEQQASSL 8911
Cdd:COG4717 310 LPALEELEEEELE--------------ELLAALGLPPDLSPEELlELLDRIEELQELLREAEELEEELQleELEQEIAAL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397727989 8912 CNAGYVSDPELLKSQVEALSNQHAsLTERatqrqsdvvanqhsIQHLTQALNLVWGDIDKASSTLDAmgpaggnvttvKA 8991
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE-LKEE--------------LEELEEQLEELLGELEELLEALDE-----------EE 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397727989 8992 LQEELkGFVKSTMEPLQKQFESVSRQGQAL---IKTAVAGSNTTGLETDLESLAERWAGLVEKVA 9053
Cdd:COG4717 430 LEEEL-EELEEELEELEEELEELREELAELeaeLEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| |
