|
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 ... |
210-314 |
5.63e-75 |
|
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: 245.00 E-value: 5.63e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 210 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 289
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1389908274 290 RNDDIADGNPKLTLGLIWTIILHFQ 314
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
207-325 |
2.17e-73 |
|
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: 241.08 E-value: 2.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 207 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 286
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908274 287 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 325
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
199-323 |
3.36e-70 |
|
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: 232.18 E-value: 3.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 199 ERAVIRIADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDF 278
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1389908274 279 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 323
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
327-432 |
4.22e-67 |
|
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: 222.59 E-value: 4.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1389908274 407 PEDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
328-432 |
7.10e-65 |
|
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: 216.10 E-value: 7.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
207-324 |
1.21e-61 |
|
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: 207.58 E-value: 1.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 207 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 286
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908274 287 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 324
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
328-432 |
1.74e-57 |
|
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: 194.82 E-value: 1.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLLDP 407
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
326-432 |
5.75e-51 |
|
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: 176.39 E-value: 5.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 326 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLL 405
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1389908274 406 DPEDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
212-315 |
1.16e-50 |
|
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: 175.65 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 290
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1389908274 291 NDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
199-311 |
4.44e-50 |
|
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: 174.48 E-value: 4.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 199 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 276
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 277 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
328-428 |
3.66e-46 |
|
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: 162.58 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
199-311 |
4.46e-45 |
|
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: 160.15 E-value: 4.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 199 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 276
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 277 DFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21193 82 AFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
208-315 |
1.28e-44 |
|
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: 158.69 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 283
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 284 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
328-428 |
1.63e-44 |
|
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: 157.94 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
206-428 |
6.09e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 169.35 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 206 ADERDRVQKKTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 282
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 283 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGKL 361
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 362 FSAIIHKHRPALIDMNQVYRQSNQE--NLEQAFSVAERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 428
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
205-311 |
7.73e-43 |
|
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: 154.41 E-value: 7.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 205 IADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQ 283
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1389908274 284 VKLVNIRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
199-311 |
7.66e-42 |
|
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: 151.36 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 199 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 276
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 277 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
208-315 |
2.82e-41 |
|
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: 148.87 E-value: 2.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 283
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 284 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1075-1151 |
8.85e-40 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 143.51 E-value: 8.85e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1075 SWQYLMRDIHIIKTWNISMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNKANQHYNTMVTS 1151
Cdd:pfam18373 2 SWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
315-428 |
1.51e-39 |
|
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: 144.04 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 315 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 394
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 395 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
327-432 |
3.50e-39 |
|
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: 142.84 E-value: 3.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1389908274 407 PEDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
328-428 |
6.43e-39 |
|
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: 142.45 E-value: 6.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
212-313 |
1.89e-38 |
|
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: 140.61 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 289
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1389908274 290 RNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
208-315 |
2.56e-38 |
|
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: 140.35 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 285
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908274 286 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
210-311 |
5.77e-38 |
|
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: 139.06 E-value: 5.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 210 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 288
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1389908274 289 IRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
324-428 |
1.29e-37 |
|
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: 138.65 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 324 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 403
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1389908274 404 LLDPEDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
327-428 |
2.50e-37 |
|
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: 137.69 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1389908274 407 PEDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
331-432 |
1.23e-36 |
|
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: 135.25 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908274 410 VDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1497-2310 |
3.36e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.99 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1497 VNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKE-EERRKMAEIQAELDKQKQMAEAHAKSVAKAEqealelkm 1575
Cdd:PTZ00121 1060 AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKaEEAKKTETGKAEEARKAEEAKKKAEDARKAE-------- 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1576 kmkeEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAEL 1655
Cdd:PTZ00121 1132 ----EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1656 QELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQA 1735
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1736 EEEKIRQIRVVEEVAQksaATQLQTKAmsfsEQTTKLEESLKKEQgnvlKLQEEADKLKKQQKEANTAREEAEQELEiwr 1815
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKK---ADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAE--- 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1816 QKANEALRLRLQAEEEAQKKSHAQEEAEkqklEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEC 1895
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1896 IRlKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLE-----DELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLE 1970
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAK----KKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1971 SEALKMKqlADEAARmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKT-----EAEMALKAKEAENE 2044
Cdd:PTZ00121 1505 AAEAKKK--ADEAKK----AEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2045 RLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS-----ELGRQKNIVEETLKQKKVVEEEIHiiKINFHKASK 2119
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAE 1656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2120 EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEE----VERLK 2195
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAK 1736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2196 KKAEDANKQKEKAEKEAEKqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQE--------------KLRDEFENAKKL- 2260
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEEldeedekrrmevdkKIKDIFDNFANIi 1811
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2261 -------------AQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2310
Cdd:PTZ00121 1812 eggkegnlvindsKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
207-315 |
1.12e-35 |
|
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: 133.12 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 207 DERDRVQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 285
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908274 286 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
312-428 |
2.56e-35 |
|
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: 132.87 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 312 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQA 391
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908274 392 FSVAERELGVTKLLDPEDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1664-2580 |
3.47e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1664 EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDElkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEekirqI 1743
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADE------ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED-----A 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1744 RVVEEVAQksaatqlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ--KEANTAR--EEAEQELEIwrQKAN 1819
Cdd:PTZ00121 1128 RKAEEARK--------------AEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKkaEAARKAEEV--RKAE 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1820 EalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEaaLKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLK 1899
Cdd:PTZ00121 1192 E-----LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA--VKKAEEAKKDAEEAKK-----AEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1900 ADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQleDELNKVRsEMDSLLQMKINAEKASMVNTEKSKqlleseALKMKQL 1979
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKKAE-EKKKADEAKKKAEEAKKADEAKKK------AEEAKKK 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1980 ADEAARMrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEN--ERLKRQAEEEAYQR 2057
Cdd:PTZ00121 1331 ADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKA 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2058 KLLEDQAAQHKQDIEEKITQLQTSSDSELgrqkniveetlkqKKVVEEeihiikinfhkasKEKADlesELKKLKGIADE 2137
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEA-------------KKKAEE-------------AKKAD---EAKKKAEEAKK 1458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2138 TQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQ 2215
Cdd:PTZ00121 1459 AEEAKKKAEEakKADEAKK----------------------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2216 VVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENE 2295
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2296 AAKQAkaqnDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvl 2375
Cdd:PTZ00121 1597 VMKLY----EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--- 1669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2376 lDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLaeEAEKMKSLAEEAGRLS 2455
Cdd:PTZ00121 1670 -AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKA 1746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2456 VEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaEKLQKQKDQAQETAKRLQEDKQQIQqrldketegf 2535
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANII---------- 1811
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1389908274 2536 qkslEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2580
Cdd:PTZ00121 1812 ----EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1711-2695 |
8.17e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.37 E-value: 8.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1711 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTkamsFSEQTTKLEESLKKEQGNVlklqEEA 1790
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA----TEEAFGKAEEAKKTETGKA----EEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1791 DKLKKQQKEANTAR--EEAEQELEIwrQKANEALRlrlqaEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKE 1868
Cdd:PTZ00121 1115 RKAEEAKKKAEDARkaEEARKAEDA--RKAEEARK-----AEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1869 NAEKELDKqrkfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1948
Cdd:PTZ00121 1188 RKAEELRK----AEDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1949 QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV--AEEAKKQrqiAEEeaARQRSEAEKILKEklaAINEAT 2026
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkADEAKKK---AEE--AKKADEAKKKAEE---AKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2027 RLKTEAEMALKAKEAenerlkRQAEEEAYQRKLledQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEE 2106
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2107 ihiikinfhkasKEKADlesELKKLKGIADETQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritAAEEeaarqc 2184
Cdd:PTZ00121 1404 ------------KKKAD---ELKKAAAAKKKADEAKKKAEEkkKADEAKK--------------------KAEE------ 1442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2185 kaaQEEVERLKKKAEDANKqkekaekeaekqvvlAKEAAQKctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEa 2264
Cdd:PTZ00121 1443 ---AKKADEAKKKAEEAKK---------------AEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE- 1501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2265 ekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKE 2344
Cdd:PTZ00121 1502 -------------AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2345 AEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRR 2424
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2425 LMQKDKDSTQKLLAEEAEKMKslAEEAGRLSVE---AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAE 2501
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKK--AEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2502 KlqkQKDQAQETAKRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRV--KELSLAQTKAEDEAKKFKK 2579
Cdd:PTZ00121 1727 E---NKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QADEVKAQLQRTEKHTTEIVVQKLETQrLQSTREADDLKSAIADleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAE 2659
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLE---------------EADAFEKHKFNKNNENGEDGN 1865
|
970 980 990
....*....|....*....|....*....|....*.
gi 1389908274 2660 LQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKK 2695
Cdd:PTZ00121 1866 KEADFNKEKDLKEDDEEEIE-EADEIEKIDKDDIER 1900
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
199-311 |
1.15e-34 |
|
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: 131.70 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 199 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 276
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 277 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 311
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1920-2784 |
1.74e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.21 E-value: 1.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1920 KNEVNSTEKQR---KQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQllESEALKMKQLADEAARMRSV------- 1989
Cdd:PTZ00121 1063 KAHVGQDEGLKpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1990 -AEEAKKQRQIAEEEAARQRSEAEKI---LKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 2065
Cdd:PTZ00121 1141 kAEEARKAEDAKRVEIARKAEDARKAeeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2066 QHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKlkgiADETQKS-KLK 2144
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKAdEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2145 AEEEAEKLKKLAAEEERRRKEAEEKVKritaaEEEAARQCKAAQEEVERLKKKAEdANKQKEKAEKEAEKQVVLAKEAAQ 2224
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKK-----AEEAKKKADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2225 KCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlLRQKAEE---AEKQKKAAEnEAAKQAK 2301
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEkkkADEAKKKAE-EAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2302 AQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEltvvklqldetdkqkvlldQELQ 2381
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-------------------AEAK 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2382 RVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAGRLSVEAEET 2461
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEE 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2462 ARQRQiaesnlaeqralaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslea 2541
Cdd:PTZ00121 1586 AKKAE-------------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-------- 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2542 ERKRQLEASAEAEKLKLRVKELSlaqTKAEDEakkfKKQADEVKAQlQRTEKHTTEIVVQKLETQrlqstREADDLKSAI 2621
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEEAKKA-EEDEKKAAEALKKEAEEA-----KKAEELKKKE 1711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2622 ADLEeerkklkkeaeelqRKSKEMANAqqEQIEQQKAElqqsfltekglLLKREKEVEGEKKRFEKQLEDEMKKAKALKD 2701
Cdd:PTZ00121 1712 AEEK--------------KKAEELKKA--EEENKIKAE-----------EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2702 EQErqrKLMEEERKKLQAIMDEAVrKQKEAEEEMKNKQREMDVLDKKRLEQEKQlAEENKKLREQLQTFEISSKTVSQTK 2781
Cdd:PTZ00121 1765 EEE---KKAEEIRKEKEAVIEEEL-DEEDEKRRMEVDKKIKDIFDNFANIIEGG-KEGNLVINDSKEMEDSAIKEVADSK 1839
|
...
gi 1389908274 2782 ESQ 2784
Cdd:PTZ00121 1840 NMQ 1842
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
328-428 |
2.14e-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: 129.06 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLY 428
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
327-425 |
1.15e-33 |
|
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: 127.15 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1389908274 407 PEDVDVPHPDEKSIITYVS 425
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1920-2819 |
2.43e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 143.36 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1920 KNEVNSTEKQRKQL--EDELNKVRSEMDSLLQMKINAEKASmvnTEKSKQLLESEALKMKQLADEAARMRSV---AEEAK 1994
Cdd:PTZ00121 1052 IDGNHEGKAEAKAHvgQDEGLKPSYKDFDFDAKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDAR 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1995 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIE-- 2072
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaa 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2073 ---EKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEA 2149
Cdd:PTZ00121 1206 rkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2150 EKLKKLAAeeerrrkeaeekvkritAAEEEAARQCKAAQE--EVERLKKKAEDANKQKEKAEKeaekqvvlAKEAAQKCT 2227
Cdd:PTZ00121 1278 RKADELKK-----------------AEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKK--------AEEAKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2228 AAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEE---AEKQKKAAENEAAKQAKAQN 2304
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2305 DTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKeltvvklqldetdkqkvlldQELQRVK 2384
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--------------------AEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2385 GEVNDAFKQKSQVEvelarvriqmeelvKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAgRLSVEAEETARQ 2464
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--------------EAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEA 1533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2465 RQIAESNLAEQRALAEKILKekmqaiQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERK 2544
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKK------AEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2545 RQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIAD 2623
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2624 LEEERKklkkeaeelQRKSKEMANAQQEQIEQQKAELQQsflteKGLLLKREKEVEGEK-KRFEKQLEDEMKKAKALKDE 2702
Cdd:PTZ00121 1687 EKKAAE---------ALKKEAEEAKKAEELKKKEAEEKK-----KAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKD 1752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2703 QERQRKLmeEERKKLQAIMDEAVRKQKEAEEEmknkqREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2782
Cdd:PTZ00121 1753 EEEKKKI--AHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
890 900 910
....*....|....*....|....*....|....*..
gi 1389908274 2783 SQTVSVEKLVAVttvgTSKGVLNGSTEVDGVKKEGDS 2819
Cdd:PTZ00121 1826 EMEDSAIKEVAD----SKNMQLEEADAFEKHKFNKNN 1858
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
327-425 |
8.34e-33 |
|
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: 124.56 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1389908274 407 PEDVDVPHPDEKSIITYVS 425
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
315-428 |
1.45e-32 |
|
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: 124.18 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 315 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 394
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 395 AERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 428
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
211-316 |
2.14e-32 |
|
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: 124.10 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 287
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1519-2771 |
3.06e-32 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 139.58 E-value: 3.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEEERRKMAEIQAELdkqkqmaeaHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNI 1598
Cdd:NF041483 91 DAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1599 QQELQHLKSLSDQEIksknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAaEAEKLRKAAQDEAer 1678
Cdd:NF041483 162 ESQARRLLDESRAEA-------EQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK-DAERLLNAASTQA-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1679 lrkqvaeetQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKirqirVVEEvAQKSAATQL 1758
Cdd:NF041483 232 ---------QEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEK-----VVAE-AKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1759 QTkAMSFSEQTTKleesLKKEQgnVLKLQEEAdklkkqQKEANTAREEAEQ-------ELEIWRQKANEALRlRLQAEEE 1831
Cdd:NF041483 297 AS-AESANEQRTR----TAKEE--IARLVGEA------TKEAEALKAEAEQaladaraEAEKLVAEAAEKAR-TVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1832 AQKKSHAQEEAEKQKLEAERDAKK--RGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSA---------------EQE 1894
Cdd:NF041483 363 AAQLAKAARTAEEVLTKASEDAKAttRAAAEEAERIRRE-AEAEADRLRGEAADQAEQLKGAakddtkeyraktvelQEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1895 CIRLKADfehAEQQRGLLDNELQRLKNE-----VNSTEKQRKQLEDELNKVRSEMDSLLQ-MKINAEKASMVNTEKSKQL 1968
Cdd:NF041483 442 ARRLRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTL 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1969 LESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKTEAEMALKAKE------ 2040
Cdd:NF041483 519 RRQAEETLERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealada 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2041 -AENERLKRQAEEEAYQrklLEDQAAqhkqdieEKITQLQTSSDSElgrqknivEETLKQKKVVEeeihiikinfhkASK 2119
Cdd:NF041483 599 rAEAERIRREAAEETER---LRTEAA-------ERIRTLQAQAEQE--------AERLRTEAAAD------------ASA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2120 EKADLESELKKLKG-IADETQKSKLKAEEEAEKLKklAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQE--------- 2189
Cdd:NF041483 649 ARAEGENVAVRLRSeAAAEAERLKSEAQESADRVR--AEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraea 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2190 --EVERLKKKAEDANKQKEKAEKEAEKQVV-LAKEAAQKCT----AAEQKAQDVlsknkedvlaqeklRDEFENAKKLAQ 2262
Cdd:NF041483 727 dqERERAREQSEELLASARKRVEEAQAEAQrLVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2263 EAEKAkekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRkeaeeeaarrAAAEAAALKQKQQADAemskhk 2342
Cdd:NF041483 793 EEIAG----------LRSAAEHAAERTRTEAQEEADRVRSDAYAERER----------ASEDANRLRREAQEET------ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2343 kEAEQALQQKSqvekeltvVKLQLDETDKQKVLLDQELQRVKGEVNDAFkqkSQVEVELARVRIQM-EELVKLKLKIEEE 2421
Cdd:NF041483 847 -EAAKALAERT--------VSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQDAARTRADArEDANRIRSDAAAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2422 NRRLMQKDKDSTQKLLAE---EAEKMKSLA-EEAGRLSVEAEETARQRQIAESNLAEQ-RALAEKILKekmQAIQEATKL 2496
Cdd:NF041483 915 ADRLIGEATSEAERLTAEaraEAERLRDEArAEAERVRADAAAQAEQLIAEATGEAERlRAEAAETVG---SAQQHAERI 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2497 KAEAEKLqkqKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslEAERKRQLEASAEAEKLKLRV-----KELSLAQTKAE 2571
Cdd:NF041483 992 RTEAERV---KAEAAAEAERLRTEAREEADRTLDEAR------KDANKRRSEAAEQADTLITEAaaeadQLTAKAQEEAL 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2572 DEAKKFKKQADE-VKAQLQRTEKHTTEIVVQKlETQRLQSTREADDL-------KSAIADLEEERKKLKKEA-----EEL 2638
Cdd:NF041483 1063 RTTTEAEAQADTmVGAARKEAERIVAEATVEG-NSLVEKARTDADELlvgarrdATAIRERAEELRDRITGEieelhERA 1141
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 QRKSKEMANAQQEQIEQ--QKAELQQSFLTEKGLLLKREKEVEGEKKRFekqleDEMKKAKALKDEQERQRKLMEEERKK 2716
Cdd:NF041483 1142 RRESAEQMKSAGERCDAlvKAAEEQLAEAEAKAKELVSDANSEASKVRI-----AAVKKAEGLLKEAEQKKAELVREAEK 1216
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2717 LQAimdEAVRkqkEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLrEQLQTFE 2771
Cdd:NF041483 1217 IKA---EAEA---EAKRTVEEGKRELDVLVRRREDINAEISRVQDVL-EALESFE 1264
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
333-428 |
9.37e-32 |
|
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: 121.69 E-value: 9.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 333 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 411
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1389908274 412 VPHPDEKSIITYVSSLY 428
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
212-315 |
1.05e-31 |
|
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: 121.63 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 289
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1389908274 290 RNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
331-433 |
2.09e-31 |
|
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: 120.80 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-ENLEQAFSVAERELGVTKLLDPE 408
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1389908274 409 DVDVPHPDEKSIITYVSSLYDVMPR 433
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
212-315 |
2.26e-31 |
|
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: 120.50 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 290
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1389908274 291 NDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
208-317 |
7.57e-31 |
|
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: 119.22 E-value: 7.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 283
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1389908274 284 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 317
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1523-2154 |
1.55e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.52 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1523 RLED--DEKAS--EKLKEEER--RKMAEIQAELDKQKQMAEAHAKSVAKAEQEALElkmkmkEEASKRQDVAADAEKQKQ 1596
Cdd:COG1196 190 RLEDilGELERqlEPLERQAEkaERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1597 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIeeeihiiriqlekttahkaksEAELQELRDRAAEAEKLRKAAQDEA 1676
Cdd:COG1196 264 ELEAELEELR----LELEELELELEEAQAEEYEL---------------------LAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1677 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQkykmQAEEAERRMKQAEEEKIRQIRvveevAQKSAAT 1756
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELE-----ELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1757 QLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKS 1836
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1837 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNEL 1916
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1917 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1996
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA----ALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1997 RQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 2076
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2077 QLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhkASKEKADLESELKKLKGIADETQksklkAEEEAEKLKK 2154
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEELLEEEALEELPEPPDLEE-----LERELERLER 774
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
331-432 |
1.66e-30 |
|
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: 117.75 E-value: 1.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908274 410 VDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1494-2073 |
9.17e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.83 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALE 1572
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1573 LKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSE 1652
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM 1732
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1733 KQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEANTAREEAEQELE 1812
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1813 IWRQKANEALRLRLQAEEEAQkksHAQEEAEKQKLEAERDAKKRGKAEEAALkqkeNAEKELDKQRKFAEQIAQQKLSAE 1892
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNI---VVEDDEVAAAAIEYLKAAKAGRATFLPL----DKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1893 QECIRLKADFEHAEQQRGLLDNELQRLKNEvnSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESE 1972
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1973 ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEE 2052
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|.
gi 1389908274 2053 EAYQRKLLEDQAAQHKQDIEE 2073
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
211-313 |
9.60e-30 |
|
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: 116.04 E-value: 9.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
331-430 |
3.51e-29 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 114.30 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED- 409
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1389908274 410 VDVPHPDEKSIITYVSSLYDV 430
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1281-2147 |
7.26e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 125.64 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1281 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSE-----AEADQVMFDRLQDDLRKAttvhDKMTRIHSERDADLE 1355
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkaEEARKAEDAKRVEIARKA----EDARKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1356 HYRQLVNGLLERWQAvfaqielRLRELDLLGRHMNSYRDSYEwlIRWLTEARQRQEKIQAVPISDSRALREQLTDEKKll 1435
Cdd:PTZ00121 1176 KKAEAARKAEEVRKA-------EELRKAEDARKAEAARKAEE--ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK-- 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1436 GEIEKNKDKIDDCHKNAKAYidsvkdYEFQILTYKALQDPIASPLKKPKMECASDDIiqeyvnlrtRYSELMTLTNQYIK 1515
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAH------FARRQAAIKAEEARKADELKKAEEKKKADEA---------KKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1516 FIIDAQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRqdvaADAEKQ 1594
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEaKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK----ADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1595 KQNIQQELQHLKSLSdQEIKSKNQQLEDALVSRRKieeeihiiRIQLEKTTAHKAKSEaELQELRDRAAEAEKLRKAAQD 1674
Cdd:PTZ00121 1386 KAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKK--------ADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1675 --EAERLRKQvAEETQR----KKNAEDelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE 1748
Cdd:PTZ00121 1456 akKAEEAKKK-AEEAKKadeaKKKAEE--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1749 VAQKSAATQlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLrlqA 1828
Cdd:PTZ00121 1533 AKKADEAKK--------AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL---Y 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1829 EEEAQKKSHAQEEAEKQKLEAERDAK-KRGKAEEAALKQKENAEKELDKQRKFAEQiaQQKLSAEQECIRLKADFEHAEQ 1907
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1908 QRGllDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMR 1987
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1988 SVAEEAKKQRQIAEEeaarQRSEAEKILKEKLAAINEATRLKTE---------AEMALKAKEAENERLKRQAEEEAYQRK 2058
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2059 LLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESEL--KKLKGIAD 2136
Cdd:PTZ00121 1834 EVADSKNMQLEEADA-FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIpnNNMAGKNN 1912
|
890
....*....|.
gi 1389908274 2137 ETQKSKLKAEE 2147
Cdd:PTZ00121 1913 DIIDDKLDKDE 1923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1681-2587 |
1.11e-27 |
|
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: 124.40 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1681 KQVAEETQRK-KNAEDELKRKSDAEKEAAKQkqralddLQKYKMQAEEAER-RMKQAEEEKIR---QIRVVEEVAQKSAA 1755
Cdd:TIGR02168 171 KERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERyKELKAELRELElalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1756 TQLQTKAM-----SFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEE 1830
Cdd:TIGR02168 244 LQEELKEAeeeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1831 EaqkkshaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRG 1910
Cdd:TIGR02168 324 Q-------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1911 LLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL----LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARM 1986
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1987 RSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENerlKRQAEEEAYQRKLLEDQAAQ 2066
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE---GYEAAIEAALGGRLQAVVVE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2067 HKQDIEEKITQLqtsSDSELGRQKNIVEETLKQKKVVEEEIHIIKiNFHKASKEKADLESELKKLKG----------IAD 2136
Cdd:TIGR02168 554 NLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRKalsyllggvlVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2137 ETQksklkaeeEAEKLKKLAAEEERRRKEAEEKVKR---ITAAEEEAARQCKAAQEEVERLKKKAEdankqkekaekeae 2213
Cdd:TIGR02168 630 DLD--------NALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSILERRREIEELEEKIE-------------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2214 kqvvlakEAAQKCTAAEQKAQDVLSKnkedvlaQEKLRDEFENAKKLAQEaekakekaekeaalLRQKAEEAEKQKKAAE 2293
Cdd:TIGR02168 688 -------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEE--------------LSRQISALRKDLARLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2294 NEAAKQAKAQNDTEKQRKEAEeeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQK 2373
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELE--------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2374 VLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEEnrrlmqkdkdstqklLAEEAEKMKSLAEEAGR 2453
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED---------------IESLAAEIEELEELIEE 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2454 LSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQEtakRLQEDKQQIQQRLDKETE 2533
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSE 947
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2534 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-------AEDEAKKFKKQADEVKAQ 2587
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1281-2078 |
3.49e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1281 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEaEADQVMFDRLQDDLRKATTVH--DKMTRIHSERDADLEHYR 1358
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRkaEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1359 QLVNGLLERWQAVFAQIELRLRELDLLGRHMNSYRDSYEwlIRWLTEAR-----QRQEKIQAVPISDSRALRE------- 1426
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE--IRKFEEARmahfaRRQAAIKAEEARKADELKKaeekkka 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1427 ---QLTDEKKLLGEIEKN----------KDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKKPKMECASDDII 1493
Cdd:PTZ00121 1293 deaKKAEEKKKADEAKKKaeeakkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNlrtRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLK--EEERRKMAEIQAELDKQKQMAEAHAKsvAKAEQEAL 1571
Cdd:PTZ00121 1373 KEEAK---KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKAD 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1572 ELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1651
Cdd:PTZ00121 1448 EAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELR--DRAAEAEKLRKAAQ-DEAERLRK--QVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAE 1726
Cdd:PTZ00121 1527 AKKAEEAKkaDEAKKAEEKKKADElKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1806
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1807 AEQEleiwrQKANEALRlrlQAEEEAQKkshaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1886
Cdd:PTZ00121 1684 EEDE-----KKAAEALK---KEAEEAKK----AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1887 QklsaEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKsk 1966
Cdd:PTZ00121 1752 D----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK-- 1825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1967 qllESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQ-----RSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 2041
Cdd:PTZ00121 1826 ---EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
810 820 830
....*....|....*....|....*....|....*..
gi 1389908274 2042 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQL 2078
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKI 1939
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
211-313 |
3.54e-27 |
|
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: 108.73 E-value: 3.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1720-2388 |
5.53e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.97 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEE--EKIRQIRvvEEVAQksaatQLqtkamsfseqttkleESLKKEQGNVLK---LQEEADKLK 1794
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlERLEDIL--GELER-----QL---------------EPLERQAEKAERyreLKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1795 KQQKEAntAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKEL 1874
Cdd:COG1196 227 AELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1875 DKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINA 1954
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1955 EKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlkTEAEM 2034
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2035 ALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIhiikinf 2114
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2115 hKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerrrkeaeekvKRITAAEEEAARQCKAAQEEVERL 2194
Cdd:COG1196 533 -EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA----------------GRATFLPLDKIRARAALAAALARG 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2195 KKKAEDANKQKEKAEKEAEKQVVLAKEAaqkctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKE 2274
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLL-----GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2275 AALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQ 2354
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
650 660 670
....*....|....*....|....*....|....
gi 1389908274 2355 VEKELTVVKLQLDETDKQKVLLDQELQRvKGEVN 2388
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEA-LGPVN 783
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
204-315 |
1.15e-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: 107.92 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 204 RIADERDRVQKKTFTKWVNKHLVKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 280
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1389908274 281 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1660-2763 |
1.24e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 121.09 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1660 DRAAEAEKLRKAAQDEAERLRkqvaeetqrkKNAEDELkrksdaeKEAAKQKQRALDDL--QKYKMQAE---EAERRMKQ 1734
Cdd:NF041483 69 DIGYQAEQLLRNAQIQADQLR----------ADAEREL-------RDARAQTQRILQEHaeHQARLQAElhtEAVQRRQQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1735 AEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ-----QKEANTAREEAEQ 1809
Cdd:NF041483 132 LDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEarqrlGSEAESARAEAEA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1810 eleIWRQKANEALRLRLQAEEEAQK-KSHAQ----------EEAEKQKLEAERDAKKRGKAEEAALKQkenAEKELDKQR 1878
Cdd:NF041483 212 ---ILRRARKDAERLLNAASTQAQEaTDHAEqlrsstaaesDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1879 KFAEQIAQQKLSAEQECirlkadfehAEQQRGLLDNELQRLKNE-VNSTEKQRKQLEDELNKVRSEMDSLLQMKinAEKA 1957
Cdd:NF041483 286 AEAKEAAAKQLASAESA---------NEQRTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEA--AEKA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1958 SMVNTEKSKQLL-----ESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE-KLAAIN-------- 2023
Cdd:NF041483 355 RTVAAEDTAAQLakaarTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDdtkeyrak 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2024 ------EATRLKTEAEMALKAKEAENERLKRQAEEEAYQR-----KLLEDQAAQHKQDIEEkiTQLQTSSDSELGRQKNI 2092
Cdd:NF041483 435 tvelqeEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE--LRSTATAESERVRTEAI 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2093 ---------VEETLKQKKvVEEEIHIIKINfHKASKEKADLESELKKLKgiaDETQKS-KLKAEEEAEKLKKLAAEEErr 2162
Cdd:NF041483 513 erattlrrqAEETLERTR-AEAERLRAEAE-EQAEEVRAAAERAARELR---EETERAiAARQAEAAEELTRLHTEAE-- 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2163 rkeaeekvKRITAAEE-------EAARQCKAAQEEVERLkkKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQD 2235
Cdd:NF041483 586 --------ERLTAAEEaladaraEAERIRREAAEETERL--RTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGEN 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2236 VLSKNKEDVLAQ-EKLRDEfenAKKLAQeaekakekaekeaallRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeae 2314
Cdd:NF041483 656 VAVRLRSEAAAEaERLKSE---AQESAD----------------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRR--- 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2315 eeaarraaaeaaalkqkqQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQ 2393
Cdd:NF041483 714 ------------------EAEETLGSARAEADQERERaREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQ 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2394 KSQ-VEVELARVRIQM-EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEA-EETARQRQIAES 2470
Cdd:NF041483 776 TAQqVRDSVAGLQEQAeEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAqEETEAAKALAER 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2471 NLAEQRALAEKILKEK---------------MQAIQEATKLKAEA-EKLQKQKDQAQETAKRL------QEDKQQIQQRL 2528
Cdd:NF041483 856 TVSEAIAEAERLRSDAseyaqrvrteasdtlASAEQDAARTRADArEDANRIRSDAAAQADRLigeatsEAERLTAEARA 935
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2529 DKETEGFQKSLEAERKR----------QLEASAEAEKLKLRVKE-LSLAQTKAE---DEAKKFKKQADEVKAQLQRTEKH 2594
Cdd:NF041483 936 EAERLRDEARAEAERVRadaaaqaeqlIAEATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERLRTEARE 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2595 TTEIVVQklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE------QQKAELQQSFLTEK 2668
Cdd:NF041483 1016 EADRTLD--EARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADtmvgaaRKEAERIVAEATVE 1093
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2669 GLLLkrekeVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAimdeavRKQKEAEEEMKNKQREMDVLDKK 2748
Cdd:NF041483 1094 GNSL-----VEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHE------RARRESAEQMKSAGERCDALVKA 1162
|
1210
....*....|....*
gi 1389908274 2749 RLEQEKQLAEENKKL 2763
Cdd:NF041483 1163 AEEQLAEAEAKAKEL 1177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1720-2583 |
1.51e-26 |
|
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: 120.55 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKeqgnvLKLQ-EEADKLKKQQK 1798
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE-----------------------LERQLKS-----LERQaEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1799 EantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaALKQKENAEKELdkqr 1878
Cdd:TIGR02168 221 E----LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKEL---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1879 kfaeqiaqQKLSAEQEciRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekas 1958
Cdd:TIGR02168 291 --------YALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1959 mvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlka 2038
Cdd:TIGR02168 352 ----------------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2039 kEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqknivEETLKQKKVVEEEIHIIKINFHKAS 2118
Cdd:TIGR02168 413 -EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL---------------EELQEELERLEEALEELREELEEAE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2119 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEE-------------------- 2178
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrlqavvven 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2179 -EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2257
Cdd:TIGR02168 555 lNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2258 KKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEA 2317
Cdd:TIGR02168 635 LELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2318 ARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNdafKQKSQV 2397
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQI 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2398 EVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2475
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2476 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKsLEAERKRQLEASAEAEK 2555
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYS 950
|
890 900 910
....*....|....*....|....*....|...
gi 1389908274 2556 LKL-----RVKELSLAQTKAEDEAKKFKKQADE 2583
Cdd:TIGR02168 951 LTLeeaeaLENKIEDDEEEARRRLKRLENKIKE 983
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
211-316 |
1.91e-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: 107.04 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2176-2828 |
3.98e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.86 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2176 AEEEAARQCKAAQEE--VERLKKKAEDANKQKEKAEKEAEKQVVLAKEA-----------------AQKCTAAEQKAQDV 2236
Cdd:PTZ00121 1100 AEEAKKTETGKAEEArkAEEAKKKAEDARKAEEARKAEDARKAEEARKAedakrveiarkaedarkAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2237 LSKNKEDVLAQEKLR--------------DEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQ--- 2299
Cdd:PTZ00121 1180 AARKAEEVRKAEELRkaedarkaeaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfee 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2300 --------AKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK----KEAEQALQQKSQVEKELTVVKLQLD 2367
Cdd:PTZ00121 1260 armahfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaeeaKKADEAKKKAEEAKKKADAAKKKAE 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2368 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK----------LKLKIEEENRRLMQKDKDSTQKLL 2437
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeekkkadeAKKKAEEDKKKADELKKAAAAKKK 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2438 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlAEQRALAEKILK--EKMQAIQEATKLKAEAEKLQKQKDQAQETAK 2515
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2516 RLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2595
Cdd:PTZ00121 1498 KADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2596 TEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKRE 2675
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2676 KEVEGEKKRFE-KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQ-REMDVLDKKRLEQE 2753
Cdd:PTZ00121 1656 EEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEA 1735
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2754 KQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL----VAVTTVGTSKGVLNGSTEVDgvKKEGDSPLSFEGIRE 2828
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrkekEAVIEEELDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
313-428 |
5.20e-26 |
|
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: 105.94 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 313 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAF 392
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908274 393 SVAERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1860-2787 |
7.66e-26 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 118.15 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1860 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNK 1939
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1940 VRSEMDSLLQmKINAEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 2019
Cdd:pfam02463 249 EQEEIESSKQ-EIEKEEEKL---AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2020 AAINEATRLKTEAEMALKAKEaENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ 2099
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2100 KKVVEEEIHIIKINFHKASKEKadlESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEE 2179
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2180 AARQCKaaQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLaqeKLRDEFENAKK 2259
Cdd:pfam02463 481 KLQEQL--ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA---ISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2260 LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMS 2339
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2340 KHKKEAeqalqqKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIE 2419
Cdd:pfam02463 636 KLKESA------KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2420 EENRRLMQKDKDSTQKLLAEEAEKmkslaeeagrlsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2499
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDK-------------INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2500 AEKLQKQKDQAQETAKRLQEdkqqiqqrldketegfqKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2579
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKL-----------------KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QaDEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2659
Cdd:pfam02463 840 L-ELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2660 LQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNK 2738
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1389908274 2739 QREMDVLDKKRLEQEkqlaEENKKLREQLQTFEISSKTVSQTKESQTVS 2787
Cdd:pfam02463 999 RLEEEKKKLIRAIIE----ETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1522-2284 |
1.39e-25 |
|
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: 117.46 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1522 RRLEDDEKASEKL-----KEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQ 1596
Cdd:TIGR02168 216 KELKAELRELELAllvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1597 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEA 1676
Cdd:TIGR02168 285 ELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1677 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT 1756
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1757 QLQTKAMSFSEqttkLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKs 1836
Cdd:TIGR02168 434 ELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1837 hAQEEAEKQKLEAERD--------AKKRGKAEEAALK--------------------QKENAEK-----ELDKQRKFAEQ 1883
Cdd:TIGR02168 509 -KALLKNQSGLSGILGvlselisvDEGYEAAIEAALGgrlqavvvenlnaakkaiafLKQNELGrvtflPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1884 IAQQKLSAEQECIRLKAD--FEHAEQQRGLLDNELQRLK--NEVNSTEKQRKQLEDELNKVRSEMDSLLQ---MKINAEK 1956
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKdlVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1957 ASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAL 2036
Cdd:TIGR02168 668 TNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2037 KAKEAENERLKRQAEEEAYQRKLLEdQAAQHKQDIEEKITQLQtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFHK 2116
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELE----AQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2117 ASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2196
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2197 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2276
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
....*...
gi 1389908274 2277 LLRQKAEE 2284
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
333-428 |
1.43e-25 |
|
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: 103.77 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 333 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 411
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1389908274 412 VPHPDEKSIITYVSSLY 428
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1494-2194 |
2.01e-25 |
|
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: 117.08 E-value: 2.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELD-KQKQMAEAHAKsVAKAEQEAL 1571
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEE-IEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1572 ELKMKmkeeaskrqdvAADAEKQKQNIQQELQHLkslsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1651
Cdd:TIGR02168 292 ALANE-----------ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDEL----KRKSDAEKEAAKQKQRALD--------DLQ 1719
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLERLEDRRERLQQEIEEllkkleeaELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRVVEEV-AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1798
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1799 EANTAREEAEQELEI---WRQKANEALRLRLQA-----EEEAQKKSHAQEEAEKQK-----LEAERDAKKRGKAEEAaLK 1865
Cdd:TIGR02168 517 GLSGILGVLSELISVdegYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQGNDREI-LK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1866 QKENAEKELDKQRKFAEQ---------------------IAQQKLSAEQECI------RLKAD----FEHAEQQRGLL-- 1912
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnaLELAKKLRPGYRIvtldgdLVRPGgvitGGSAKTNSSILer 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1913 DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM-------------KINAEKASMVNTEKSKQLLESE------- 1972
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrQISALRKDLARLEAEVEQLEERiaqlske 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1973 ----ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA---EMALKAKEAENER 2045
Cdd:TIGR02168 756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2046 LKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLE 2125
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--------LEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2126 SELKKLKGIADETQKSKLKAEEEAEKLK--------KLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2194
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
315-428 |
2.06e-25 |
|
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: 104.01 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 315 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 394
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 395 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
329-428 |
5.14e-25 |
|
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: 102.25 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 329 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 408
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1389908274 409 D-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1788-2626 |
5.31e-25 |
|
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: 115.54 E-value: 5.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1788 EEA---DKLKKQQKEANTAREEAEQEL--------EIWRQKAnealRLRLQAE--EEAQKKSHAQEEAEKQKLEAERDAK 1854
Cdd:TIGR02168 162 EEAagiSKYKERRKETERKLERTRENLdrledilnELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1855 KRgKAEEAALKQKENAEKELDKQRKFAEqiAQQKLSaEQECIRLKADFEHAEQQRGLLD--NELQRLKNEVNSTEKQRKQ 1932
Cdd:TIGR02168 238 RE-ELEELQEELKEAEEELEELTAELQE--LEEKLE-ELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 2012
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----ELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2013 KILKEKLAAINEATRLKTEAEMAlkakEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqkni 2092
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERL----EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL-------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2093 vEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 2172
Cdd:TIGR02168 450 -EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2173 ITAAEE---------------------EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ 2231
Cdd:TIGR02168 529 ISVDEGyeaaieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2232 KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKA 2291
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2292 AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2371
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2372 QKVLLDQELQRVKGEVNdafKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAE 2449
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2450 EAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2529
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2530 KETEGFQKsLEAERKRQLEASAEAEKLklrvkELSLAQTKAEDEAKKFKKQADEVKaQLQRTEKHTTEIVVQKLETQRLQ 2609
Cdd:TIGR02168 926 QLELRLEG-LEVRIDNLQERLSEEYSL-----TLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEEL 998
|
890
....*....|....*..
gi 1389908274 2610 STREaDDLKSAIADLEE 2626
Cdd:TIGR02168 999 KERY-DFLTAQKEDLTE 1014
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
328-428 |
7.18e-25 |
|
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: 101.73 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 407
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1389908274 408 EDV---DVphPDEKSIITYVSSLY 428
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
315-428 |
9.75e-25 |
|
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: 102.11 E-value: 9.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 315 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 394
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 395 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
215-312 |
1.54e-24 |
|
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: 100.85 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 215 KTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 290
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1389908274 291 NDDIADGnPKLTLGLIWTIILH 312
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
327-433 |
2.38e-24 |
|
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: 100.44 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 327 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ--ENLEQAFSVAERELGVTK 403
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1389908274 404 -LLDPEDVDvpHPDEKSIITYVSSLYDVMPR 433
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
328-432 |
2.59e-24 |
|
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: 100.25 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1389908274 408 EDVDVPHPDEKSIITYVSSLYDVMP 432
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1924-2723 |
3.96e-24 |
|
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: 112.84 E-value: 3.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1924 NSTEKQRKQLEDELNKVRSEMDSLlqmKINAEKAsmvntEKSKQLleSEALKMKQLADEAARMRSvAEEAKKQRQIAEEE 2003
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSL---ERQAEKA-----ERYKEL--KAELRELELALLVLRLEE-LREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2004 AARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssd 2083
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2084 sELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAD---ETQKSKLKAEEEAE-----KLKKL 2155
Cdd:TIGR02168 327 -ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVAQLELQIaslnnEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2156 AAEEERRRKEAEEKVKRITAAEEEAAR-QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQ 2234
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2235 DVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEkeaaLLRQKAEEAEKQKKAAE--------------NEAAKQA 2300
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG----VLSELISVDEGYEAAIEaalggrlqavvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2301 KA---QNDTEKQ-----RKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAE-----------------QALQQKSQV 2355
Cdd:TIGR02168 562 IAflkQNELGRVtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddldNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2356 EKELTVVKLQLD-------------ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEEL----VKLKLKI 2418
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeelEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2419 EEENRRLmqkdkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKA 2498
Cdd:TIGR02168 722 EELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2499 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAK 2575
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2576 KFKKQADEVKAQLQ--RTEKHTTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeelqrkskemANAQQEQI 2653
Cdd:TIGR02168 877 ALLNERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAQ----------------------LELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2654 EQQKAELQQSFLTEKGLLL-----------KREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEE 2712
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLeeaealenkieDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTE 1014
|
890
....*....|.
gi 1389908274 2713 ERKKLQAIMDE 2723
Cdd:TIGR02168 1015 AKETLEEAIEE 1025
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
212-315 |
6.86e-24 |
|
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: 99.28 E-value: 6.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 287
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
315-428 |
2.98e-23 |
|
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: 97.84 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 315 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 394
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 395 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1494-2360 |
5.48e-23 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 108.91 E-value: 5.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALEL 1573
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1574 -KMKMKEEASKRQDVAADAEKQKQN---------IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK 1643
Cdd:pfam02463 246 lRDEQEEIESSKQEIEKEEEKLAQVlkenkeeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1644 TTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQ----RALDDLQ 1719
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeeleLKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1799
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1800 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1879
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1880 FAEQIAQQKLSAEQECIRLKADFE----HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAE 1955
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLplksIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1956 KASMVNTEKSKQLLESEALKMKQLADeaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEma 2035
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSEL---TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE-- 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2036 lkakEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR---QKNIVEETLKQKKVVEEEIHIIKI 2112
Cdd:pfam02463 721 ----ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELslkEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2113 NFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVE 2192
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2193 RLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ----KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAK 2268
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKeneiEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2269 EKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADA---EMSKHKKEA 2345
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLElfvSINKGWNKV 1036
|
890
....*....|....*
gi 1389908274 2346 EQALQQKSQVEKELT 2360
Cdd:pfam02463 1037 FFYLELGGSAELRLE 1051
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
331-431 |
1.20e-22 |
|
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: 95.61 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPEDV 410
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1389908274 411 DVPHPDEKSIITYVSSLYDVM 431
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1652-2520 |
1.20e-22 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 107.75 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSdAEKEAAKQKQRALDDLQKYKMQAE----- 1726
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL-RDEQEEIESSKQEIEKEEEKLAQVlkenk 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 EAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1806
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAK--EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1807 AEQELEiwrqkanealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQrkfaEQIAQ 1886
Cdd:pfam02463 354 EEEEEE--------------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL----LELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1887 QKLSAEQECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSK 1966
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELK---QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1967 QLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL 2046
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2047 KRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLES 2126
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPI----LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2127 ELKKLKGIA-DETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQK 2205
Cdd:pfam02463 647 GLRKGVSLEeGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2206 ekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEA 2285
Cdd:pfam02463 727 --------------VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2286 EKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKqqadAEMSKHKKEAEQALQQKSQVEKELTVVKLQ 2365
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL----ALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2366 LDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMK 2445
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2446 SLAEEAgRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2520
Cdd:pfam02463 949 EKEENN-KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2027-2593 |
1.20e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2027 RLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsELGRQKNIVEETLKQKKvveEE 2106
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEELR---LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2107 IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKA 2186
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2187 AQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEK 2266
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2267 AKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKK 2343
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2344 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR------IQMEELVKLKLK 2417
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2418 IEEENRRLMQKDKDSTQKLLAEEAEKMKSL-------------AEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2484
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLgdtllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2485 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELS 2564
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*....
gi 1389908274 2565 LAQTKAEDEAkkfKKQADEVKAQLQRTEK 2593
Cdd:COG1196 749 EEEALEELPE---PPDLEELERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1589-2530 |
3.02e-22 |
|
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: 106.68 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1589 ADAEKQKQNIQQELQHL-KSLSDQEIKSKNQQLEDALVSRRKIEEeihiiriQLEKTTAHKAKSEAELQELRDRAAEAEK 1667
Cdd:TIGR02168 209 AEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEE-------ELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1668 LRKAAQDEAERLRKQVAEETQRKKnaedelkrksdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvve 1747
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQ--------------ILRERLANLERQLEELEAQLEELESKLDELAEE--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1748 evaqksaATQLQTKAMSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANTAREEAEQELEiwRQKANEALRLRLQ 1827
Cdd:TIGR02168 339 -------LAELEEKLEELKEELESLEAELEELEA---ELEELESRLEELEEQLETLRSKVAQLEL--QIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1828 AEEEAQKKSHAQEEAEKQKLEaerdakkrgkaEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQ 1907
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELL-----------KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1908 QRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK-INAEKASMVNTEKSKQLLESEALkmkqladeAARM 1986
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgILGVLSELISVDEGYEAAIEAAL--------GGRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1987 RSV----AEEAKKQRQ-IAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerlkrQAEEEAyqRKLLE 2061
Cdd:TIGR02168 548 QAVvvenLNAAKKAIAfLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2062 DQAAQHK--QDIEEKITQLqtssdSELGRQKNIVeeTLKQKKV---------VEEEIHII---KINFHKASKEKADLESE 2127
Cdd:TIGR02168 620 YLLGGVLvvDDLDNALELA-----KKLRPGYRIV--TLDGDLVrpggvitggSAKTNSSIlerRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2128 LKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEK 2207
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2208 AEKeaekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEK 2287
Cdd:TIGR02168 773 AEE-------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2288 QKKAAENEAAKQAKAQNDTEKQRkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLD 2367
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2368 ETDKQKVLLDQELQRVKGEVNDAFKQKSqvevelARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaeeaekmksl 2447
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI----------- 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2448 aEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaeklqkqkdqaqETAKRLQEDKQQIQQR 2527
Cdd:TIGR02168 982 -KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR----------------EARERFKDTFDQVNEN 1044
|
...
gi 1389908274 2528 LDK 2530
Cdd:TIGR02168 1045 FQR 1047
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2124-2723 |
3.33e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2124 LESELKKLKGIADETQKSK-LKAEE---EAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2199
Cdd:COG1196 198 LERQLEPLERQAEKAERYReLKEELkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2200 DANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLR 2279
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2280 QKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEL 2359
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2360 TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-QKLLA 2438
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2439 EEAEKMKSLAEEAGRLSVE--AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLkaEAEKLQKQKDQAQETAKR 2516
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2517 LQEDKQQIQQRLDKETEGFQKSLEA-------ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2589
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2590 RTEKHTTEIVVQKL-ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEK 2668
Cdd:COG1196 676 EAEAELEELAERLAeEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2669 GLLLKREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEEERKKLQAIMDE 2723
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
332-430 |
4.44e-22 |
|
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: 93.95 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 332 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 410
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908274 411 DVPHPDEKSIITYVSSLYDV 430
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
211-316 |
4.78e-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: 94.76 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
211-316 |
7.36e-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: 94.38 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 211 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1683-2589 |
1.03e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 104.67 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1683 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvvEEVAQKSAATQLQTka 1762
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--------ELEEEYLLYLDYLK-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1763 msfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEA 1842
Cdd:pfam02463 234 ----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1843 EKQKLEAERDAKKRGKAEEAALKQKENAEkELDKQRKFAEQIAQQKLSAEQECIRLKadfEHAEQQRGLLDNELQRLKNE 1922
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIE-ELEKELKELEIKREAEEEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMvNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 2002
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK-EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2003 EAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE-AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTS 2081
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2082 SDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK-----GIADETQKSKLKAEEEAEKLKKLA 2156
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2157 AEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV 2236
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2237 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEE 2316
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2317 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQqksQVEKELTVVKLQLDETDKQKVLLDQELQrvKGEVNDAFKQKSQ 2396
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQ--KLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2397 VEVELARVRIQMEELVKLKLKIEEENRRLMQK-DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2475
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKeEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2476 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqKSLEAERKRQLEASAEaEK 2555
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK---ERLEEEKKKLIRAIIE-ET 1015
|
890 900 910
....*....|....*....|....*....|....
gi 1389908274 2556 LKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2589
Cdd:pfam02463 1016 CQRLKEFLELFVSINKGWNKVFFYLELGGSAELR 1049
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
328-426 |
1.60e-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: 92.30 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGKLFSAIIHKHRPALIDMN-QVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1389908274 407 PEDVDVPHPDEKSIITYVSS 426
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2277-2767 |
4.41e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2277 LLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVE 2356
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2357 KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL------MQKDK 2430
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaeelleALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2431 DSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2510
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2511 QETAKRLQEDKQQIQQRLD------KETEGFQKSLEAERK---------------------RQLEASAEAEKLKLRVKEL 2563
Cdd:COG1196 476 EAALAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2564 SLAQTKAEDEAKKFKK------QADEVKAQLQRTEKHTT------------EIVVQKLETQRLQSTREADDLKSAIADLE 2625
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflPLDKIRARAALAAALARgaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2626 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALK--DEQ 2703
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAeaEEE 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2704 ERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2767
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
328-427 |
4.60e-21 |
|
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: 91.00 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 407
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908274 408 ED-VDVPHPDEKSIITYVSSL 427
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
973-1039 |
7.67e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.86 E-value: 7.67e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 973 QLKPRNptTPLKGKMPIQAVCDFKQMEITVHRGDECALLNNSNPFKWQVLNDTGSEASVPSICFLVP 1039
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
324-431 |
8.49e-21 |
|
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: 90.39 E-value: 8.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 324 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 403
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1389908274 404 LLDPEDV-DVPHPDEKSIITYVSSLYDVM 431
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1933-2553 |
1.74e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.40 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK-------KQRQIAEEEAA 2005
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEaeleeleAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2006 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsE 2085
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-----E 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2086 LGRQKNIVEETLKQKKVVEEEIhiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKE 2165
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2166 AEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDvlSKNKEDVL 2245
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2246 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE--------NEAAKQAKAQNDTEKQRKEAEEEA 2317
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqnivVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2318 ARRAAAEAAALKQKQQADAEMSKH-------KKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGE---V 2387
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAvdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2388 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2467
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2468 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ-------AQETAKRLQEDKQQIQQRLD------KETEG 2534
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREdleearETLEE 816
|
650
....*....|....*....
gi 1389908274 2535 FQKSLEAERKRQLEASAEA 2553
Cdd:COG1196 817 AIEEIDRETRERFLETFDA 835
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
328-428 |
1.98e-20 |
|
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: 89.32 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 407
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1389908274 408 EDVDV--PHPDEKSIITYVSSLY 428
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1533-2234 |
3.49e-20 |
|
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: 99.66 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1533 KLKEEERRKMAEIQAELDKQKQMA--------EAHAKSVAKAEQEALE--LKMKMKEEASKRQDVAADAEKQKQNIQQEL 1602
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLAlmefakkkSLHGKAELLTLRSQLLtlCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1603 QHLKSLSDQEIKSKNQQLedalvsrrKIEEEIHIIRIQLEKTTAHKAKSEaELQELRDRAAEAEKLrKAAQDEAERLRKQ 1682
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPL-AAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1683 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQirvveevAQKSAATQLQTKA 1762
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-------EISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1763 MSFSEQTTKLEESLKKEQGNVLKLQEEAdklkkQQKEANTAREEAEQEleiwrQKANEALRLRLQAEEEAQKKSHAQEEA 1842
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQ-----ATIDTRTSAFRDLQG-----QLAHAKKQQELQQRYAELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1843 EKQKLE--AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQECIrLKADFEHAEQQRGLLDN------ 1914
Cdd:TIGR00618 452 QCEKLEkiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL--ELQEEPCP-LCGSCIHPNPARQDIDNpgpltr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1915 --------------ELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEaLKMKQLA 1980
Cdd:TIGR00618 529 rmqrgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ-CDNRSKEDIPNLQNITVRLQDL-TEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1981 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAineatrLKTEAEMALKAKEAENERLKRQAEEEAYQRKLL 2060
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA------LHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2061 EDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvveeeIHIIKINFHKASKEKADLESELKKLKGIADETQK 2140
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-------FNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2141 SKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLK-KKAEDANKQKEKAEKEAEKQVVLA 2219
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAA------EIQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLV 827
|
730
....*....|....*
gi 1389908274 2220 KEAAQKCTAAEQKAQ 2234
Cdd:TIGR00618 828 QEEEQFLSRLEEKSA 842
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
331-427 |
8.54e-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: 87.37 E-value: 8.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 331 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ----ENLEQAFSVAERELGVTKLLD 406
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1389908274 407 PEDVDVPHPDEKSIITYVSSL 427
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
328-427 |
1.97e-19 |
|
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: 86.44 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 407
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908274 408 ED-VDVPHPDEKSIITYVSSL 427
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1519-2616 |
2.60e-19 |
|
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: 96.78 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLkEEERRKMAEIQAELDKQKQMAEAhAKSVAKAEQEALELKMK-MKEEASKRQDVAADAEKQKQN 1597
Cdd:pfam01576 79 ELESRLEEEEERSQQL-QNEKKKMQQHIQDLEEQLDEEEA-ARQKLQLEKVTTEAKIKkLEEDILLLEDQNSKLSKERKL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1598 IQQELQHLKS-LSDQEIKSKNqqledalvsrrkieeeihiiriqlekTTAHKAKSEAELQELRDRAAEAEKLRkaaqdea 1676
Cdd:pfam01576 157 LEERISEFTSnLAEEEEKAKS--------------------------LSKLKNKHEAMISDLEERLKKEEKGR------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1677 ERLRKqvaeetqrkknaedeLKRKSDAEkeaAKQKQRALDDLQkykMQAEEAERRMKQAEEE-KIRQIRVVEEVAQKSAA 1755
Cdd:pfam01576 204 QELEK---------------AKRKLEGE---STDLQEQIAELQ---AQIAELRAQLAKKEEElQAALARLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1756 tqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQAEEEAQKK 1835
Cdd:pfam01576 263 -----------------LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD-TTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1836 SHAQEEAEKQKLEAErdaKKRGKAEEAALKQKENA-----EKELDKQRKFAEQIAQQKLSAEQECIRLKADFE------- 1903
Cdd:pfam01576 325 REQEVTELKKALEEE---TRSHEAQLQEMRQKHTQaleelTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakq 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1904 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmVNTEKSKQLLESEALKMKQLADEA 1983
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKN-IKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1984 ARMRsvAEEAKKQRQIAEEEAArqrseaekiLKEKLAAINEATRlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQ 2063
Cdd:pfam01576 481 TRQK--LNLSTRLRQLEDERNS---------LQEQLEEEEEAKR---NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2064 AAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 2143
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAA--------YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2144 KAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaekeaekqvVLAKEAA 2223
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL----------------------VSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2224 QKCTAAEQKAQDVLSKNKEDVLAQ-EKLRDEF---ENAKklaqeaekakekaekeaalLRQkaeEAEKQKKAAENEAAKQ 2299
Cdd:pfam01576 677 GKNVHELERSKRALEQQVEEMKTQlEELEDELqatEDAK-------------------LRL---EVNMQALKAQFERDLQ 734
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2300 AKAQNDTEKQRkeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQE 2379
Cdd:pfam01576 735 ARDEQGEEKRR---------------QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2380 LQRVKGEVNDAfkQKSQVEVELARVRI------------QME-ELVKLK--LKIEEENRRLMQKDKDSTQKLLAEEAEKM 2444
Cdd:pfam01576 800 LKKLQAQMKDL--QRELEEARASRDEIlaqskesekklkNLEaELLQLQedLAASERARRQAQQERDELADEIASGASGK 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2445 KSLAEEAGRLSveaeetARQRQIAESNLAEQ---RALAEKILKEKMQAIQEATKLKAEAEKLQKQKD-------QAQETA 2514
Cdd:pfam01576 878 SALQDEKRRLE------ARIAQLEEELEEEQsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSESarqqlerQNKELK 951
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2515 KRLQEDKQQIQQR-------LDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQAD----- 2582
Cdd:pfam01576 952 AKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEkgnsr 1031
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 1389908274 2583 --EVKAQLQRTEKHTTEIVVQKLETQR-LQSTREADD 2616
Cdd:pfam01576 1032 mkQLKRQLEEAEEEASRANAARRKLQReLDDATESNE 1068
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2438-2759 |
3.76e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2438 AEEAEKMKSLAEEAGRLsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2517
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2518 QEDKQQIQQRLDKEtegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTE 2597
Cdd:COG1196 287 QAEEYELLAELARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2598 IVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ-QEQIEQQKAELQQSFLTEKGLLLKREK 2676
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2677 EVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQL 2756
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
...
gi 1389908274 2757 AEE 2759
Cdd:COG1196 523 AGA 525
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
213-313 |
5.00e-19 |
|
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: 85.33 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 288
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1389908274 289 IRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1773-2734 |
1.70e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 94.12 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR------------LRLQAEeeaQKKSHAQE 1840
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAE---QLLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1841 EAEKQKLEAERdakkrgkaeeaalkqkenaekELDKQRKFAEQIAQqklsaeqecirlkadfEHAEQQrglldnelQRLK 1920
Cdd:NF041483 84 QADQLRADAER---------------------ELRDARAQTQRILQ----------------EHAEHQ--------ARLQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1921 NEVNSTEKQRKQ-LEDELNKVRSEMDSLLQMKIN-AEKASMVNTEKSKQLL-ESEALKMKQLADEAARMRSVAEEAKkQR 1997
Cdd:NF041483 119 AELHTEAVQRRQqLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEAR-QR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1998 QIAEEEAARqrSEAEKILK------EKL--AAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqrklLEDQAAQHKQ 2069
Cdd:NF041483 198 LGSEAESAR--AEAEAILRrarkdaERLlnAASTQAQEATDHAEQLRSSTAAESDQARRQAAE-------LSRAAEQRMQ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2070 DIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikiNFHKASKEKADLESE-LKKLKGIADETQKSKLKAEEE 2148
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQ------RTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2149 AEKLkklaaeeerrrKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2228
Cdd:NF041483 343 AEKL-----------VAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAA----------AEEAERIRRE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2229 AEQKAqDVLSKNKEDVLAQEK---LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQND 2305
Cdd:NF041483 402 AEAEA-DRLRGEAADQAEQLKgaaKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAAR 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2306 TEKQrkeaeeeaarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKElTVVKLQLDETdkqkvlldqeLQRVKG 2385
Cdd:NF041483 481 TAEE------------------LLTKAKADADELRSTATAESERVRTEAIERA-TTLRRQAEET----------LERTRA 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2386 EvndAFKQKSQVEVELARVRIQMEELVKlklKIEEENRRLMQkdkdstqkllAEEAEKmkslAEEAGRLSVEAEEtarQR 2465
Cdd:NF041483 532 E---AERLRAEAEEQAEEVRAAAERAAR---ELREETERAIA----------ARQAEA----AEELTRLHTEAEE---RL 588
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2466 QIAESNLAEQRALAEKILKEkmqAIQEATKLKAEA-EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFqksleAERK 2544
Cdd:NF041483 589 TAAEEALADARAEAERIRRE---AAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENV-----AVRL 660
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2545 RQlEASAEAEKLKLRVKEL-----SLAQTKAE---DEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADD 2616
Cdd:NF041483 661 RS-EAAAEAERLKSEAQESadrvrAEAAAAAErvgTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEE 739
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2617 -LKSAIADLEEERKKLKKEAEELQRKSKEMANAqQEQIEQQKAElqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKK 2695
Cdd:NF041483 740 lLASARKRVEEAQAEAQRLVEEADRRATELVSA-AEQTAQQVRD------SVAGLQEQAEEEIAGLRSAAEHAAERTRTE 812
|
970 980 990
....*....|....*....|....*....|....*....
gi 1389908274 2696 AkalKDEQERQRKLMEEERKKLQaimDEAVRKQKEAEEE 2734
Cdd:NF041483 813 A---QEEADRVRSDAYAERERAS---EDANRLRREAQEE 845
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1805-2614 |
2.63e-18 |
|
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: 93.59 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1805 EEAEQELEIWRQKANEalrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQI 1884
Cdd:TIGR02169 180 EEVEENIERLDLIIDE---KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1885 AQQKLSAEQECIRLKADFEHAEQQ-RGLLDNELQRLKNEVNSTEKQRKQLEdelnkvRSEMDSLLQMKINAEKASMVNTE 1963
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLE------RSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1964 KSKQLLESEALKmKQLADEAARMRSVAEEAKKqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMaLKAKEAEN 2043
Cdd:TIGR02169 331 IDKLLAEIEELE-REIEEERKRRDKLTEEYAE----LKEELEDLRAELEEVDKEFAETRDELKDYREKLEK-LKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2044 ERLKRQAEEEAYQrklLEDQAAQHKQDI---EEKITQLQTSSDS---ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKA 2117
Cdd:TIGR02169 405 KRELDRLQEELQR---LSEELADLNAAIagiEAKINELEEEKEDkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2118 SKEKADLESELKKLkgiadETQKSKLKAEEE----AEKLKKLAAEEERRRKEAEEKVKR--ITAAEEEAARQCKA----- 2186
Cdd:TIGR02169 482 EKELSKLQRELAEA-----EAQARASEERVRggraVEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNvvved 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2187 ---AQEEVERLK-KKAEDA-----NKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedVLAQEKLRDEFENA 2257
Cdd:TIGR02169 557 davAKEAIELLKrRKAGRAtflplNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKY----VFGDTLVVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2258 KKLAQEA-------------------EKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAA 2318
Cdd:TIGR02169 633 RRLMGKYrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2319 RRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2398
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND-------LE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2399 VELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQKL----LAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESN--L 2472
Cdd:TIGR02169 786 ARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2473 AEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQ------KSLEAERKRQ 2546
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelSEIEDPKGED 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2547 LEASAE---AEKLKLRVKELSLA-------QTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV--VQKLETQRLQSTREA 2614
Cdd:TIGR02169 944 EEIPEEelsLEDVQAELQRVEEEiralepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILerIEEYEKKKREVFMEA 1023
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1506-2155 |
3.01e-18 |
|
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: 93.32 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1506 LMTLTNQYIKFIIDAQRRLEDDEKAS---EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS 1582
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRqelEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1583 KRqdvaadAEKQKQNiqQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkaKSEAELQELRD-R 1661
Cdd:pfam01576 258 QK------NNALKKI--RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSkR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1662 AAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaeKEAAKQKQRALDDLQKYKmQAEEAERRMKQAEEEKIR 1741
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1742 QIRVVEEVAQKSAATQLQTKAMSFSE---QTTKLEESLKKEQG---NVLKLQEEAD-KLKKQQKEANTAREEAE--QEL- 1811
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEKLSKLQSeleSVSSLLNEAEgKNIKLSKDVSSLESQLQdtQELl 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1812 -EIWRQKANEALRLRlQAEEEAQKKSHAQEEAEKQKLEAERdakkrgkaeeaalkQKENAEKELDKQRKFAEQIAQQKLS 1890
Cdd:pfam01576 478 qEETRQKLNLSTRLR-QLEDERNSLQEQLEEEEEAKRNVER--------------QLSTLQAQLSDMKKKLEEDAGTLEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1891 AEQECIRLKADFEHAEQQrglldneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvNTEKSKQLLE 1970
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQ-------LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK----KQKKFDQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1971 SEALKMKQLADEAARMRSVAEEaKKQRQI----AEEEAARQRSEAEKILKEKLAAINEATRLKT-------EAEMALKAK 2039
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEARE-KETRALslarALEEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhELERSKRAL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2040 EAENERLKRQAEEeayqrklLED--QAAQH-KQDIEEKITQLQTSSDSELGRQKNIVEET----LKQKKVVEEEIHIIKI 2112
Cdd:pfam01576 691 EQQVEEMKTQLEE-------LEDelQATEDaKLRLEVNMQALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERK 763
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1389908274 2113 NFHKASKEKADLESELKKLKGIADETQKSKlkaEEEAEKLKKL 2155
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKKL 803
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1447-2134 |
5.61e-18 |
|
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: 92.34 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1447 DCHKNAKAYIDSVKDyEFQILTYKALQDPIASPLKKPKMEcasddiiQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLED 1526
Cdd:TIGR00618 187 AKKKSLHGKAELLTL-RSQLLTLCTPCMPDTYHERKQVLE-------KELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1527 DEKASEKLKEEER-----RKMAEIQAELDKQKQMAE--AHAKSVAKAEQEAL----ELKMKMKEEASKRQDVAAdAEKQK 1595
Cdd:TIGR00618 259 QQLLKQLRARIEElraqeAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQrihtELQSKMRSRAKLLMKRAA-HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1596 QNIQQELQHLKSLSDQEIKSKNQQLEDALV----SRRKIEEEIHIIRIQ---------------LEKTTAHKAKSEAELQ 1656
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIreisCQQHTLTQHIHTLQQqkttltqklqslckeLDILQREQATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1657 ELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAE---DELKRKSDAEKEAAKQKQRALddLQKYKMQAEEAER 1730
Cdd:TIGR00618 418 AFRDlqgQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKihlQESAQSLKEREQQLQTKEQIH--LQETRKKAVVLAR 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1731 RMKQAEEEKI--RQIRVVEEVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKLQEEADKLKKQQKEAntarEEA 1807
Cdd:TIGR00618 496 LLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLETSEEDVYHQLTSERKQRASLKEQMQEI----QQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1808 EQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERdAKKRGKAEEAALKQK----ENAEKELdKQRKFAEQ 1883
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVrlhlQQCSQEL-ALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1884 IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV-NT 1962
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAsSS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1963 EKSKQLLESEAL-----KMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRL--KTEAEMA 2035
Cdd:TIGR00618 730 LGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLlkTLEAEIG 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2036 LKAKEAENERLKRQaeeeayqrKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQkkvveeeihiikinFH 2115
Cdd:TIGR00618 810 QEIPSDEDILNLQC--------ETLVQEEEQFLSRLEEKSATL-----GEITHQLLKYEECSKQ--------------LA 862
|
730
....*....|....*....
gi 1389908274 2116 KASKEKADLESELKKLKGI 2134
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNGI 881
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
330-428 |
8.65e-18 |
|
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: 81.96 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1389908274 410 -VDVPHPDEKSIITYVSSLY 428
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
332-430 |
9.99e-18 |
|
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: 81.85 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 332 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 410
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908274 411 DVPHPDEKSIITYVSSLYDV 430
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
214-311 |
1.53e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.85 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 214 KKTFTKWVNKHL-VKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 289
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1389908274 290 RNDDI-ADGNPKLTLGLIWTIIL 311
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
330-429 |
4.68e-17 |
|
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: 79.62 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1389908274 410 VDV--PHPDEKSIITYVSSLYD 429
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
330-433 |
6.03e-17 |
|
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: 79.32 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1389908274 410 VDV--PHPDEKSIITYVSSLYDVMPR 433
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
333-428 |
1.03e-16 |
|
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: 78.94 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 333 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDPED-VD 411
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1389908274 412 VPHPDEKSIITYVSSLY 428
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1279-2154 |
1.35e-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: 87.80 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1279 ADAEETLKNYEARLRDVSKVPSeQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYR 1358
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL-VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1359 QLVNGLLERWQAVFAQIELRLREldllgrhMNSYRDSYEWLIRWLTEARQRQEKiqavpisdsraLREQLTDEKKLLGEI 1438
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESKLDE-----------LAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1439 EKNKDKIDDCHKNAKAyidsvkdyefqiltykalqdpiasplKKPKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFII 1518
Cdd:TIGR02168 350 KEELESLEAELEELEA--------------------------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEE--------ERRKMAEIQAELDKQKQMAEAHAKSVAKAEqEALELKMKMKEEASKRQDvaaD 1590
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEieellkklEEAELKELQAELEELEEELEELQEELERLE-EALEELREELEEAEQALD---A 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1591 AEKQKQNIQQELQHLKSLsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA--HKAKSEA---ELQELRDRAAEA 1665
Cdd:TIGR02168 480 AERELAQLQARLDSLERL--QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyEAAIEAAlggRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1666 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAkqkQRALDDLQKYKMQAEEAERRMKQaeeekirQIRV 1745
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF---LGVAKDLVKFDPKLRKALSYLLG-------GVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1746 VEEVAQksaATQLQtKAMSFSEQTTKLEESLKKEQGNVLklqeeadklkKQQKEANTAREEAEQELEIWRQKANEalrlr 1825
Cdd:TIGR02168 628 VDDLDN---ALELA-KKLRPGYRIVTLDGDLVRPGGVIT----------GGSAKTNSSILERRREIEELEEKIEE----- 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 lqAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1905
Cdd:TIGR02168 689 --LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1906 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEalkmkqlADEAAR 1985
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLERR-------IAATER 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1986 MRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 2065
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2066 QHKQDIEEKITQLQTssdSELGRQKNIveETLKQKKVVEEEIHIIKINFHKASKEKAdlESELKKLKGIADETQKSKLKA 2145
Cdd:TIGR02168 919 ELREKLAQLELRLEG---LEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEA--RRRLKRLENKIKELGPVNLAA 991
|
....*....
gi 1389908274 2146 EEEAEKLKK 2154
Cdd:TIGR02168 992 IEEYEELKE 1000
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2333-2747 |
2.63e-16 |
|
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: 87.05 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2333 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLD--ETDKQKVLLDQELQRVKGEV---------NDAFKQKSQVEVEL 2401
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYegyellkekEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2402 ARVRiqmEELVKLKLKIEEENRRLMQKdkdstQKLLAEEAEKMKSLAEEagrlsveaeetarqrqiaesnlaEQRALAEK 2481
Cdd:TIGR02169 247 ASLE---EELEKLTEEISELEKRLEEI-----EQLLEELNKKIKDLGEE-----------------------EQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2482 ILKekmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDK---ETEGFQKSLEAERKRQLEASAEAEKLKl 2558
Cdd:TIGR02169 296 IGE-----------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELK- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2559 rvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStrEADDLKSAIADleeerkklkkeaeel 2638
Cdd:TIGR02169 364 --EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE--ELQRLSEELAD--------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 qrkskemANAQQEQIEQQKAELQqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERqrklMEEERKKLQ 2718
Cdd:TIGR02169 425 -------LNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQ 489
|
410 420
....*....|....*....|....*....
gi 1389908274 2719 AIMDEAVRKQKEAEEEMKNKQREMDVLDK 2747
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1733-2761 |
3.27e-16 |
|
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: 86.77 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1733 KQAEE--EKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEESLKKEQgnvlKLQEEADKL------KKQQKEANT 1802
Cdd:pfam01576 2 RQEEEmqAKEEELQKVKERQQKAESelKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMrarlaaRKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1803 AREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER-DAKKRGKAEEAALKQKENAEKELDKQRKFA 1881
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvTTEAKIKKLEEDILLLEDQNSKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1882 EQ-IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNS---TEKQRKQLEDELNKVRSEMdslLQMKINAEKA 1957
Cdd:pfam01576 158 EErISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGESTDLQEQI---AELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1958 SMVNTEKSKQLLESEALKMKQLADEAARMRSVAEeakKQRQIAE--EEAARQRSEAEKILKEKLAAINEATRLKTEAEMA 2035
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKIRE---LEAQISElqEDLESERAARNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2036 LKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQkniVEETLKQKKVVEEEIHIIKinfh 2115
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE-MRQKHTQALEELTEQ---LEQAKRNKANLEKAKQALE---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2116 kasKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaaeeeaarqckaaQEEVERLK 2195
Cdd:pfam01576 384 ---SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL--------------QSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2196 KKAEDANKQKEKaekeaekqvvLAKEAAQkctaAEQKAQDVLSknkedvLAQEKLRDEFENAKKLAQEAEKAKEkaekea 2275
Cdd:pfam01576 447 SLLNEAEGKNIK----------LSKDVSS----LESQLQDTQE------LLQEETRQKLNLSTRLRQLEDERNS------ 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2276 alLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQV 2355
Cdd:pfam01576 501 --LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2356 EKELTVVKLQLDET-------DKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRiqmeELVKLKLKIEEENRRLMQK 2428
Cdd:pfam01576 579 QQELDDLLVDLDHQrqlvsnlEKKQKKFDQMLAEEKAISARYAEERDRAEAE-AREK----ETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2429 DKDSTQKLLAEEAEKMKSLAEEAGRlsvEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEAtKLKAEAeKLQKQKD 2508
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGK---NVHELERSKRALEQQVEEMKTQLEE-LEDELQATEDA-KLRLEV-NMQALKA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2509 QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSL---AQTKAEDEA----KKFKKQA 2581
Cdd:pfam01576 728 QFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAqidAANKGREEAvkqlKKLQAQM 807
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2582 DEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLksaiadleeerkklkkeaeelqRKSKEMANA--QQEQIEQQKAE 2659
Cdd:pfam01576 808 KDLQRELEEARASRDEILAQSKESEKKLKNLEAELL----------------------QLQEDLAASerARRQAQQERDE 865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2660 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEE-------ERKKLQAimDEAVRKQK 2729
Cdd:pfam01576 866 LADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelaaERSTSQK--SESARQQL 943
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 1389908274 2730 EAE-EEMKNKQREMD------------VLDKKRLEQEKQLAEENK 2761
Cdd:pfam01576 944 ERQnKELKAKLQEMEgtvkskfkssiaALEAKIAQLEEQLEQESR 988
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1529-2194 |
3.84e-16 |
|
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: 86.66 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1529 KASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvaadaekqkQNIQQELQHLKS- 1607
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ----------LRVKEKIGELEAe 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1608 --LSDQEIKSKNQQLEDALVSRRKieeeihiIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE 1685
Cdd:TIGR02169 303 iaSLERSIAEKERELEDAEERLAK-------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1686 ETQRKKNAEDELK---RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaqksaatqLQTKA 1762
Cdd:TIGR02169 376 VDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE--------KEDKA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1763 MSFSEQTTKLE---ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL------------- 1826
Cdd:TIGR02169 448 LEIKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtv 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1827 ----QAEEEAQKkshAQEEAEKQKLEA-----ERDAK------KRGKAEEAA---LKQKENAEKELDKQRK--------- 1879
Cdd:TIGR02169 528 aqlgSVGERYAT---AIEVAAGNRLNNvvvedDAVAKeaiellKRRKAGRATflpLNKMRDERRDLSILSEdgvigfavd 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1880 ---FAEQIAqqklSAEQECIRLKADFEHAEQQRGLLDN------------------------------------ELQRLK 1920
Cdd:TIGR02169 605 lveFDPKYE----PAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggsraprggilfsrsepaELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1921 NEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK------ 1994
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvkse 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1995 ----------KQRQIAEEEAAR---QRSEAEKILKEKLAAIN--EATRLKTEA-----EMALKAKEAENERLKRQAEEEA 2054
Cdd:TIGR02169 760 lkelearieeLEEDLHKLEEALndlEARLSHSRIPEIQAELSklEEEVSRIEArlreiEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2055 YQRKLLEDQAAQHKQDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 2134
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2135 ADETqksKLKAEEEAEKLKKLAAEEERRRKEAEEkvkriTAAEEEAARQCKAAQEEVERL 2194
Cdd:TIGR02169 919 LSEL---KAKLEALEEELSEIEDPKGEDEEIPEE-----ELSLEDVQAELQRVEEEIRAL 970
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
330-428 |
3.94e-16 |
|
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: 77.43 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1389908274 410 -VDVPHPDEKSIITYVSSLY 428
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1663-2359 |
8.47e-16 |
|
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: 85.41 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1663 AEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAA------KQKQRALDDLQKYKMQAEEAERRMKQAE 1736
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshaylTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1737 ---------EEKIRQIRVVEEVAQKSAAT-----QLQTKAMSFSEQTTKLEESLKKEQGNV---LKLQEEADKLKKQQKE 1799
Cdd:TIGR00618 274 aqeavleetQERINRARKAAPLAAHIKAVtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVkqqSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1800 ANTAREEAEQELeIWRQKANEALRLRLQAEEEAQKKSHA------------QEEAEKQKLEAERDAKKRGKAEEAALKQK 1867
Cdd:TIGR00618 354 EIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQKTTLtqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1868 ENAEKE-LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKnEVNSTEKQRKQLEDELNKVRSEMDS 1946
Cdd:TIGR00618 433 QELQQRyAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1947 LLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 2026
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQ----TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2027 RLKTEAEMALKAKEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvvEEE 2106
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQ--HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE----RVR 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2107 IHIIKINFHKASK------EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEA 2180
Cdd:TIGR00618 662 EHALSIRVLPKELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2181 ARQCKAAQEEverlkkkaedankqkekaekeaekqvvlAKEAAQKCTAAEQkaqdvlsKNKEDVLAQEKLRDEFENakkL 2260
Cdd:TIGR00618 742 NQSLKELMHQ----------------------------ARTVLKARTEAHF-------NNNEEVTAALQTGAELSH---L 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2261 AQEAEKAKEKAEKEAALLRQKaeEAEKQKKAAENEAAKQakAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSK 2340
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILN--LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
730
....*....|....*....
gi 1389908274 2341 HKKEAEQALQQKSQVEKEL 2359
Cdd:TIGR00618 860 QLAQLTQEQAKIIQLSDKL 878
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
210-309 |
9.71e-16 |
|
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: 76.03 E-value: 9.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 210 DRVQKKTFTKWVNKHLVKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 284
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1389908274 285 KLVNIRNDDIADGNPKLTLGLIWTI 309
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1703-2722 |
1.07e-15 |
|
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: 85.10 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1703 AEKEAAKQKQRALDDLQKYkMQAEEAERRMKQAEEEKIRQIRVveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGN 1782
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRY-IKALETLRQVRQTQGQKVQEHQM-----ELKYLKQYKEKACEIRDQITSKEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1783 VLKLQEEADKLKKQQKEANTARE---EAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEaEKQKLEAERDAKKRGKA 1859
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE-QLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1860 EEAALKQKE----NAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-------NSTEK 1928
Cdd:TIGR00606 319 RELVDCQREleklNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqikNFHTL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1929 QRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK----QRQIAEEEA 2004
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2005 ARQRSEAEKILKEKlaaiNEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkqdiEEKITQLQTSSDS 2084
Cdd:TIGR00606 479 ELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-----MEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2085 ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKgiaDETQKSKLKAEEEAEKLKKLAaeeerrrk 2164
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLN---KELASLEQNKNHINNELESKE-------- 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2165 eaeekvKRITAAEEEAARQCKAAQEEV--ERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTA----------AEQK 2232
Cdd:TIGR00606 619 ------EQLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2233 AQDVLSK-NKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRK 2311
Cdd:TIGR00606 693 LQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2312 EAEEEAARRAaaeaaaLKQKQQADAEMskhkkeAEQALQQKSQVEKELTVVKLQLDETDkqkvlLDQELQRVKGEVNDaf 2391
Cdd:TIGR00606 773 LLGTIMPEEE------SAKVCLTDVTI------MERFQMELKDVERKIAQQAAKLQGSD-----LDRTVQQVNQEKQE-- 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2392 kqksqvevelarvriQMEELVKLKLKIEEeNRRLMQKDKDSTQKLlaeeaekmKSLAEEAGRLSVEAEETARQRQIAESN 2471
Cdd:TIGR00606 834 ---------------KQHELDTVVSKIEL-NRKLIQDQQEQIQHL--------KSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2472 LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ---AQETAKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqle 2548
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEElisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE-------- 961
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2549 asaeaeklklrvkelSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI------VVQKLETQRLQSTREADDLKSAIA 2622
Cdd:TIGR00606 962 ---------------NKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKInedmrlMRQDIDTQKIQERWLQDNLTLRKR 1026
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2623 DLEEERKKLKKEAEELQrkSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkKAKALKDE 2702
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL-----REPQFRDA 1099
|
1050 1060
....*....|....*....|
gi 1389908274 2703 QERQRKLMEEERKKLQAIMD 2722
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKD 1119
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1961-2725 |
1.28e-15 |
|
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: 84.64 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1961 NTEKSKQLLEsEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE 2040
Cdd:TIGR00618 161 KSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2041 AENERLkRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFhKASKE 2120
Cdd:TIGR00618 240 QSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2121 KADLESELKKLKGIADETQKSkLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQckaaQEEVERLKKKAED 2200
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ----HTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2201 ANKQKEKAEKEAEKQVVLAKEAAQkcTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQ 2280
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2281 KAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2360
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2361 VVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVEL-------ARVRIQMEELVKLKLKIEEENRRLMQK--DKD 2431
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKlqPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2432 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQ--------IAESNLAEQRALAEKILKEKMQAI--------QEATK 2495
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrehalsirVLPKELLASRQLALQKMQSEKEQLtywkemlaQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2496 LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgFQKSLEAERKRQLEASAEAEK---LKLRVKELSLAQ-TKAE 2571
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAALQTGAElSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2572 DEAKKFKKQADEVKAQLQRTE-KHTTEIV--VQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKemana 2648
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEaEIGQEIPsdEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK----- 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2649 QQEQIEQQKAELQQsflTEKGLLLKREKEVEGEKKRFEKQLEDEM-KKAKALKDEQERQ---RKLMEEERKKLQAIMDEA 2724
Cdd:TIGR00618 860 QLAQLTQEQAKIIQ---LSDKLNGINQIKIQFDGDALIKFLHEITlYANVRLANQSEGRfhgRYADSHVNARKYQGLALL 936
|
.
gi 1389908274 2725 V 2725
Cdd:TIGR00618 937 V 937
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
328-425 |
1.59e-15 |
|
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: 75.11 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1389908274 407 PEDVDVPHPDEKSIITYVS 425
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1526-1950 |
1.86e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.94 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1526 DDEKASEKLKEEERRKmAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHL 1605
Cdd:PRK02224 308 DAEAVEARREELEDRD-EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1606 KSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQ------------ 1673
Cdd:PRK02224 387 EEL-EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1674 --DEAERLRKQVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaq 1751
Cdd:PRK02224 466 hvETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL-- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1752 KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANT------AREEAEQELEIWRQkanealRLR 1825
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLRE------KRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 LQAEEEAQKKSHAQEEAE-KQKLEAERDakkrGKAEEAALKQKENAEKELDKqrkfaeqiaqqklsAEQECIRLKADFEH 1904
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFD----EARIEEAREDKERAEEYLEQ--------------VEEKLDELREERDD 678
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1389908274 1905 AEQQRGLLDNELQRLknevNSTEKQRKQLE---DELNKVRSEMDSLLQM 1950
Cdd:PRK02224 679 LQAEIGAVENELEEL----EELRERREALEnrvEALEALYDEAEELESM 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1597-1925 |
2.38e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 83.25 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1597 NIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQElrdRAAEAEKLRKAAQD-E 1675
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME---RERELERIRQEERKrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1676 AERLRKQ-VAEETQRKKnaedELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRVVEEVAQKSA 1754
Cdd:pfam17380 362 LERIRQEeIAMEISRMR----ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE-MEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1755 ATQLQTKAMSFSEQTtKLEESLKKEQGNVLKLQEEADKLKKQQKEantaREEAEqeleiwRQKANEALRLRLQAEEEAQK 1834
Cdd:pfam17380 437 VRRLEEERAREMERV-RLEEQERQQQVERLRQQEEERKRKKLELE----KEKRD------RKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1835 KSHAQEEAEKQKLEAERDAK--------KRGKAEEAALKQKENAEKeldkqrkfaEQIAQQKLSAEQECIRLKADFEHAE 1906
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERqkaiyeeeRRREAEEERRKQQEMEER---------RRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|....*....
gi 1389908274 1907 QQRGLLDNELQRLKNEVNS 1925
Cdd:pfam17380 577 MMRQIVESEKARAEYEATT 595
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
328-428 |
2.50e-15 |
|
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: 75.11 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 407
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1389908274 408 ED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1612-2199 |
2.51e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1612 EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKK 1691
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1692 NAEDELKrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQ-KSAATQLQTKAMSFSEQTT 1770
Cdd:PRK03918 249 SLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEyLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1771 KLEESLKKEQGNVLKLQEEADKLKKQQKEANtAREEAEQELEIWRQKANEALRLRLQ-AEEEAQKKSHAQEEAEKQKLEA 1849
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRlTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ERDAKKRgKAEEAALKQKENAEKELDKQRKfaeqiaqqklSAEQECIRLKADFEhaEQQRGLLdneLQRLKNEVNSTEKQ 1929
Cdd:PRK03918 404 EEEISKI-TARIGELKKEIKELKKAIEELK----------KAKGKCPVCGRELT--EEHRKEL---LEEYTAELKRIEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1930 RKQLEDELNKVRSEMDSLlqmkinaekasmvnteKSKQLLESEALKMKQLADEaarMRSVAEEAKKqrqIAEEEAARQRS 2009
Cdd:PRK03918 468 LKEIEEKERKLRKELREL----------------EKVLKKESELIKLKELAEQ---LKELEEKLKK---YNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2010 EAEKiLKEKLAAIN-EATRLKTEAEM--ALKAKEAENERLKRQAEEE-AYQRKLLEDQAAQHKQDIEEKITQLQTSSDS- 2084
Cdd:PRK03918 526 EYEK-LKEKLIKLKgEIKSLKKELEKleELKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEy 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2085 -ELGRQKNIVEETLKQKKVVEEEIhiikinfHKASKEKADLESELKKLKGIADETQKSklKAEEEAEKLKKLAAEEERRR 2163
Cdd:PRK03918 605 lELKDAEKELEREEKELKKLEEEL-------DKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELREEYLELSREL 675
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908274 2164 KEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2199
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4214-4252 |
4.02e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.02e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 4214 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNEIL 4252
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1519-2097 |
4.57e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEEE--------RRKMAEIQAELDK---QKQMAEA---HAKSVAKAEQEALELKMKMKEEASKR 1584
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDlherlnglESELAELDEEIERyeeQREQAREtrdEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1585 QDVAADAEKQKQNIQQELQHLKslsdqeiksknQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAE 1664
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLR-----------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1665 AEKLRKAAQDEAERLRKQVA---EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIR 1741
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADdleERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1742 QIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGNVlklqEEADKLKKQQK--EANTAREEAE--QELEIWRQK 1817
Cdd:PRK02224 410 AEDFLEELREERDELR---------EREAELEATLRTARERV----EEAEALLEAGKcpECGQPVEGSPhvETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1818 ANEALRLRLQAEEEaqkkshaqEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIR 1897
Cdd:PRK02224 477 VEELEAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1898 LKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNtEKSKQLLESEALKMK 1977
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1978 QLADEAARMRSVAEEAKKQRQiaeEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqR 2057
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER----R 700
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1389908274 2058 KLLEDQaAQHKQDIEEKITQLQTSS---DSELgRQKNIveETL 2097
Cdd:PRK02224 701 EALENR-VEALEALYDEAEELESMYgdlRAEL-RQRNV--ETL 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1561-2389 |
4.73e-15 |
|
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: 82.46 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1561 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKS--KNQQLEDALVSRRkieeEIHIIR 1638
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSR----LYSKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1639 IQLEKTTAHKAKSEAELQELRDRAAEAEKL----RKAAQD---EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQK 1711
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIieaqRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1712 QRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE--VAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklQEE 1789
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEElrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1790 ADKLKKQQKEANTAREEAEQELEIWRQKANE-ALRLRLQAE---EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1865
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQDEnlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1866 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQqrgLLDNELQRLKNevnsTEKQRKQLEDELNKVRSEMD 1945
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEK----NEDQLKIITMELQKKSSELE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1946 SLLQMKINAEkasmVNTEKSKQLLESEalkmKQLADEAARMRSVAEEAK-KQRQIAEEEAARQRSEAEKILKEKLAAINE 2024
Cdd:pfam05483 395 EMTKFKNNKE----VELEELKKILAED----EKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2025 ATRLKTEAEMAlkaKEAENERLKRQAEEEAYQRKLLEDQaaqhkqdieeKITQLQTSSDSELGRQKNIVEETLKQKKVVE 2104
Cdd:pfam05483 467 EHYLKEVEDLK---TELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2105 EEIHIIKinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQC 2184
Cdd:pfam05483 534 KQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2185 KAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKedvLAQEKLRDEFENAKKLAQEA 2264
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLEEVEKAKAIADEA 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2265 EKAkekaekeaallrQKAEEAEKQKKAAENEA-AKQAKAQNDtekqrkeaeeeaarraaaeaaalKQKQQADAEMSKHKK 2343
Cdd:pfam05483 688 VKL------------QKEIDKRCQHKIAEMVAlMEKHKHQYD-----------------------KIIEERDSELGLYKN 732
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1389908274 2344 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVND 2389
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
328-428 |
6.05e-15 |
|
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: 73.91 E-value: 6.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 407
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1389908274 408 ED-VDVPHPDEKSIITYVSSLY 428
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
213-313 |
6.65e-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: 73.49 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNKHLVK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 284
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1389908274 285 KLVNIRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2459-2791 |
1.15e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.52 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2459 EETARQRQIAESNLAEqralAEKILKEkmqaiqeatkLKAEAEKLQKQKDQAQEtAKRLQEDKQQIQQRL--------DK 2530
Cdd:COG1196 175 EEAERKLEATEENLER----LEDILGE----------LERQLEPLERQAEKAER-YRELKEELKELEAELlllklrelEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2531 ETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQS 2610
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---DIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2611 TREADDLKsaiADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLE 2690
Cdd:COG1196 317 RLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2691 DEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKK-RLEQEKQLAEENKKLREQLQT 2769
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEaELEEEEEALLELLAELLEEAA 473
|
330 340
....*....|....*....|..
gi 1389908274 2770 FEISSKTVSQTKESQTVSVEKL 2791
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLL 495
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
797-987 |
1.27e-14 |
|
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: 75.95 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 797 QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAF 876
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 877 TAALQTQWSWLLQLCCCIETHLKENTAHFQFFTDVKEAEEKLKKMQDTMKRKYTCDrsiTVTRLEDLLQDAADEKEQLAE 956
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1389908274 957 FKTNLEALKRRAKTVIQLKPRNPTTPLKGKM 987
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1655-2155 |
1.62e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1655 LQELRDRAAEA----EKLRKAAQDEAERLRKQVAEetqrkKNAEDELKRKSDAEKEAAKQKqralDDLQKYKMQAEEAER 1730
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLNGLESELAELD----EEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1731 RMKQAE------EEKIRQIRVVEEVAQKSAAtqlqTKAMSFSEQTTkLEESLKKEQGNVLKLQEE--------------A 1790
Cdd:PRK02224 235 TRDEADevleehEERREELETLEAEIEDLRE----TIAETEREREE-LAEEVRDLRERLEELEEErddllaeaglddadA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1791 DKLKKQQKEANTAREEAEQELEIWRQKA----NEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------ 1857
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAqahnEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRReeieel 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1858 -KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAE------------------------------ 1906
Cdd:PRK02224 390 eEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkcpecgqpvegsphvet 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1907 -----QQRGLLDNELQRLKNEVNSTEKQRKQLEDeLNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESEALKMKQLAD 1981
Cdd:PRK02224 470 ieedrERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL----IAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1982 EAARMRSVAEEAKKQRQIAEEEAARQRSEAeKILKEKLAAINEA-TRLKTEAEMALKAKEAENERLKRQAEEEAYQRKll 2060
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEDEIERLREKREALAEL-- 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2061 EDQAAQHKQDIEEKITQLQTSSDSELgrqkniVEETLKQKKVVEEEIhiikinfhkaskekADLESELKKLKGIADETQK 2140
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEAR------IEEAREDKERAEEYL--------------EQVEEKLDELREERDDLQA 681
|
570
....*....|....*
gi 1389908274 2141 SKLKAEEEAEKLKKL 2155
Cdd:PRK02224 682 EIGAVENELEELEEL 696
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
330-425 |
1.97e-14 |
|
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: 72.03 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 408
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1389908274 409 DVDVPHPDEKSIITYVS 425
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3231-3269 |
2.54e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.66 E-value: 2.54e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 3231 FLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEIHERL 3269
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1786-2609 |
5.02e-14 |
|
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: 79.39 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1786 LQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQaeeEAQKKSHAQEEAEKQKLEAERDAKKRGKAE----E 1861
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID-LQTKLQ---EMQMERDAMADIRRRESQSQEDLRNQLQNTvhelE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1862 AALKQKENAEKELDKQrkfAEQIAQQKLSAE---QECIRLKADFEHAEQQR----------------GLLDNELQRLKNE 1922
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQ---IEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdsmstmhfrslgSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 2002
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2003 EAARQRSEAEKILKEKLAAINEatrLKTEAEMALKAKEAENERLKRQ---AEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 2079
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2080 TSSDSelgRQKNIVEETLKQKKVVEEEIHiIKINFHKASKEKADLESELKKLKGIAdETQKSKLKAEEEAEklkklaAEE 2159
Cdd:pfam15921 384 ADLHK---REKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQ------MAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2160 ERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANkqkekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSK 2239
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE-----------------RTVSDLTASLQEKERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2240 NKEDVlaqeKLRDEFEnakklaqeaekakekaEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDtekqrkeaeeeaar 2319
Cdd:pfam15921 516 NAEIT----KLRSRVD----------------LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD-------------- 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2320 raaAEAAALKQKQQADAEM-SKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2398
Cdd:pfam15921 562 ---KVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LE 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2399 VELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL--LAEEAEKMK-SLAEEAGRLSVEAEETARQRQIAESNLAEQ 2475
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2476 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE---DKQQIQQRLDKETEGFQKSLEAERKRQLEASAE 2552
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2553 AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQ-KLETQRLQ 2609
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1941-2782 |
5.65e-14 |
|
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: 79.34 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1941 RSEMDSLL-QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAArmrSVAE-EAKKQRQIAEEEAARQRSE-AEKILKE 2017
Cdd:TIGR02169 119 LSEIHDFLaAAGIYPEGYNVVLQGDVTDFISMSPVERRKIIDEIA---GVAEfDRKKEKALEELEEVEENIErLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2018 KlaaINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ---HKQDIEEKITQLqTSSDSELGRQKNIVE 2094
Cdd:TIGR02169 196 K---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAierQLASLEEELEKL-TEEISELEKRLEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2095 ETLKQ-----KKVVEEEIHIIKinfhkasKEKADLESELKKLKGIADEtqkSKLKAEEEAEKLKKLAAEEERRRKEAEEK 2169
Cdd:TIGR02169 272 QLLEElnkkiKDLGEEEQLRVK-------EKIGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2170 VKRItaaeEEAARQCKAAQEEVERLKKKAEDAnkqkekaekeaekqvvlakeaaqkctaaEQKAQDVLSKNKEDVLAQEK 2249
Cdd:TIGR02169 342 EREI----EEERKRRDKLTEEYAELKEELEDL----------------------------RAELEEVDKEFAETRDELKD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2250 LRDEFEnakKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAArraaaeaaalk 2329
Cdd:TIGR02169 390 YREKLE---KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW----------- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2330 QKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQElQRVKGEVNDAFKQKSQVEVELARVRIQME 2409
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSVG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2410 ELVKLKLKIEEENRR---LMQKDKDSTQ--KLLAEEA---------EKMKSLAEEAGRLS-----------VEAEETAR- 2463
Cdd:TIGR02169 535 ERYATAIEVAAGNRLnnvVVEDDAVAKEaiELLKRRKagratflplNKMRDERRDLSILSedgvigfavdlVEFDPKYEp 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2464 ------QRQIAESNLAEQRALAEKI--------LKEKMQAIQE-ATKLKAEAEKLQKQKDQAQETAKRLQEdkqqiqqrL 2528
Cdd:TIGR02169 615 afkyvfGDTLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGgSRAPRGGILFSRSEPAELQRLRERLEG--------L 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2529 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtteivvQKLETQRl 2608
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK- 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2609 qstREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQQSFLTEKGLLLK-------------RE 2675
Cdd:TIGR02169 758 ---SELKELEARIEEL------------------EEDLHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearlRE 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2676 KEVEGEKKRFEKQ-LEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEK 2754
Cdd:TIGR02169 817 IEQKLNRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
890 900
....*....|....*....|....*...
gi 1389908274 2755 QLAEENKKLREQLQTFEISSKTVSQTKE 2782
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKA 924
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1424-2085 |
1.46e-13 |
|
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: 77.91 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1424 LREQLTDEKKLLGEIEKNKDKIDdchknakayiDSVKDYEFQILTYKALQDPIASPLKKPKMECASddiiqeyvnLRTRY 1503
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLE----------GESTDLQEQIAELQAQIAELRAQLAKKEEELQA---------ALARL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1504 SELMTLTNQYIKFIIDAQRRLED------DEKASEKLKEEERRKMAE----IQAELDKQKQMAEAHAKSVAKAEQEALEL 1573
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQISElqedleSERAARNKAEKQRRDLGEeleaLKTELEDTLDTTAAQQELRSKREQEVTEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1574 KMKMKEEaSKRQDVAADAEKQKQNiqqelQHLKSLSDQ-----EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHK 1648
Cdd:pfam01576 333 KKALEEE-TRSHEAQLQEMRQKHT-----QALEELTEQleqakRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1649 -AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEE 1727
Cdd:pfam01576 407 rKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1728 AERRMKQAEEEK--IRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEE---SLKKEQGNVLKLQEEADKLKKQQKEANT 1802
Cdd:pfam01576 487 LSTRLRQLEDERnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1803 AREEAEQELEIWRQKANEAL------RLRLQAEEEAQKKSH---AQEEAEKQKLEAERD---AKKRGKAEEA-----ALK 1865
Cdd:pfam01576 567 AYDKLEKTKNRLQQELDDLLvdldhqRQLVSNLEKKQKKFDqmlAEEKAISARYAEERDraeAEAREKETRAlslarALE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1866 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA----EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVR 1941
Cdd:pfam01576 647 EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSkralEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALK 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1942 SEMDSLLQMKINAekasmvNTEKSKQLLEsEALKMKQLADEAARMRSVAEEAKKQRQIAEEE-------AARQRSEAEKI 2014
Cdd:pfam01576 727 AQFERDLQARDEQ------GEEKRRQLVK-QVRELEAELEDERKQRAQAVAAKKKLELDLKEleaqidaANKGREEAVKQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2015 LK--------------EKLAAINEATRLKTEAEMALKAKEAE----------NERLKRQAEEEayqRKLLEDQAA----- 2065
Cdd:pfam01576 800 LKklqaqmkdlqreleEARASRDEILAQSKESEKKLKNLEAEllqlqedlaaSERARRQAQQE---RDELADEIAsgasg 876
|
730 740
....*....|....*....|....*
gi 1389908274 2066 -----QHKQDIEEKITQLQTSSDSE 2085
Cdd:pfam01576 877 ksalqDEKRRLEARIAQLEEELEEE 901
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1494-2078 |
1.58e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNLRTRYSELMTLtnqyikfiiDAQRRLEDDEKASEKLKEEERRkmaeIQAELDKQKQMAEAHAKSVAKAEQEALEL 1573
Cdd:COG4913 262 ERYAAARERLAELEYL---------RAALRLWFAQRRLELLEAELEE----LRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1574 kmkmkeeaskRQDVAADAEKQKQNIQQELQHLKSLSDqEIKSKNQQLEDALVS-RRKIEEEIHIIRIQLEKTTAHKAKSE 1652
Cdd:COG4913 329 ----------EAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD---DLqkykMQAEEAE 1729
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPfvgEL----IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1730 RRMKQAEEEKIRQIR---VVEEVAQKSAA-----TQLQTKAmsfseQTTKLEESLKKEQGNVLKLQEEADKLkkqQKEAN 1801
Cdd:COG4913 474 ERWRGAIERVLGGFAltlLVPPEHYAAALrwvnrLHLRGRL-----VYERVRTGLPDPERPRLDPDSLAGKL---DFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1802 TAREEAEQEL-----------------------------------EIWRQKA----------NEALRLRLQAEEEAQKKS 1836
Cdd:COG4913 546 PFRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRirsryvlgfdNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1837 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRGLLDNEL 1916
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1917 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEkasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1996
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE-------DLARLELRALLEERFAAALGDAVERELRENLEER 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1997 RQIAEEEAARQRSEAEKILKE--------------KLAAINEA----TRLKTEaemALKAKEAE-NERLKRQAEEEayqR 2057
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEYlallDRLEED---GLPEYEERfKELLNENSIEF---V 848
|
650 660
....*....|....*....|.
gi 1389908274 2058 KLLEDQAAQHKQDIEEKITQL 2078
Cdd:COG4913 849 ADLLSKLRRAIREIKERIDPL 869
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
231-310 |
1.66e-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: 69.54 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 231 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 302
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1389908274 303 LGLIWTII 310
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3895-3933 |
1.93e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 1.93e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 3895 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3933
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1512-2202 |
2.31e-13 |
|
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: 77.47 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1512 QYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE-----EASK--R 1584
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvhelEAAKclK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1585 QDVAADAEKQKQNIQQ-ELQHLKSLsdQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKS----EAELQELR 1659
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmMLSHEGVL--QEIRSILVDFEEA--SGKKIYEHDSMSTMHFRSLGSAISKIlrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1660 DR----AAEAEKLRKAAQDEAERLRKQ------------------VAEETQRKKNAEDELKRKSDAEKEAAKQKQ----R 1713
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQhqdrieqliseheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1714 ALDDLQKYKMQAEEAERRMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKL 1793
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELE-KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1794 KKQQKEA------------NTAREEAEQELEIWRQkanEALRLRLqaeeeaqkKSHAQEEAEKQKleaerdAKKRGKAEE 1861
Cdd:pfam15921 397 KEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRL---EALLKAM--------KSECQGQMERQM------AAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1862 AALKQKENAEKELDKQ--RKFAEQIAQQKL---SAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDE 1936
Cdd:pfam15921 460 LEKVSSLTAQLESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1937 LNKVRSemdslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQrqiAEEEAARQRSEAE--KI 2014
Cdd:pfam15921 540 GDHLRN-----VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ---LEKEINDRRLELQefKI 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2015 LKEKL-AAINEATRLKTEAEM-ALKAKEAENERLKRQaeeeayqrklledqaaqhkQDIEEKITQLQtssdselgrqkNI 2092
Cdd:pfam15921 612 LKDKKdAKIRELEARVSDLELeKVKLVNAGSERLRAV-------------------KDIKQERDQLL-----------NE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2093 VEETLKQKKVVEEEIHIIKINFHKASKEkadLESELKKLKGiadETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 2172
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEE---METTTNKLKM---QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
730 740 750
....*....|....*....|....*....|
gi 1389908274 2173 ITAAEEeaarQCKAAQEEVERLKKKAEDAN 2202
Cdd:pfam15921 736 ITAKRG----QIDALQSKIQFLEEAMTNAN 761
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
206-312 |
2.46e-13 |
|
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: 69.23 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 206 ADERDrvqKKTFTKWVNKHLVKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 277
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908274 278 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 312
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
215-316 |
2.57e-13 |
|
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: 69.19 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 215 KTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2057-2772 |
2.68e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2057 RKLLEDQA--AQHKQDIEEKITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHI-IKINFHKASKEKADLESELKKLKG 2133
Cdd:TIGR02168 158 RAIFEEAAgiSKYKERRKETERKLERTREN-LDRLEDILNELERQLKSLERQAEKaERYKELKAELRELELALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2134 IADETQKSKLKAEEEAEKLKKLAAEEERrrkeAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAE 2213
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQE----LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2214 KQVVLAKEAAQKCTAAEQKAQDVL-----SKNKEDVLAQEK--LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAE 2286
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAeelaeLEEKLEELKEELesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2287 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQadAEMSKHKKEAEQALQQKSQVEKELTVVKLQL 2366
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2367 DETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKL---------KLKIEEENRRLMQKD-KDSTQKL 2436
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEGYEAAIEAAlGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2437 LAEEAEKMKSLAE-----EAGRLSVEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLK-------------- 2497
Cdd:TIGR02168 551 VVENLNAAKKAIAflkqnELGRVTFLPLDSIKGTEI-QGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvd 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2498 --AEAEKLQKQKD----------------------------QAQETAKRLQEDKQQIQQRLDKETEGfQKSLEAERKRQL 2547
Cdd:TIGR02168 630 dlDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAEL-EKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2548 EASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQklETQRLQSTREADDLKSAIADLEEE 2627
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE--IEELEERLEEAEEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2628 RKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKR---EKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2704
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaatERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2705 RQRKLmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL---REQLQTFEI 2772
Cdd:TIGR02168 867 LIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLEV 936
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1512-1808 |
4.11e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.32 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1512 QYIKFIIDAQRRLEDDEKasEKLKE-EERRKMAEI----QAELDKQKQMAEAHAKSVAKAEQEALELKM---KMKEEASK 1583
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKE--EKAREvERRRKLEEAekarQAEMDRQAAIYAEQERMAMERERELERIRQeerKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1584 RQDVAADAEKQKqniqqELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELR---- 1659
Cdd:pfam17380 367 QEEIAMEISRMR-----ELERLQ----MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrev 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1660 -----DRAAEAEKLRKAA-----------QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1723
Cdd:pfam17380 438 rrleeERAREMERVRLEEqerqqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1724 QAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQTTKLeESLKKEQgnvlklqeeadKLKKQQKEAN 1801
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRL-EAMERER-----------EMMRQIVESE 585
|
....*..
gi 1389908274 1802 TAREEAE 1808
Cdd:pfam17380 586 KARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1422-2079 |
4.12e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1422 RALREQLTDEKK--LLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIAspLKKPKMECASDDIIQEYVNL 1499
Cdd:TIGR02168 216 KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1500 RTRYSELmtltNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE 1579
Cdd:TIGR02168 294 ANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1580 EASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKttAHKAKSEAELQELR 1659
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1660 DRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKS-----------------DAEKEAAKQKQR--------- 1713
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsEGVKALLKNQSGlsgilgvls 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1714 --------------------------------------------------ALDDLQKYKMQAEEAERRMKQAE------- 1736
Cdd:TIGR02168 527 elisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflPLDSIKGTEIQGNDREILKNIEGflgvakd 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1737 ----EEKIR--------QIRVVEEVAQksaATQLQTK-------------------AMSFSEQTT------------KLE 1773
Cdd:TIGR02168 607 lvkfDPKLRkalsyllgGVLVVDDLDN---ALELAKKlrpgyrivtldgdlvrpggVITGGSAKTnssilerrreieELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1774 ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-------------LRLRLQAEEEAQKKSHAQE 1840
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarleaeveqLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1841 EAEKQKLEAERDAKKRGKAEEAALKQK---------------ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1905
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1906 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEA-- 1983
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEELre 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1984 --ARMRSVAEEAKKQR-QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKAKEAENERLKRQAEEEAYQRKLL 2060
Cdd:TIGR02168 923 klAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEELKER 1001
|
810
....*....|....*....
gi 1389908274 2061 EDQAAQHKQDIEEKITQLQ 2079
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2085-2791 |
4.63e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.25 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2085 ELGRQKNIVEETLKQKKVVEEE---IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLaaeeer 2161
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEaagISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2162 rrkeaeekvKRITAAEEEA-----ARQCKAAQEEVERLKKKAedankqkekaekeaekqvvlaKEAAQKCTAAEQKAQDV 2236
Cdd:TIGR02168 216 ---------KELKAELRELelallVLRLEELREELEELQEEL---------------------KEAEEELEELTAELQEL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2237 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQakaqndtekqrkeaeee 2316
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL----------------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2317 aarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQ 2396
Cdd:TIGR02168 329 -----------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2397 VEVELARVRIQMEELvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQR 2476
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2477 ALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------KETEGFQKSLEA--------- 2541
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqav 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2542 ------ERKRQLEASAEAEKLKLRVKELSLAQ-TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvQKLETQRLQSTREA 2614
Cdd:TIGR02168 551 vvenlnAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKL--RKALSYLLGGVLVV 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2615 DDLKSAIADLEEERKKL--------------------KKEAEELQRKSKEMANAQQE-----------QIEQQKAELQQS 2663
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKieeleekiaelEKALAELRKELE 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2664 FLTEKGLLLKREKE--------VEGEKKRFEK---QLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE 2732
Cdd:TIGR02168 709 ELEEELEQLRKELEelsrqisaLRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2733 EEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2791
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1772-2200 |
5.18e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1772 LEESLKKEQGNVLKLQEEADKLKKQQ-KEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEK-QKLEA 1849
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLD-NELQRLKNEVNSTEK 1928
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1929 QRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEAL---------------------------------- 1974
Cdd:COG4717 207 RLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1975 -------KMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 2047
Cdd:COG4717 286 lallfllLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2048 RQAEEEAYQRKLLEDQA------------AQHKQDIEEKITQLQTSSDSELGRQKNIVEETlkQKKVVEEEIHIIKINFH 2115
Cdd:COG4717 365 LEELEQEIAALLAEAGVedeeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2116 KASKEKADLESELKKLkgiadETQKSKLKAEEEAEKLKklaaeeerrrKEAEEKVKRITAAEEEAARqCKAAQEEVERLK 2195
Cdd:COG4717 443 ELEEELEELREELAEL-----EAELEQLEEDGELAELL----------QELEELKAELRELAEEWAA-LKLALELLEEAR 506
|
....*
gi 1389908274 2196 KKAED 2200
Cdd:COG4717 507 EEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1513-2149 |
5.33e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.87 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1513 YIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkeeaskrqdvaadae 1592
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE------------------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1593 kqkqniqqelqhlkslsdqEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKaksEAELQELRDRAAEAEKLRKAA 1672
Cdd:PRK03918 235 -------------------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL---KKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1673 qDEAERLRKQVAEETQRKKNAEDELKRKSdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevaqk 1752
Cdd:PRK03918 293 -EEYIKLSEFYEEYLDELREIEKRLSRLE----EEINGIEERIKELEEKEERLEELKKKLKELEKRLEE----------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1753 saatqLQTKAMSFSEQTTKLE--ESLKKEQGNvlklqEEADKLKKQQKEANTAREEAEQELEIWRQKANE------ALRL 1824
Cdd:PRK03918 357 -----LEERHELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1825 RLQAEEEAQKK----------SHAQEEAEKQKLEAERDAKKRGKAEEA---ALKQKENAEKELDKQRKFA--EQIAQQKL 1889
Cdd:PRK03918 427 AIEELKKAKGKcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKerkLRKELRELEKVLKKESELIklKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1890 SAEQECirLKADFEHAEQQRglldNELQRLKNEVNSTEKQRKQLEDELNkvrsemdsllqmKINAEKASMVNTEKSKQLL 1969
Cdd:PRK03918 507 ELEEKL--KKYNLEELEKKA----EEYEKLKEKLIKLKGEIKSLKKELE------------KLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1970 ESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQ 2049
Cdd:PRK03918 569 EEE---LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2050 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKinfhKASKEKADLESELK 2129
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE----KAKKELEKLEKALE 721
|
650 660
....*....|....*....|
gi 1389908274 2130 KLKGIADETQKSKLKAEEEA 2149
Cdd:PRK03918 722 RVEELREKVKKYKALLKERA 741
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3638-3674 |
6.30e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 6.30e-13
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 3638 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMAK 3674
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1498-2100 |
6.42e-13 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 75.56 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1498 NLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDkqkqmAEAHAKSVAKAEQEALELKMKM 1577
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----ALAVAEKAGQAEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1578 KEEASKRQDVAAdaekqkqniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElqe 1657
Cdd:pfam07111 127 AEMVRKNLEEGS---------QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE--- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1658 lrdraaeaeklrkaAQDEAERLRKQVAE------------ETQRKKNAEDELKRKSDAEKEAAKQK--------QRALDD 1717
Cdd:pfam07111 195 --------------AQKEAELLRKQLSKtqeeleaqvtlvESLRKYVGEQVPPEVHSQTWELERQElldtmqhlQEDRAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1718 LQK---------------YKMQAEEAERRMKQA---EEEKIRQIR-VVEEVAQKSAATQLQTKAmsfseQTTKLEESLKK 1778
Cdd:pfam07111 261 LQAtvellqvrvqslthmLALQEEELTRKIQPSdslEPEFPKKCRsLLNRWREKVFALMVQLKA-----QDLEHRDSVKQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1779 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKAnEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1858
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSA-KGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1859 A---------EEAALK------------QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD----FEHAEQQRGLLD 1913
Cdd:pfam07111 415 IwlettmtrvEQAVARipslsnrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADlsleLEQLREERNRLD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1914 NELQR----LKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKinaeKASMVNTeksKQLLESEALKMKQLADEAARMRsv 1989
Cdd:pfam07111 495 AELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA----QESLASV---GQQLEVARQGQQESTEEAASLR-- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1990 aEEAKKQRQIAEEEAARQRSEAEKILKEKLA----AINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAA 2065
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSdtkrRLNEARREQAKAVVSLRQIQHRATQEKERNQE---LRRLQDEARK 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908274 2066 QHKQDIEEKItqlqtssdSELGRQKNIVEETLKQK 2100
Cdd:pfam07111 642 EEGQRLARRV--------QELERDKNLMLATLQQE 668
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1529-2154 |
1.02e-12 |
|
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: 74.76 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1529 KASEKLK--EEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQEALELKMKMKEEASKrqdvaadaekqkqniqqeLQHL 1605
Cdd:pfam05483 166 RSAEKTKkyEYEREETRQVYMDLNNNiEKMILAFEELRVQAENARLEMHFKLKEDHEK------------------IQHL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1606 KSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEkttahkakseaelqELRDRAAEAEKLRKAAQDEAERLRKQVAE 1685
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE--------------ESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1686 ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkmqAEEAERRMKQAEEEKIRQIRVVEEVaqKSAATQLQTKAMSF 1765
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---TEEKEAQMEELNKAKAAHSFVVTEF--EATTCSLEELLRTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1766 SEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE-----AEQELEIWRQKANEALRLRLQAEEEAQKKSHAQE 1840
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1841 EAEKQKLEAERDAKKrgKAEEAALKQKENAEKELDKQR-KFAEQIAQ-QKLSAEQECIRLKAD---FEHAEQQRGLLDNE 1915
Cdd:pfam05483 449 EKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKlKNIELTAHcDKLLLENKELTQEASdmtLELKKHQEDIINCK 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1916 LQ--RLKNEVNSTEKQRKQLEDELNKVRSEmdslLQMKINAEKASMVNTEKSKQLLESEALK----MKQLADEAARMRSV 1989
Cdd:pfam05483 527 KQeeRMLKQIENLEEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1990 AEEAKKQRQIAEEE--AARQRSEAE-------KILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQA-EEEAYQRKL 2059
Cdd:pfam05483 603 IENKNKNIEELHQEnkALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKA 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2060 LEDQAAQHKQDI----EEKITQLQTSSDSELGRQKNIVEETlkqkkvvEEEIHIIKINFHKASKEKADLESELKKLKGIA 2135
Cdd:pfam05483 683 IADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKIIEER-------DSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
650
....*....|....*....
gi 1389908274 2136 DETQKSKLKAEEEAEKLKK 2154
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKM 774
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3562-3600 |
1.32e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.66 E-value: 1.32e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 3562 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPELHEKL 3600
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2475-2768 |
1.38e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.39 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2475 QRALAEKILKEKMQaiqeatklKAEAEKLQKQKDQ-AQETAKR--LQEDKQQIQQRLDKetegfQKSLEAERKR-QLEAS 2550
Cdd:pfam17380 281 QKAVSERQQQEKFE--------KMEQERLRQEKEEkAREVERRrkLEEAEKARQAEMDR-----QAAIYAEQERmAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2551 AEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHttEIVVQKLETQRLQSTREADdlksaiadleeERKK 2630
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN--ERVRQELEAARKVKILEEE-----------RQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2631 LKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkRFEKQLEDEMKKAKALKDEQERQRKLM 2710
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2711 EEERKKLQAIMDEavRKQKEAEEEMKNKQREMDVLDKKRL---EQEKQLAEENKKLREQLQ 2768
Cdd:pfam17380 491 EQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQQEME 549
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2249-2794 |
1.49e-12 |
|
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: 74.37 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2249 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEaarraaaeaaaL 2328
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN-----------L 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQKSQVEKELtvvKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2408
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EELVKlklkieeenrrlmqkdkdSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRalaeKILKEKMQ 2488
Cdd:pfam05483 362 EELLR------------------TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2489 AIQEATKLKAEAEKLQKQKdqaQETAKRLQEDKQQI-------------QQRLDKETEGFQKSLEAERKRQLEASAEAEK 2555
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKE---QELIFLLQAREKEIhdleiqltaiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2556 LKLRVKELS-------LAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvQKLETQRLQSTREADDLKSAIADLEEER 2628
Cdd:pfam05483 497 LLLENKELTqeasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDKSEENA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2629 KKLKKEAEELQ-------------RKSKEMANAQQEQIEQQKAELQQSFLTEKGLLL-------KREKEVEGEKKRFEKQ 2688
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvnKLELELASAKQKFEEI 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2689 LEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENK------K 2762
Cdd:pfam05483 656 IDNYQKEIEDKKISEEK----LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDselglyK 731
|
570 580 590
....*....|....*....|....*....|...
gi 1389908274 2763 LREQLQ-TFEISSKTVSQTKESQTVSVEKLVAV 2794
Cdd:pfam05483 732 NKEQEQsSAKAALEIELSNIKAELLSLKKQLEI 764
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2905-2943 |
1.74e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.74e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 2905 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPELHDRL 2943
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1543-2003 |
2.56e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1543 AEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQELQHLKSLSDQeiKSKNQQLED 1622
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1623 ALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD 1702
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1703 AEKEAAKQKQRALDDLQKYKMQAEEAERRmkQAEEEKIRQIRVV------------EEVAQKSAATQLQTKAMSFSEQTT 1770
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEA--AALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1771 KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAE 1850
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1851 RDAKKRGKAEEAALKQKENAEKELDKQRKFaEQIAQQKLSAEQECIRLKADFEHAEQQRGL--LDNELQRLKNEVNSTEK 1928
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 1929 QRKQLEDELNKVRSEMDSLLQMKINAEKasmvnteksKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEE 2003
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELAEL---------LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4484-4522 |
4.06e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.06e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 4484 LLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMVDRI 4522
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
208-307 |
4.26e-12 |
|
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: 65.91 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRvQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 279
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1389908274 280 KHRQVKLVNIRNDDIADGNPKLTLGLIW 307
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
330-429 |
4.30e-12 |
|
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: 65.44 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSN---QENLEQAFSVAERE-LGVTKLL 405
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1389908274 406 DPEDVdVPHPDEKSIITYVSSLYD 429
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1653-2088 |
1.10e-11 |
|
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: 71.91 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 AELQELRDRAAEAEKLRKAAqdeaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkMQAeeaerrM 1732
Cdd:COG3096 278 NERRELSERALELRRELFGA-------RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLV-QTA------L 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1733 KQAEeeKIrqIRVVEEVAQKSAATQLQtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ----------QKEANT 1802
Cdd:COG3096 344 RQQE--KI--ERYQEDLEELTERLEEQ------EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyqqaldvQQTRAI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1803 AREEAEQELEiwrqKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqRKFAE 1882
Cdd:COG3096 414 QYQQAVQALE----KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV---CKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1883 QI-AQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdELNKvrsemdsllQMKINAEKASMVN 1961
Cdd:COG3096 487 EVeRSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ---------RIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1962 TEKSKQllesEAlkmkQLADEAARMRSVAEEAKKQRQiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 2041
Cdd:COG3096 557 ELLAEL----EA----QLEELEEQAAEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE 627
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908274 2042 ENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR 2088
Cdd:COG3096 628 VTAAMQQLLERER-EATVERDELAARKQALESQIERLSQPGGAEDPR 673
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1670-1894 |
1.22e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 69.49 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLqKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1749
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1750 AQKSAAtqlqtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqeleiwRQKANEAlrlrlQAE 1829
Cdd:TIGR02794 125 KAKQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK------KKAEAEA-----KAK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 1830 EEAQKKshAQEEAEKQKLEAerdAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIAQQKLSAEQE 1894
Cdd:TIGR02794 183 AEAEAK--AKAEEAKAKAEA---AKAKAAAEAAAKAEAEAAAAaAAEAERKADEAELGDIFGLASG 243
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1514-2074 |
1.34e-11 |
|
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: 71.29 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1514 IKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQ---MAEAHAKSVAKAEQEALELKMK----MKEEASKRQD 1586
Cdd:pfam05483 259 LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKALEEDLQIATKticqLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1587 VAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1666
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1667 KLrkaaQDEAERLRKqVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeEAERRMKQAEEEKIRQIrvv 1746
Cdd:pfam05483 419 KL----LDEKKQFEK-IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNI--- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1747 eEVAQKSAATQLQTKAMsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKanealrLRL 1826
Cdd:pfam05483 489 -ELTAHCDKLLLENKEL--TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE------FIQ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1827 QAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAlkqkENAEKELDKQRKFAEQIAQqklsaeqecirlkadfehae 1906
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKNIEELHQ-------------------- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1907 qqrglldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM---KINAEKASMVNTEKSKQLLESEALKMKQLADEA 1983
Cdd:pfam05483 616 --------ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1984 ARMRSVAEEaKKQRQIAEEEA--ARQRSEAEKILKEKLAAI-------NEATRLKTEAEMALKAKEAENERLKRQAEEEA 2054
Cdd:pfam05483 688 VKLQKEIDK-RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
570 580
....*....|....*....|
gi 1389908274 2055 YQRKLLEDQAAQHKQDIEEK 2074
Cdd:pfam05483 767 EEKEKLKMEAKENTAILKDK 786
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2981-3019 |
1.36e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.36e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 2981 FLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADMNKKL 3019
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2329-2559 |
1.37e-11 |
|
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: 69.79 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2408
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EELVKLKLKIEEENR---RLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKE 2485
Cdd:COG4942 107 AELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA----ELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2486 KMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2559
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
330-428 |
1.40e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 63.91 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 330 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 409
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1389908274 410 VdVPHPDEKSIITYVSSLY 428
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3971-4009 |
1.45e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.45e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 3971 LLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKETHERL 4009
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2091-2759 |
2.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.86 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2091 NIVEETLKQKKVVEEEIHIIKinFHKASKEKADLESELKKLKgiadETQKSKLKAEEEAEKLKKlaaEEERRRKEAEEKV 2170
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIK---EKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2171 KRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV--LSKNKEDVLAQE 2248
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2249 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeaEEEAARRAAAEAAAL 2328
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK--RLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQqadAEMSKHKKEAEqalqqksqvEKELTVVKLQLDETDKQKVLLDQELQRVKGEvndafkqKSQVEVELARVRIQM 2408
Cdd:PRK03918 368 KAKK---EELERLKKRLT---------GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EELVKLKLKIEEENRRLMQKDKdstQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRAL-AEKILKEKM 2487
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2488 QAIQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDketegfqkslEAERKRQLEASAEAEKLKLRVKELSLAQ 2567
Cdd:PRK03918 506 KELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK----------ELEKLEELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2568 TKAEDEAKKFkKQADEVKAQLQRTEKHTTEIVVQKLETQRLQST-READDLKSAIADLeeerkklkkeaeelqRKSKEMA 2646
Cdd:PRK03918 575 LLKELEELGF-ESVEELEERLKELEPFYNEYLELKDAEKELEREeKELKKLEEELDKA---------------FEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2647 NAQQEQIEQQKAELQQSFLTE-----KGLLLKREKEVEGEKKRFEkQLEDEMKKAKALKDEQERQRKLMEEERKKLqaim 2721
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKEL---- 713
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908274 2722 dEAVRKQKEAEEEMKNKQREMDVLDKKR-LEQEKQLAEE 2759
Cdd:PRK03918 714 -EKLEKALERVEELREKVKKYKALLKERaLSKVGEIASE 751
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1903-2599 |
2.80e-11 |
|
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: 70.05 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1903 EHAEQQrglLDNELQRLKNEVNSTEKQRKQLEDELNKvRSEMDSLLQMKINAEKASmVNTEKSKQLLESEalKMKQLADE 1982
Cdd:TIGR04523 32 DTEEKQ---LEKKLKTIKNELKNKEKELKNLDKNLNK-DEEKINNSNNKIKILEQQ-IKDLNDKLKKNKD--KINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1983 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEaemaLKAKEAENERLKRQAEEEAYQRKLLED 2062
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2063 QaaqhKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKASKEKADLESELKKLKGIADETQKSK 2142
Cdd:TIGR04523 181 E----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2143 LKAEEEAEKLKKlaaeeerrrkeaeekvkritaaeeeaarQCKAAQEEVERLKKKAEDANKQkekaekeaekqvvLAKEA 2222
Cdd:TIGR04523 256 NQLKDEQNKIKK----------------------------QLSEKQKELEQNNKKIKELEKQ-------------LNQLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2223 AQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA---------------KKLAQEAEKAKEKAEKEAALLRQKAEEAEK 2287
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2288 QKKaaENEAAKQAKAQ-----NDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVV 2362
Cdd:TIGR04523 375 LKK--ENQSYKQEIKNlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2363 KLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAE 2442
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2443 KMKslaeeagrlsVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQ 2522
Cdd:TIGR04523 533 KKE----------KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2523 QIQQRLDKETEgfqksLEAERKRQLE-ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2599
Cdd:TIGR04523 600 DLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2434-2774 |
2.86e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.15 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2434 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQ----RQIAESNLAEQRALAEK--ILKEK----MQAIQEATKLKAEAEKL 2503
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREverrRKLEEAEKARQAEMDRQaaIYAEQermaMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2504 QKQKDQAQETA---------KRLQEDKQQIQQRLDKETEGF--QKSLEAERKRQL-EASAEAEKLKLRVKELSLAQTKAE 2571
Cdd:pfam17380 361 ELERIRQEEIAmeisrmrelERLQMERQQKNERVRQELEAArkVKILEEERQRKIqQQKVEMEQIRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2572 DEAKKfkKQADEVKAQLQRtEKHTTEIVVQKLETQRlqstreaddlksaiadleeerkKlkkeaeelqrKSKEManaQQE 2651
Cdd:pfam17380 441 EEERA--REMERVRLEEQE-RQQQVERLRQQEEERK----------------------R----------KKLEL---EKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2652 QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRfeKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaiMDEAVRKQKEA 2731
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKR--KLLEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQM 558
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1389908274 2732 EEEMKNKQReMDVLDKKRlEQEKQLAEENKKLREQLQTFEISS 2774
Cdd:pfam17380 559 RKATEERSR-LEAMERER-EMMRQIVESEKARAEYEATTPITT 599
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1648-1897 |
3.15e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 68.33 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1648 KAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEEtQRKKNAEDELKRKSDAEKEAAKQKQRALDDlqkyKMQAEE 1727
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQAEEKQKQAEEAKAKQAAE----AKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1728 AERRMKQAEEEKIRQirvvEEVAQKSAATQLQTKAmsfseqttklEESLKKEqgnvlklqeEADKLKKQQKEANTAREEA 1807
Cdd:TIGR02794 138 AEAERKAKEEAAKQA----EEEAKAKAAAEAKKKA----------EEAKKKA---------EAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1808 EQELEIWRQKanealrlrlqAEEEAQKKShAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1887
Cdd:TIGR02794 195 KAKAEAAKAK----------AAAEAAAKA-EAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
250
....*....|
gi 1389908274 1888 KLSAEQECIR 1897
Cdd:TIGR02794 264 YAAIIQQAIQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2328-2767 |
3.83e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKvlldQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2407
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2408 MEELVKLKLKIEEENRRLMQKDKDSTQ------------KLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2475
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2476 RALAEKI---------LKEKMQAIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRLDKETE--GFQKSL 2539
Cdd:PRK03918 341 EELKKKLkelekrleeLEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITAriGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2540 EAERKRQLEASAEA--------------------EKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA------------- 2586
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliklke 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2587 ---QLQRTEKHTTEIVVQKLEtqrlQSTREADDLKSAIADLEEERKKLKKEAEELQ--RKSKEMANAQQEQIEQQKAELQ 2661
Cdd:PRK03918 501 laeQLKELEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2662 QSfLTEKGL-----LLKREKEVEGEKKRF------EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2730
Cdd:PRK03918 577 KE-LEELGFesveeLEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510
....*....|....*....|....*....|....*...
gi 1389908274 2731 -AEEEMKNKQREMDVLDKKRLEQEKQLaEENKKLREQL 2767
Cdd:PRK03918 656 ySEEEYEELREEYLELSRELAGLRAEL-EELEKRREEI 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2002-2784 |
3.86e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2002 EEAA------RQRSEAEKilkeKLAAINEA-TRLkteaEMALKAKEAENERLKRQAEE-EAYQRKLLEDQAAQH---KQD 2070
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAEKaERYKELKAELRELELallVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2071 IEEKITQLQTSsDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAE 2150
Cdd:TIGR02168 234 LEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2151 KLKKlaaeeerrrkeaeeKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAE 2230
Cdd:TIGR02168 313 NLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2231 QKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2310
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2311 KeaeeeaarraaaeaaalkqkQQADAEMSKHKKEAEQALQQKSQvekeltvvklQLDETDKQKVLLDQELQRVKGE---V 2387
Cdd:TIGR02168 459 L--------------------EEALEELREELEEAEQALDAAER----------ELAQLQARLDSLERLQENLEGFsegV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2388 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLaeeaGRLSVEAEETARQR 2465
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQNEL----GRVTFLPLDSIKGT 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2466 QIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ------KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSL 2539
Cdd:TIGR02168 585 EI-QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2540 EAERKRQ--LEASAEAEKLKLRVKELslaqtkaEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStreaddl 2617
Cdd:TIGR02168 664 GSAKTNSsiLERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS------- 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2618 ksaiadleeerkklkkeaeeLQRKSKEMANAQQEQIEQQKAELQqsfltekglllKREKEVEGEKKRFEKQLEDEMKKAK 2697
Cdd:TIGR02168 730 --------------------ALRKDLARLEAEVEQLEERIAQLS-----------KELTELEAEIEELEERLEEAEEELA 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2698 ALkdeqerqrklmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2777
Cdd:TIGR02168 779 EA-----------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
....*..
gi 1389908274 2778 SQTKESQ 2784
Cdd:TIGR02168 848 EELSEDI 854
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1640-2062 |
4.27e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK--QVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDD 1717
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAEL-PERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1718 LQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQtkamSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ 1797
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE----ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1798 KEANTAREEAEQE--------------------------------------LEIWRQKANEALRLRLQAEEEAQKKSHAQ 1839
Cdd:COG4717 237 EAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1840 EEAEKQKLEAERDAKKRGKAEEA--ALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNelq 1917
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1918 rlKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkinaekasmVNTEKSKQLLESEALKMKQLADEAARMRsvAEEAKKQR 1997
Cdd:COG4717 394 --AEEYQELKEELEELEEQLEELLGELEELLEA---------LDEEELEEELEELEEELEELEEELEELR--EELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 1998 QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKeaenERLKRQAEEEaYQRKLLED 2062
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELL----EEAREEYREE-RLPPVLER 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2118-2769 |
5.56e-11 |
|
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: 69.61 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2118 SKEKADLESELKKL---KGIADETQKSKLKAEEEAEKLKK---LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAA 2187
Cdd:TIGR00618 162 SKEKKELLMNLFPLdqyTQLALMEFAKKKSLHGKAELLTLrsqLLTLCTPCMPDTYHERKQVLEKElkhlREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2188 QEEVERLKKKAEDANKQKEkaekeaekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRdEFENAKKLAQEAEKA 2267
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQ-----------LLKQLRARIEELRAQEAVLEETQERINRARKAAP-LAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2268 KEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQ 2347
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2348 ALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAFKQK--SQVEVELARVRIQmEELVKLKLKIEEENRrL 2425
Cdd:TIGR00618 390 TLTQKLQSLCKEL---DILQREQATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAIT-CTAQCEKLEKIHLQE-S 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2426 MQKDKDSTQKLLAEEA----EKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQA-IQEATKLKAEA 2500
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQihlqETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2501 EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2579
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAiadleEERKKLKKEAEELQRKSKEMANaQQEQIEQQKAE 2659
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQS-EKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2660 LQQsflteKGLLLKREKEVEGEKKRFEKQLEDEMKKAKA-----LKDEQERQRKLMEEERKKLQAimdeavrkqKEAEEE 2734
Cdd:TIGR00618 699 LAQ-----CQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKA---------RTEAHF 764
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908274 2735 MKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQT 2769
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1417-2154 |
5.69e-11 |
|
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: 69.69 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1417 PISDSRALREQLTD---EKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASplkKPKMECASDDII 1493
Cdd:TIGR00606 164 PLSEGKALKQKFDEifsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS---KEAQLESSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVN----LRTRYSELMTLTNQYIKfIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQ 1568
Cdd:TIGR00606 241 KSYENeldpLKNRLKEIEHNLSKIMK-LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1569 EALELKMKMKEEASKRQDVaaDAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHK 1648
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLL--NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1649 AKSEAElqelRDRAAEAEKLRKAAQDEaERLRKQVAEETQRKKNAedeLKRKSDAEKEAAKQKQRALDDLQKYKMQAEEA 1728
Cdd:TIGR00606 398 LVIERQ----EDEAKTAAQLCADLQSK-ERLKQEQADEIRDEKKG---LGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1729 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQkeaNTAREEAE 1808
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1809 QELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-KFAE 1882
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLsSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1883 QIAQQKLSAEQECI--RLKADFEHAEQQRGLL-------------------------------DNELQ----RLKNEVNS 1925
Cdd:TIGR00606 627 KLFDVCGSQDEESDleRLKEEIEKSSKQRAMLagatavysqfitqltdenqsccpvcqrvfqtEAELQefisDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1926 TEKQRKQLEDELNKVRSEMDSLLqmkINAEKASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQ--IAEEE 2003
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEML---GLAPGRQSIIDLKEKEIPELRN-KLQKVNRDIQRLKNDIEEQETLLGtiMPEEE 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2004 AAR--------------QRSEAEKILkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhKQ 2069
Cdd:TIGR00606 783 SAKvcltdvtimerfqmELKDVERKI-AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ-IQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2070 DIEEKITQLQT---SSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAE 2146
Cdd:TIGR00606 861 HLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
....*...
gi 1389908274 2147 EEAEKLKK 2154
Cdd:TIGR00606 941 DKVNDIKE 948
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1640-1948 |
5.72e-11 |
|
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: 69.33 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDaEKEAAKQKQRALD--- 1716
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELEari 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1717 -----DLQKYKMQAEEAERRMKQAEEEKI-RQIRVVEEVAQK--SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE 1788
Cdd:TIGR02169 768 eeleeDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRieARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1789 EADKLKKQQKEANTAREEAEQELEiwrqkanealrlRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaaLKQKE 1868
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELE------------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1869 NAEKELDKQRKFAEQIAQQKLS-------AEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLE 1934
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSeiedpkgEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELK 992
|
330
....*....|....
gi 1389908274 1935 DELNKVRSEMDSLL 1948
Cdd:TIGR02169 993 EKRAKLEEERKAIL 1006
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3307-3345 |
6.39e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 6.39e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 3307 LLEAQLSTGGIVDPVKSYRIPHEVACKRGYFDDKMSKTL 3345
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
206-313 |
6.66e-11 |
|
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: 62.60 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 206 ADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLKH 281
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 282 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2352-2782 |
7.14e-11 |
|
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: 68.98 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2352 KSQVEKELTVVKLQLDETDKQKVLLDQELQRvkgEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKD 2431
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2432 STQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQkdqAQ 2511
Cdd:pfam05483 280 QDENL-KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE---FE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2512 ETAKRLQEDKQQIQQRLDKETEGFQ--------KSLEAERKRQLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADE 2583
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKiitmelqkKSSELEEMTKFKNNKEVELEEL--KKILAEDEKLLDEKKQFEKIAEE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2584 VKA---------QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEerkklkkeaeelqRKSKEMANAQQEQIE 2654
Cdd:pfam05483 434 LKGkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL-------------KNIELTAHCDKLLLE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2655 QQKAELQQSFLTekgLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2730
Cdd:pfam05483 501 NKELTQEASDMT---LELKKHQEdiinCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2731 AEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE-QLQTFEISSKTVSQTKE 2782
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElHQENKALKKKGSAENKQ 630
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1693-1952 |
8.47e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 67.18 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1693 AEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRmKQAEEEKIRQIRvveevaQKSAAtqlqtkamsfsEQTTKL 1772
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELE------QRAAA-----------EKAAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQgnvLKLQEEADKLKKQQKEANTAREEAEQEleiwRQKANEALRlrlQAEEEAQKKshAQEEAEKQKLEAERD 1852
Cdd:TIGR02794 107 AEQAAKQA---EEKQKQAEEAKAKQAAEAKAKAEAEAE----RKAKEEAAK---QAEEEAKAK--AAAEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1853 AKKRGKAEEAALKQK--ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1930
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAkaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
250 260
....*....|....*....|..
gi 1389908274 1931 KQLEDELNKVRSEMDSLLQMKI 1952
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAIQQNL 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1849-2082 |
8.81e-11 |
|
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: 67.48 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1849 AERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTE 1927
Cdd:COG4942 17 AQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1928 KQRKQLEDELNKVrseMDSLLQMKINAEKASMVNTEKSKQLLESEALkMKQLADeaARMRSVAEEAKKQRQIAE--EEAA 2005
Cdd:COG4942 97 AELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAP--ARREQAEELRADLAELAAlrAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2006 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSS 2082
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2337-2765 |
9.46e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2337 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSqvevELARVRIQMEELVKLKL 2416
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2417 KIEEENRRLMQKDKDsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnlaeqraLAEKILKEKMQAIQEATKL 2496
Cdd:PRK03918 249 SLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2497 KAEAEKLQKQKDQAQETAKRLQEDKQQIQQrLDKETEGFQKSLEA-ERKRQLEAsaEAEKLKLRVKELSLAQTKAE-DEA 2574
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELyEEAKAKKE--ELERLKKRLTGLTPEKLEKElEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2575 KKFKKQ-ADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQqEQI 2653
Cdd:PRK03918 397 EKAKEEiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE-EKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2654 EQQKAELqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE- 2732
Cdd:PRK03918 476 RKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEk 550
|
410 420 430
....*....|....*....|....*....|....
gi 1389908274 2733 -EEMKNKQREmdvLDKKRLEQEKQLAEENKKLRE 2765
Cdd:PRK03918 551 lEELKKKLAE---LEKKLDELEEELAELLKELEE 581
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1689-2311 |
1.13e-10 |
|
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: 68.12 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1689 RKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQ 1768
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE----KINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1769 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANtareeaEQELEIwrqkANEALRLrlqaEEEAQKKSHAQEEAEKQKLE 1848
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENK------KNIDKF----LTEIKKK----EKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1849 AERDAKKrgkaeeaALKQKENAEKELDKQRKfAEQIAQQKLSAEQECIR----LKADFEHAEQQRGLLDN-------ELQ 1917
Cdd:TIGR04523 171 LENELNL-------LEKEKLNIQKNIDKIKN-KLLKLELLLSNLKKKIQknksLESQISELKKQNNQLKDniekkqqEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1918 RLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLAdEAARMRSVAEEAKKQR 1997
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSE-KQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1998 qiaeeeaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQ 2077
Cdd:TIGR04523 321 --------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2078 -----LQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEK 2151
Cdd:TIGR04523 393 indleSKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2152 LKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvvLAKEAAQKCTAAEQ 2231
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----------LESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2232 KAQDVLSKNkeDVLAQEKLRDEF----ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTE 2307
Cdd:TIGR04523 543 LEDELNKDD--FELKKENLEKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
....
gi 1389908274 2308 KQRK 2311
Cdd:TIGR04523 621 KAKK 624
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4482-4519 |
1.25e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 59.03 E-value: 1.25e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1389908274 4482 QRLLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMV 4519
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2329-2779 |
1.29e-10 |
|
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: 68.12 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVevelarvriqM 2408
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD----------W 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRALAEKILKEKMQ 2488
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE-------LEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2489 AIQEATKLKAEAEKLQKQKDQAQETAkrlqedkqqiqQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2568
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2569 KAEDEAKKFKKQADEVKAQLQrtekhTTEIVVQKLETQRLQSTREADDLKSAIadleeerkklkkeaeelqrkskEMANA 2648
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLK-----VLSRSINKIKQNLEQKQKELKSKEKEL----------------------KKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2649 QQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDemKKAKALKDEQERQRKLMEEERKKLQaimdEAVRKQ 2728
Cdd:TIGR04523 504 EKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKN----KEIEEL 573
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2729 KEAEEEMKNKQREMDvldkkrlEQEKQLAEENKKLREQLQTFEISSKTVSQ 2779
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQ-------ELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2328-2771 |
1.33e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQ 2407
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2408 MEELvklKLKIEEENRRLMQKDKdstqkLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKM 2487
Cdd:COG4717 148 LEEL---EERLEELRELEEELEE-----LEAELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2488 QAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLA 2566
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2567 QTKAEDEAKKFKKQADEVKAQLQRtekhtteivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMA 2646
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPAL----------EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2647 NAQ--QEQIEQQKAELQQSF-------LTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklMEEERKKL 2717
Cdd:COG4717 360 EEElqLEELEQEIAALLAEAgvedeeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEEL 437
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2718 QAimdeavrKQKEAEEEMKNKQREmdvldKKRLEQEKQLAEENKKLREQLQTFE 2771
Cdd:COG4717 438 EE-------ELEELEEELEELREE-----LAELEAELEQLEEDGELAELLQELE 479
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1656-2101 |
1.45e-10 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 68.16 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1656 QELRDraAEAEKlrKAAQDEaerlrkqVAEETQRKKNAEDElkRKSDAEKeaAKQKQRALDDLQKYKMQAeeaeRRMKQA 1735
Cdd:PRK10929 30 QELEQ--AKAAK--TPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPKLSAEL----RQQLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1736 EEEKIRQIRvveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQeleiwr 1815
Cdd:PRK10929 91 ERDEPRSVP------PNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIER------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1816 qkanealrlRLQAeeeAQKKSHAQEEAEKQKLeaerdakkrgKAEEAALKQKENaekELDkqrkfaeqIAQqkLSA--EQ 1893
Cdd:PRK10929 159 ---------RLQT---LGTPNTPLAQAQLTAL----------QAESAALKALVD---ELE--------LAQ--LSAnnRQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1894 ECIRLKADFEHAEQQRglLDNELQRLKNEVNStekQRKQledelnkvrsemdsllqmkiNAEKAsmvnTEKSKQLLESEA 1973
Cdd:PRK10929 204 ELARLRSELAKKRSQQ--LDAYLQALRNQLNS---QRQR--------------------EAERA----LESTELLAEQSG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1974 LKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKIL--KEKLAAINEATRLKTEAEM---ALKAKEA------E 2042
Cdd:PRK10929 255 DLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLqvRQALNTLREQSQWLGVSNAlgeALRAQVArlpempK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2043 NERLKRQAEEEAYQRKLLEDQAAQHKQDieekiTQLQTSSDSEL-GRQKNIVEETLKQKK 2101
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNKQPQL-----RQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1655-1875 |
1.59e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.75 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1655 LQELRDRAAEAEKLR-KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDlQKykmQAEEAERRMK 1733
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-QK---QAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1734 QAEEEKIRQIRVVEEVAQKSAAtqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqelei 1813
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAA-----------------AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK----- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 1814 wrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELD 1875
Cdd:PRK09510 201 --KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2356-2775 |
1.63e-10 |
|
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: 67.74 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2356 EKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmqkdkdstQK 2435
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2436 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE---QRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQE 2512
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2513 TAKRLQEDKQQIQQRLDKETEGFQ--KSLEAERKRQLEA-SAEAEKLKLRVKELS--LAQTKAEDEAKKFKKQAD---EV 2584
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEkQKELEQNNKKIKELEkqLNQLKSEISDLNNQKEQDwnkEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2585 KAQLQRTEKHTTEIvvqklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmanaQQEQIEQQKAElQQSF 2664
Cdd:TIGR04523 313 KSELKNQEKKLEEI-----QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKLKKE-NQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2665 LTEKGLLLKREKEVEGE---KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNkqre 2741
Cdd:TIGR04523 383 KQEIKNLESQINDLESKiqnQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN---- 458
|
410 420 430
....*....|....*....|....*....|....
gi 1389908274 2742 mdvLDKKRLEQEKQLAEENKKLREQLQTFEISSK 2775
Cdd:TIGR04523 459 ---LDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
702-891 |
1.84e-10 |
|
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: 64.00 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 702 LRYTQDLLGWVEENQRRVDEGEWGSDLPTVESLLGSHRGLHQCVEEFRSKIERAKADESQV---SPASKAAYRDYLGKLE 778
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 779 LQYGKLLTSSKARLRYLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAV 855
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908274 856 QTTGDKLLRDGHP-ARKTIEAFTAALQTQWSWLLQLC 891
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1642-1893 |
1.86e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1642 EKTTAHKAKS--EAELQEL-RDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDl 1718
Cdd:PRK05035 444 EKKKAEEAKArfEARQARLeREKAAREARHKKAAEARAAKDKDAVAA-------ALARVKAKKAAATQPIVIKAGARPD- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1719 QKYKMQAEEAERRMKQAEEEKIRQirvVEEVAQKSAA-------TQLQTKAMSFSEQTTKLEESLKKEQgnVLKLQEEAd 1791
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQA---AAAADPKKAAvaaaiarAKAKKAAQQAANAEAEEEVDPKKAA--VAAAIARA- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1792 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1871
Cdd:PRK05035 590 KAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669
|
250 260
....*....|....*....|....*.
gi 1389908274 1872 KELDKQRK--FAEQIA--QQKLSAEQ 1893
Cdd:PRK05035 670 EEAEDPKKaaVAAAIAraKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1699-2143 |
1.87e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1699 RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1778
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1779 EQGNVLKLQEEADKLKKQQKEantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1858
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1859 AEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRL------KADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQ 1932
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 LEDELNKVR--SEMDSLLQMKINAEKAS-MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEA--ARQ 2007
Cdd:COG4717 300 LGKEAEELQalPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2008 RSEAEKILKEKLAAINEATRLK---TEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkQDIEEKITQLQTssds 2084
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKeelEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELRE---- 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2085 ELGRQKNIVEETLKQKKVVE--EEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 2143
Cdd:COG4717 454 ELAELEAELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4138-4176 |
1.93e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.93e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 4138 LLEAQAATGYVIDPIKNLKLNVTEAVKMGIVGTEFKDKL 4176
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2083-2771 |
3.16e-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: 67.02 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2083 DSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLEsELKKLKGIADETQ-----KSKLKAEEEAEKLKK--- 2154
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERqla 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2155 -LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAAQEEVERLKKKAEDankqKEKAEKEAEKQVVLAKEAAQKCTAA 2229
Cdd:TIGR02169 248 sLEEELEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2230 EQKAQDVLSKNKEDVlaqEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQ 2309
Cdd:TIGR02169 324 LAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2310 RkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL-------QLDETDKQKVLLDQELQR 2382
Cdd:TIGR02169 401 I-------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeikkqewKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2383 VKGEVNDAFKQKSQVEVELARV---RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAG-RLS--- 2455
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGnRLNnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2456 VEAEETA-------RQRQIAE----------------------------------------------------SNLAEQR 2476
Cdd:TIGR02169 554 VEDDAVAkeaiellKRRKAGRatflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2477 ALAEKI--------LKEKMQAI-----------QEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD-------- 2529
Cdd:TIGR02169 634 RLMGKYrmvtlegeLFEKSGAMtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDelsqelsd 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2530 --KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQR 2607
Cdd:TIGR02169 714 asRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2608 LQSTREADDLK------SAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgE 2681
Cdd:TIGR02169 794 PEIQAELSKLEeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-E 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2682 KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQE-------- 2753
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeels 952
|
810
....*....|....*....
gi 1389908274 2754 -KQLAEENKKLREQLQTFE 2771
Cdd:TIGR02169 953 lEDVQAELQRVEEEIRALE 971
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2434-2755 |
3.67e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 64.94 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2434 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQET 2513
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2514 AKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEklkLRVKELSLAQTKAEDEAKKFKKQADEVKaqlqrtEK 2593
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2594 HTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGL-LL 2672
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQ--------------ERKERQKEREEAEKKARQRQELQQAREEQIELkER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2673 KREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDE---AVRKQKEAEEEMKNKQREMDVLDKKR 2749
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1389908274 2750 LEQEKQ 2755
Cdd:pfam13868 331 IEEERQ 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2337-2768 |
4.98e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 66.15 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2337 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKL 2416
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2417 KIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnLAEQRALAEKILKEKMQAIQEAT 2494
Cdd:TIGR00618 240 QSHAYLTQKreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2495 KLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRqlEASAEAEKLKLRVKELSLAQTKAEDE- 2573
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR--EISCQQHTLTQHIHTLQQQKTTLTQKl 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 ----AKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMAN-- 2647
Cdd:TIGR00618 396 qslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQql 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2648 AQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFE-----------------------KQLEDEMKKAKALKDEQE 2704
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNparqdidnpgpltrrmqrgeqtyAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2705 RQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK---KRLEQEKQLAEENKKLREQLQ 2768
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQ 622
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2405-2819 |
5.29e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.15 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2405 RIQMEELV---KLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAgrlsVEAEETARQRQIAESNLAEQRALAEK 2481
Cdd:pfam02463 155 RLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKE----QAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2482 ILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQqRLDKETEGFQKSLEAERKRQLEaSAEAEKLKLRVK 2561
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN-KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2562 ELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQSTREADDLksaiADLEEERKKLKKEAEELQRK 2641
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL---EKELKELEIKREAEEEEEEEL----EKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2642 SKEMANAQQEQIEQQKAELqqsfltekgllLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaim 2721
Cdd:pfam02463 382 ESERLSSAAKLKEEELELK-----------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT--- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2722 deaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSK 2801
Cdd:pfam02463 448 ---EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410
....*....|....*...
gi 1389908274 2802 GVLNGSTEVDGVKKEGDS 2819
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYK 542
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
214-310 |
5.53e-10 |
|
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: 59.51 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 214 KKTFTKWVNKHLVKaQRHVT----------DLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 278
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 279 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 310
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2245-2658 |
5.54e-10 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 65.79 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2245 LAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAE 2324
Cdd:COG5281 15 AAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2325 AAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARV 2404
Cdd:COG5281 95 AEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2405 RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2484
Cdd:COG5281 175 AAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2485 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQL--EASAEAEKLKLRVKE 2562
Cdd:COG5281 255 AAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAaaAAQALRAAAQALAAL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2563 LSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKS 2642
Cdd:COG5281 335 AQRALAAAALAAAAQEAALAAAAAALQAAL---EAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAF 411
|
410
....*....|....*.
gi 1389908274 2643 KEMANAQQEQIEQQKA 2658
Cdd:COG5281 412 SGLTDALAGAVTTGKL 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1668-2079 |
5.75e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1668 LRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1747
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1748 EVAQKSAATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQ 1827
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1828 AEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIA---------------------- 1885
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1886 ------------QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVN-STEKQRKQLEDELNKVRSEMDSLLQMKI 1952
Cdd:COG4717 279 lflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1953 NAEKASMVNTEKSKQLLeseaLKMKQLADEAArMRSVAEEAKKQRQIAEE--EAARQRSEAEKILKEKLAAINEATRLKT 2030
Cdd:COG4717 359 LEEELQLEELEQEIAAL----LAEAGVEDEEE-LRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2031 EAEMALKAKEAENER---LKRQAEEEAYQRKLLEDQAAQH-KQDIEEKITQLQ 2079
Cdd:COG4717 434 LEELEEELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELR 486
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
328-427 |
5.96e-10 |
|
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: 59.70 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYrQSNQ--ENLEQAFSVAERELGVTKLL 405
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1389908274 406 DPEDVDVPHPDEKSIITYVSSL 427
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1525-1879 |
6.41e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 65.27 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1525 EDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN-IQ 1599
Cdd:pfam02029 1 IEDEEEAARERRrrarEERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKrLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1600 QELQHLK---------SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRK 1670
Cdd:pfam02029 81 EALERQKefdptiadeKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1671 AAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRalddLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVA 1750
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG----HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1751 QKSAATQLQTkamsfsEQttKLEESLKKEQGnvlKLQEEADKLKKQQkeantarEEAEQELEIWRQKANEalRLRLQAEE 1830
Cdd:pfam02029 237 EEEAEVFLEA------EQ--KLEELRRRRQE---KESEEFEKLRQKQ-------QEAELELEELKKKREE--RRKLLEEE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 1831 EAQKKshaQEEAEKQKLEAERdaKKRGKAE------EAALKQKENAEKELDKQRK 1879
Cdd:pfam02029 297 EQRRK---QEEAERKLREEEE--KRRMKEEierrraEAAEKRQKLPEDSSSEGKK 346
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1709-2132 |
6.61e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1709 KQKQRALDDL------QKYKMQAEEAE---RRMKQAEEEKIRQIRvvEEVAQKSAA------TQLQTKAMSFSEQTTKLE 1773
Cdd:PRK02224 149 SDRQDMIDDLlqlgklEEYRERASDARlgvERVLSDQRGSLDQLK--AQIEEKEEKdlherlNGLESELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1774 EslKKEQGNVLKlqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1853
Cdd:PRK02224 227 E--QREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1854 KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQL 1933
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1934 EDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE----------- 2002
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2003 -----EAARQRSEAEKILKEKLAAINEA-TRLKTEAEMALKAKEAEnerlkRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 2076
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEvEEVEERLERAEDLVEAE-----DRIERLEERREDLEELIAERRETIEEKRE 537
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 2077 QLQtssdsELGRQKNIVEETLKQKKVVEEEIHiikINFHKASKEKADLESELKKLK 2132
Cdd:PRK02224 538 RAE-----ELRERAAELEAEAEEKREAAAEAE---EEAEEAREEVAELNSKLAELK 585
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1641-2062 |
9.22e-10 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 65.03 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1641 LEKTTAHKAKSEAELqelrdraaeAEKLRKAAQDEAERLRKQVAEETqrKKNAEDElKRKSDAEKEAAKQKQralDDLQK 1720
Cdd:NF033838 101 LYELNVLKEKSEAEL---------TSKTKKELDAAFEQFKKDTLEPG--KKVAEAT-KKVEEAEKKAKDQKE---EDRRN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1721 Y--------KMQAEEAERRMKQAEEEkirqirVVEEVAQKSaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADK 1792
Cdd:NF033838 166 YptntyktlELEIAESDVEVKKAELE------LVKEEAKEP-----------------RDEEKIKQAKAKVESKKAEATR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1793 LKKqqkeANTAREEAEQeleiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKleaeRDAKKRGKAEEAALKQKENAEK 1872
Cdd:NF033838 223 LEK----IKTDREKAEE----------EAKRRADAKLKEAVEKNVATSEQDKPK----RRAKRGVLGEPATPDKKENDAK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1873 ELDKQRKfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRlknevNSTEKQRKQLEDELNKVRSEMDSLLQMKI 1952
Cdd:NF033838 285 SSDSSVG-EETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELEIAESDVKVKEAELELV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1953 NAEKASMVNTEKSKQLLESEALKMKqladEAARMrsvaEEAKKQRQIAEEEAARQRSEAEKIlKEKLAAINEATRLKTEA 2032
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKV-KEKPAEQPQPAPAPQPE 429
|
410 420 430
....*....|....*....|....*....|....
gi 1389908274 2033 EMALK----AKEAENERLKRQAEEEAYQRKLLED 2062
Cdd:NF033838 430 KPAPKpekpAEQPKAEKPADQQAEEDYARRSEEE 463
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1537-1901 |
1.11e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1537 EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKeeaskrqdvaaDAEKQKQNIQQELQHLkslsDQEIKSK 1616
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-----------DASRKIGEIEKEIEQL----EQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1617 NQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE-KLR----KAAQDEAERLRKQVAEETQRKK 1691
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLShsriPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1692 NAEDELKRKSDAEKEAAKQKQraldDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQT 1769
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1770 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELeiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKLEA 1849
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 1850 ERDAKKRGKAEEAALKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLKAD 1901
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEVLKRLDELKE-----KRAKLEEERKAILERIE 1010
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1429-2137 |
1.17e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.04 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1429 TDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKalqdpiaSPLKKPKMECASDDIIQEYVNLR-TRYSELM 1507
Cdd:TIGR04523 82 QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE-------VELNKLEKQKKENKKNIDKFLTEiKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1508 TLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahAKSVAKAEQEALELKMKMKEEASKRQDV 1587
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL----LSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1588 aadaEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRdraAEAEK 1667
Cdd:TIGR04523 231 ----KDNIEKKQQEINEKT----TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK---SEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1668 LRKAAQDEaerLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1747
Cdd:TIGR04523 300 LNNQKEQD---WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1748 EVAQ--KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLR 1825
Cdd:TIGR04523 377 KENQsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV---KE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 LQAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKenaEKELDKQRKFAEQIAQQKLSAEQECIRLKadfeha 1905
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSI--------NKIKQNLEQK---QKELKSKEKELKKLNEEKKELEEKVKDLT------ 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1906 eQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkinaekasmVNTEKSKQLLESEALKMKQLADEAar 1985
Cdd:TIGR04523 517 -KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-------------ENLEKEIDEKNKEIEELKQTQKSL-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1986 mrsvaeeAKKQRQiAEEEAARQRSEAEKILKEklaaINEATRLKTEAEMALKAKEAENERL----------KRQAEEEAY 2055
Cdd:TIGR04523 581 -------KKKQEE-KQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLssiiknikskKNKLKQEVK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2056 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEiHIIKINFHKASKEKADLESELKKLKGIA 2135
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR-MIRIKDLPKLEEKYKEIEKELKKLDEFS 727
|
..
gi 1389908274 2136 DE 2137
Cdd:TIGR04523 728 KE 729
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1519-1809 |
1.42e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS--------------KR 1584
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeelaeaeaEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1585 QDVAADAEKQKQNIQQELQHLKSLSDQ------EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL 1658
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1659 RDRAAEAEKLRKAAQDEaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1738
Cdd:TIGR02168 865 EELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1739 KIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNV--------LKLQEEADKLKKQQKEANTAREEAE 1808
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKrlENKIKELGPVnlaaieeyEELKERYDFLTAQKEDLTEAKETLE 1020
|
.
gi 1389908274 1809 Q 1809
Cdd:TIGR02168 1021 E 1021
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1658-2033 |
2.36e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1658 LRDRAAEAEKLRKAAQDEAERL--RKQVAEETQRKKNAEDELKRKSDAEKE--------------------AAKQKQRAL 1715
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1716 DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNV 1783
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1784 L---KLQEEADKLKKQQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAE 1850
Cdd:PRK04863 435 LtadNAEDWLEEFQAKEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1851 RDAKKRGKAEEaaLKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1930
Cdd:PRK04863 514 QLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1931 KQLEDELNKVRSEMDSLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSE 2010
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQAL 657
|
410 420
....*....|....*....|...
gi 1389908274 2011 AEKILKEKLAAINEATRLKTEAE 2033
Cdd:PRK04863 658 DEEIERLSQPGGSEDPRLNALAE 680
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2412-2772 |
2.41e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2412 VKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ 2491
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2492 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQ--RLDKETEGFQKsLEAERKRQLEASAEAEKLKLRVKELSLAQTK 2569
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2570 AEDEAKKFKKQADEVKAQLQRTEKHTTEI--VVQKLETQRlQSTREADDLKSAIADleeerkklkkeaeelqrKSKEMAN 2647
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELeeRHELYEEAK-AKKEELERLKKRLTG-----------------LTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2648 AQQEQIEQQKAELQQSFLTekglLLKREKEVEGEKKRFEKQLEdEMKKAK-------ALKDEQERQRkLMEEERKKLQAI 2720
Cdd:PRK03918 391 KELEELEKAKEEIEEEISK----ITARIGELKKEIKELKKAIE-ELKKAKgkcpvcgRELTEEHRKE-LLEEYTAELKRI 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2721 MDEaVRKQKEAEEEMKNKQREMD--VLDKKRLEQEKQLAEENKKLREQLQTFEI 2772
Cdd:PRK03918 465 EKE-LKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1872-2763 |
2.49e-09 |
|
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: 64.30 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1872 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLL---DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1948
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItskEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1949 QM--KINAEKASMVNTEKSKQLLESEALKMKQLADEaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 2026
Cdd:TIGR00606 266 KLdnEIKALKSRKKQMEKDNSELELKMEKVFQGTDE--QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2027 RLKTE-AEMALKAKEAENERLKRQAEEEAYQRKLlEDQAAQHKQDIEEKITQLQT-----SSDSELGRQKNIVE----ET 2096
Cdd:TIGR00606 344 ELLVEqGRLQLQADRHQEHIRARDSLIQSLATRL-ELDGFERGPFSERQIKNFHTlvierQEDEAKTAAQLCADlqskER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2097 LKQKKVVEEEIHIiKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA 2176
Cdd:TIGR00606 423 LKQEQADEIRDEK-KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2177 EEEAARQCKAaqeEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKctaaEQKAQDVLSKNKEDVLAQEKlrdEFEN 2256
Cdd:TIGR00606 502 EVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK----DEQIRKIKSRHSDELTSLLG---YFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2257 AKKLAQEAEKakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQkQQADA 2336
Cdd:TIGR00606 572 KKQLEDWLHS-----------KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2337 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevndaFKQKSQVEvELARVRIQMEELVKLKL 2416
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV-------FQTEAELQ-EFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2417 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQralaEKILKEKMQAIQEATKL 2496
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVC 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2497 KAEAEKLQKQKDQAQETAKRLQedkqqiQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKK 2576
Cdd:TIGR00606 788 LTDVTIMERFQMELKDVERKIA------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2577 FKKQADEVKAQlqRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEqiEQQ 2656
Cdd:TIGR00606 862 LKSKTNELKSE--KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET--SNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2657 KAELQQSFLTEK-----GLLLKREKEVEGEKKRFEKQLEDEMKKAKA-LKDEQERQRKLMEEERKKLQAIMDEAVR---- 2726
Cdd:TIGR00606 938 KAQDKVNDIKEKvknihGYMKDIENKIQDGKDDYLKQKETELNTVNAqLEECEKHQEKINEDMRLMRQDIDTQKIQerwl 1017
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1389908274 2727 -----------KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL 2763
Cdd:TIGR00606 1018 qdnltlrkrenELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL 1065
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1526-1772 |
3.06e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1526 DDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskRQDVAADAEKQKQNIQQELQHL 1605
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1606 KslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL-RDRAAEAEKLRkAAQDEAERLRKQVA 1684
Cdd:COG4942 96 R----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1685 EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKyKMQAEEAERRMKQAEEEKIRqiRVVEEVAQKSAATQLQTKAMS 1764
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEK-ELAELAAELAELQQEAEELE--ALIARLEAEAAAAAERTPAAG 247
|
....*...
gi 1389908274 1765 FSEQTTKL 1772
Cdd:COG4942 248 FAALKGKL 255
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1726-2135 |
4.00e-09 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 62.85 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1726 EEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1805
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1806 EAEQELEiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAK------KRGKAEEAALKQKENAEKELDKQRK 1879
Cdd:pfam09731 132 EVLKEAI---SKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISRekatdsALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1880 FA-EQIAQQKLSAEQECIRLKAdfehaeqqrglLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL-QMKINAEKA 1957
Cdd:pfam09731 209 AApPLLDAAPETPPKLPEHLDN-----------VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFpDIIPVLKED 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1958 SMVNTEKSKQLLESEALKMKQLADEAARMRsVAEEAKKQRQIAEEEAARQRSEAEKI--LKEKLAAINEATRLKTEAEMA 2035
Cdd:pfam09731 278 NLLSNDDLNSLIAHAHREIDQLSKKLAELK-KREEKHIERALEKQKEELDKLAEELSarLEEVRAADEAQLRLEFERERE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2036 LKAKEAENE---RLKRQAEE-EAYQRKLLEDQAAQ----HKQDIEEKITQLQTSSDSELGRQK---NIVEETLKQKKVVE 2104
Cdd:pfam09731 357 EIRESYEEKlrtELERQAEAhEEHLKDVLVEQEIElqreFLQDIKEKVEEERAGRLLKLNELLanlKGLEKATSSHSEVE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1389908274 2105 EE----------IHIIKINFHKAS--KEKADLESELKKLKGIA 2135
Cdd:pfam09731 437 DEnrkaqqlwlaVEALRSTLEDGSadSRPRPLVRELKALKELA 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1499-1853 |
4.38e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 4.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1499 LRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahaksvakaEQEALELKMKMK 1578
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL-----------EQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1579 EEASKRQDVAADAEKqkqnIQQELQHLK-SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1657
Cdd:TIGR02169 762 ELEARIEELEEDLHK----LEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1658 LRDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEE 1737
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1738 EkirqirvVEEvaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklqEEADKLKKQQKEantaREEAEQELEiwrqk 1817
Cdd:TIGR02169 911 Q-------IEK--KRKRLSELKAKLEALEEELSEIEDPKGEDEEIP----EEELSLEDVQAE----LQRVEEEIR----- 968
|
330 340 350
....*....|....*....|....*....|....*.
gi 1389908274 1818 ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1853
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2343-2581 |
4.43e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2343 KEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRiqmEELVKLKLKIEEen 2422
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2423 rrlMQKDKDSTQKLLAE---EAEKMKSLAEEAGRLSVE-AEETARQRQIAESNLAEQRALAEKILKEKmqaiqeatklkA 2498
Cdd:COG4942 95 ---LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADL-----------A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2499 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFK 2578
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1389908274 2579 KQA 2581
Cdd:COG4942 241 ERT 243
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
215-309 |
4.53e-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: 56.96 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 215 KTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 286
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1389908274 287 VNIRNDDIADGNPKLTLGLIWTI 309
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2368-2771 |
4.78e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.14 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2368 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEENRRLMQKDKDSTQKLLAEEAEK---M 2444
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2445 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKD----QAQETAKRLQED 2520
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeledRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2521 KQQIQQrldketegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV 2600
Cdd:PRK02224 334 RVAAQA--------HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2601 Q--KLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQR--------------KSKEMANA---QQEQIEQQKAEL- 2660
Cdd:PRK02224 406 DlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETieeDRERVEELEAELe 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2661 ----QQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMK 2736
Cdd:PRK02224 486 dleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430
....*....|....*....|....*....|....*
gi 1389908274 2737 NKQREMDVLDKkrLEQEKQlaeENKKLREQLQTFE 2771
Cdd:PRK02224 566 EAEEAREEVAE--LNSKLA---ELKERIESLERIR 595
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1532-1984 |
5.05e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 62.92 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1532 EKLKEEERRKMAEIQA------ELDKQ----KQMAEAHAKSVAKAEQ---------EALELKMKMKEEA-SKRQDVAADA 1591
Cdd:pfam10174 292 DQLKQELSKKESELLAlqtkleTLTNQnsdcKQHIEVLKESLTAKEQraailqtevDALRLRLEEKESFlNKKTKQLQDL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1592 EKQKQNIQQELQHLKSLSDQE------IKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHkakSEAELQELRDRAAEA 1665
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKerkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN---TDTALTTLEEALSEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1666 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAekeaakqkqralddlqkykMQAEEAERrmkqaeeekirqirv 1745
Cdd:pfam10174 449 ERIIERLKEQREREDRERLEELESLKKENKDLKEKVSA-------------------LQPELTEK--------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1746 veevaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwrqkaneALRLR 1825
Cdd:pfam10174 495 ------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-------NDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 LQAEEEAQKKshaqEEAEKQKLEAERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQ-IAQQKLSAEQECIRLKAdfe 1903
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVEnEKNDKDKKIAELESLTLRQMKEQnKKVANIKHGQQEMKKKG--- 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1904 haeqqRGLLDNELQRLKNEV-NSTEKQRKQLEDELNKVRSEMDSlLQMKIN------AEKASMVNT---EKSKQLleSEA 1973
Cdd:pfam10174 635 -----AQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQELDA-TKARLSstqqslAEKDGHLTNlraERRKQL--EEI 706
|
490
....*....|.
gi 1389908274 1974 LKMKQLADEAA 1984
Cdd:pfam10174 707 LEMKQEALLAA 717
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1519-1718 |
5.64e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEEERRKMAEIQ---AELDKQKQMAEAHAKSVAKAEQEALElKMKMKEEASKRQDVAADAEKQK 1595
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQerlKQLEKERLAAQEQKKQAEEAAKQAAL-KQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1596 QNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKieeeihiiriQLEKTTAHKAKSEAElqelrdRAAEAEKLRKAAQD- 1674
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKK----------KAEAEAAAKAAAEAK------KKAEAEAKKKAAAEa 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1389908274 1675 --EAERLRKQVAEETQRKKNAEDELKRKSDA-EKEAAKQKQRALDDL 1718
Cdd:PRK09510 216 kkKAAAEAKAAAAKAAAEAKAAAEKAAAAKAaEKAAAAKAAAEVDDL 262
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
213-312 |
6.13e-09 |
|
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: 56.74 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILH 312
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4560-4598 |
6.84e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.26 E-value: 6.84e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 4560 FLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTAQKL 4598
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2179-2557 |
6.95e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2179 EAARQCKAAQEEVERLKK-KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2257
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2258 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQkkaaENEAAKQAKAQnDTEKQRKEaeeeaarraaaeaaalkqkQQADAE 2337
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQ----ELEAARKVKIL-EEERQRKI-------------------QQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2338 MSKHKKEAEQALQQKSQV---EKELTVVKLQLDETDKQkvlldQELQRVKgevndafkqksQVEVELARVRIQMEELVKL 2414
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRleeERAREMERVRLEEQERQ-----QQVERLR-----------QQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2415 KLKIEEENRRLMQKDKdstqkllaeEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlaEQRALAEKiLKEKMQAIQeat 2494
Cdd:pfam17380 486 RKRAEEQRRKILEKEL---------EERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEE-ERRKQQEME--- 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2495 klkaEAEKLQKQKDQAQETAKRLQEdkqqiqqrLDKETEGFQKSLEAERKRQ-LEASAEAEKLK 2557
Cdd:pfam17380 550 ----ERRRIQEQMRKATEERSRLEA--------MEREREMMRQIVESEKARAeYEATTPITTIK 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2489-2762 |
7.13e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2489 AIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2568
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2569 KAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIAdleeerkklkkeaeelqrkSKEMANA 2648
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQY-------------------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2649 QQEQIEQQKAELQQsfLTEKglllkrekevegekkrfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ 2728
Cdd:COG4942 148 RREQAEELRADLAE--LAAL-----------------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|....
gi 1389908274 2729 KEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKK 2762
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1714-1944 |
7.45e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1714 ALDDLQKYKMQAEEAERRMKQAEEeKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESlkKEQGNVLKLQEEADKL 1793
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAAR---------ERLAELEYL--RAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1794 KKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK------ 1867
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalgl 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 1868 --ENAEKELDKQRkfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEM 1944
Cdd:COG4913 374 plPASAEEFAALR---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2377-2587 |
9.09e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2377 DQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmQKDKDSTQKLLAEEAEKMKSLAEEAGRLSV 2456
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2457 EAEETARQRQIAE--------SNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRL 2528
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2529 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQ 2587
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1845-2310 |
9.32e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1845 QKLEAERDA--KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1922
Cdd:COG4717 49 ERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VN--STEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIA 2000
Cdd:COG4717 125 LQllPLYQELEALEAELAELPERLEELEE-------------------------RLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2001 EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEayqrklledQAAQHKQDIEEKITQLQT 2080
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL---------ENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2081 SSDSE------LGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAdetQKSKLKAEEEAEKLKK 2154
Cdd:COG4717 251 LLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP---ALEELEEEELEELLAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2155 LAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQE-EVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKA 2233
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEL 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2234 QDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2310
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
323-427 |
9.87e-09 |
|
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: 55.87 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 323 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGV 401
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*.
gi 1389908274 402 TKLLDPEDVDVPHPDEKSIITYVSSL 427
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1571-2130 |
1.12e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 61.58 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1571 LELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ-EIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKA 1649
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA--QAKQDSELAKLRVEEMEQGIADEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1650 K--SEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEE 1727
Cdd:pfam05701 119 SvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1728 AERRMKQAEEEKIRqirvveevaqksaatqlqtKAMSFSEQTTKLEESLKkeqgnvlKLQEEADKLKKQQkeanTAREEA 1807
Cdd:pfam05701 199 AHAAHLEAEEHRIG-------------------AALAREQDKLNWEKELK-------QAEEELQRLNQQL----LSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1808 EQELEiwrqkANEALRLRLQAEEEAQKKSHAQEEAEKQKLEaerdaKKRGKAEEAALKQkenAEKELDKQRKFAEqiaqq 1887
Cdd:pfam05701 249 KSKLE-----TASALLLDLKAELAAYMESKLKEEADGEGNE-----KKTSTSIQAALAS---AKKELEEVKANIE----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1888 KLSAEQECIRLKAdfehaeqqrGLLDNELQRLKNEVNSTeKQRK--------QLEDELNKVRSEMdSLLQMKINAEKASM 1959
Cdd:pfam05701 311 KAKDEVNCLRVAA---------ASLRSELEKEKAELASL-RQREgmasiavsSLEAELNRTKSEI-ALVQAKEKEAREKM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1960 VNTEKSKQLLESEALKMKQLAdEAARmrsvaEEAKKQRQIAEE-EAARQRSEA--EKILKEKLAAiNEATRLKTEAEMAL 2036
Cdd:pfam05701 380 VELPKQLQQAAQEAEEAKSLA-QAAR-----EELRKAKEEAEQaKAAASTVESrlEAVLKEIEAA-KASEKLALAAIKAL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2037 KAKEAENE----------------------RLKRQAEEEAYQRklledqaaqhkqdIEEKITQLQTSSDSELgRQKNIVE 2094
Cdd:pfam05701 453 QESESSAEstnqedsprgvtlsleeyyelsKRAHEAEELANKR-------------VAEAVSQIEEAKESEL-RSLEKLE 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908274 2095 ETLKQKKVVEEEIHIIKINFHKASKEKADLESELKK 2130
Cdd:pfam05701 519 EVNREMEERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1709-1891 |
1.22e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.04 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1709 KQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIrvveevaQKSAATQLQTKAmsfseqttklEESLKKEQGNVLKLQE 1788
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEI-------AIAQANREAEEA----------ELEQEREIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1789 EADKLKKQ---QKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1865
Cdd:COG2268 243 EAELAKKKaeeRREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1389908274 1866 QKENAEKELDKQRKFAEQIAQQKLSA 1891
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1882-2608 |
1.29e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1882 EQIAQQKLSAEQECIRlKADFEHAEQQRGL---LDNELQRLKNEVNSTEKQRKQLEDELNKVRSemdsLLQMKINAEKAS 1958
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1959 MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKA 2038
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2039 kEAENERLKR--QAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNI---VEETLKQKKVVEEEIHIIKIN 2113
Cdd:pfam05483 205 -QAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2114 FHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVER 2193
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2194 LKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEK 2273
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2274 EAALLRQKAEEAEKQ---KKAAENEAAKQA---KAQNDTEKQRKEAEEEAARRAAAEAAALKQ----------KQQADae 2337
Cdd:pfam05483 444 LLQAREKEIHDLEIQltaIKTSEEHYLKEVedlKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlelkKHQED-- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2338 MSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK---- 2413
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENkcnn 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2414 LKLKIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEeTARQRQIAESNLAEQRALAEKILKEKM-QAI 2490
Cdd:pfam05483 599 LKKQIENKNKNIeeLHQENKALKKKGSAENKQLNAYEIKVNKLELELA-SAKQKFEEIIDNYQKEIEDKKISEEKLlEEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2491 QEATKLKAEAEKLQKQKDqaqetaKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqlEASAEAEKLKLRVKELSLAQTKA 2570
Cdd:pfam05483 678 EKAKAIADEAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIE-------ERDSELGLYKNKEQEQSSAKAAL 744
|
730 740 750
....*....|....*....|....*....|....*...
gi 1389908274 2571 EDEAKKFKKQADEVKAQLQrtekhtteivVQKLETQRL 2608
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLE----------IEKEEKEKL 772
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2333-2574 |
1.30e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2333 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV 2412
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2413 klklkieeenrRLMQKDKDSTQKLLA-EEAEkmkSLAEEAGRLSVEAEETARQRQIAESnLAEQRALAEKILKEKMQAIQ 2491
Cdd:COG3883 93 -----------RALYRSGGSVSYLDVlLGSE---SFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2492 EATKLKAEAEK----LQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ 2567
Cdd:COG3883 158 ELEALKAELEAakaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1389908274 2568 TKAEDEA 2574
Cdd:COG3883 238 AAAAAAA 244
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
332-427 |
1.77e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.16 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 332 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-----------------------EN 387
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 388 LEQAFSVAER-----------ELG-VTKLLDPEDVDVPHPDEKSIITYVSSL 427
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1669-1887 |
1.80e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 60.74 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1669 RKAAQDEAERLRKQVAE----ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKmqAEEAERRMKQAEEEKIRQir 1744
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR--FEEIRLRKQRLEEERQRQ-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1745 vveevAQKSAATQLQTKAMSfsEQTTKLEESLKKeqgnvlKLQEEadKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1824
Cdd:pfam15709 404 -----EEEERKQRLQLQAAQ--ERARQQQEEFRR------KLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 1825 RLQAEEEaqkkshaQEEAEKQKLEAErdAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1887
Cdd:pfam15709 469 MEMAEEE-------RLEYQRQKQEAE--EKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
328-425 |
1.97e-08 |
|
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: 55.56 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 328 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 406
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1389908274 407 PEDVDVPHPDEKSIITYVS 425
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1747-2536 |
1.99e-08 |
|
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: 61.01 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1747 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQ-----------EEADKLKKQQKEANTAREEAEQELEIWR 1815
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdetLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1816 QKANEaLRLRLQAEEEA-QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQiAQQKLSAEQE 1894
Cdd:pfam12128 301 EKRDE-LNGELSAADAAvAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTG-KHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1895 CIRLKADFEHAeqqRGLLDNElQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINaekasmvNTEKSKQLLESEAL 1974
Cdd:pfam12128 379 RRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-------EFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1975 KMKQLADEAarmrSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL-KRQAEEE 2053
Cdd:pfam12128 448 ELKLRLNQA----TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeERQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2054 AYQRKL----------LEDQAAQHKQDIEEKITQ---LQTSSDSELGRQKNIVEETLKQKKVVEEEIHIikinfhkasKE 2120
Cdd:pfam12128 524 ELELQLfpqagtllhfLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV---------PE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2121 KADLESELKKLKGIADETqkskLKAEEEaeklkklaaeeerrrkeaeekvkRITAAEEEAArqckAAQEEVERLKKKAED 2200
Cdd:pfam12128 595 WAASEEELRERLDKAEEA----LQSARE-----------------------KQAAAEEQLV----QANGELEKASREETF 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2201 ANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLrdefeNAKKLAQEAEKAKEKAEKEAALLRQ 2280
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-----LDKKHQAWLEEQKEQKREARTEKQA 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2281 KAEEAEKQKKAAEnEAAKQAKAQndTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2360
Cdd:pfam12128 719 YWQVVEGALDAQL-ALLKAAIAA--RRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2361 VVKLQLDETdkqkvlLDQELQRVKGEVNDAFKQKSQVEVELARvriqMEELVKLKLKIEEENRrlmqKDKDSTQKLLAEE 2440
Cdd:pfam12128 796 RYFDWYQET------WLQRRPRLATQLSNIERAISELQQQLAR----LIADTKLRRAKLEMER----KASEKQQVRLSEN 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2441 AEKMKSLAEEAGRLSVEAEETARQRQIAESNlaeqRALAEkiLKEKMQAIQEATKLKAEAEKLQKQKDQAQ---ETAKRL 2517
Cdd:pfam12128 862 LRGLRCEMSKLATLKEDANSEQAQGSIGERL----AQLED--LKLKRDYLSESVKKYVEHFKNVIADHSGSglaETWESL 935
|
810 820
....*....|....*....|..
gi 1389908274 2518 QEDKQQI---QQRLDKETEGFQ 2536
Cdd:pfam12128 936 REEDHYQndkGIRLLDYRKLVP 957
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1854-2055 |
2.11e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 60.56 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1854 KKRGKAEEAALKQKENAEKEldkqrkfAEQIAQQKLS-AEQECIRLKADFEhaeqqrglldNELQRLKNEVNSTEKQRKQ 1932
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 LEDELNKvrsEMDSLlqmkinaekasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEA-KKQRQIAEEEAARQRSEA 2011
Cdd:PRK12704 94 KEENLDR---KLELL---------------EKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908274 2012 EKILKEKLaaineatRLKTEAEMALKAKEAENErLKRQAEEEAY 2055
Cdd:PRK12704 156 KEILLEKV-------EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2236-2784 |
2.15e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2236 VLSKNKEDVLAQ-EKLRDEFENAKK-LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEA 2313
Cdd:TIGR02169 227 ELLKEKEALERQkEAIERQLASLEEeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2314 EEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQ 2393
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2394 KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL------LAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2467
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2468 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ---QRLDKETEGFQKSLEAERK 2544
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHgtvAQLGSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2545 RQLEA--------SAEAEKLKLRVK--------------ELSLAQTKAEDEAKKF--------KKQADEVKAQLQRTekh 2594
Cdd:TIGR02169 547 NRLNNvvveddavAKEAIELLKRRKagratflplnkmrdERRDLSILSEDGVIGFavdlvefdPKYEPAFKYVFGDT--- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2595 tteIVVQKLETQRLQS-------------------TREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--I 2653
Cdd:TIGR02169 624 ---LVVEDIEAARRLMgkyrmvtlegelfeksgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrrI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2654 EQQKAELQQSFLTEKGLLLKREKEVE---GEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVR---- 2726
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKleea 780
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2727 ----KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVsQTKESQ 2784
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-QELQEQ 841
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1647-1855 |
2.53e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 60.18 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1647 HKAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQrkknaEDELKRKSDAEKEAaKQKQRALDDLqkykmqae 1726
Cdd:PRK12704 25 RKKIAEAKIKEAE---EEAKRILEEAKKEAEAIKKEALLEAK-----EEIHKLRNEFEKEL-RERRNELQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 eaERRMKQAEEekirqirvveevaqksaatQLQTKamsfSEQTTKLEESLKKEQGNVLKLQEEadkLKKQQKEANTAREE 1806
Cdd:PRK12704 88 --EKRLLQKEE-------------------NLDRK----LELLEKREEELEKKEKELEQKQQE---LEKKEEELEELIEE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 1807 AEQELE----IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1855
Cdd:PRK12704 140 QLQELErisgLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2401-2771 |
2.61e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2401 LARVRIQMEELVKLKLKIEEENRRLMQKdkdsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiAESNLAEQRALAE 2480
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2481 KIL------KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAE 2554
Cdd:COG4717 123 KLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2555 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhtteivVQKLETQR------------LQSTREADDLKSAIA 2622
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------EERLKEARlllliaaallalLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2623 DLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKA------ELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKA 2696
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAleeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2697 KALkdEQERQRKLMEEERKKL----QAIMDEAVRKQKEAEEEMKNKQREMDVLdkkrleqEKQLAEENKKLREQLQTFE 2771
Cdd:COG4717 357 EEL--EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEEL-------EEQLEELLGELEELLEALD 426
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1540-1887 |
2.80e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.89 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1540 RKMAEIQAELdkqKQMAEAHAKSVAKaeqealelKMKMKEEASKRQDVAadaEKQKQNIQQELQ----HLKSLSDQEIKS 1615
Cdd:COG2268 116 RDPEEIEELA---EEKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1616 KNQQLeDALvSRRKIEEEihiiriqleKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERlrkqvaeetqrkknaed 1695
Cdd:COG2268 182 ENNYL-DAL-GRRKIAEI---------IRDARIAEAEAE-RETEIAIAQANREAEEAELEQER----------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1696 ELKRKSDAEKEAAKQKQRAlddlqkykmqaeEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfseqttklees 1775
Cdd:COG2268 233 EIETARIAEAEAELAKKKA------------EERREAETARAEAEAAYEIAEANAEREVQRQLEIAE------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1776 lkkeqgnvlklQEEADKLKKQQKEantaREEAEQELEIwrQKANEALRLRLQAEEEAqkkshaqeEAEKQKLEAERDAKK 1855
Cdd:COG2268 288 -----------REREIELQEKEAE----REEAELEADV--RKPAEAEKQAAEAEAEA--------EAEAIRAKGLAEAEG 342
|
330 340 350
....*....|....*....|....*....|....
gi 1389908274 1856 RGKAEEAALKQKENAEKE--LDKQRKFAEQIAQQ 1887
Cdd:COG2268 343 KRALAEAWNKLGDAAILLmlIEKLPEIAEAAAKP 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1539-1949 |
2.83e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 60.58 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1539 RRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeASKRQDVaadaeKQKQniqQELQHLKSLSDQEIKSKNQ 1618
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL---NEMRQRY-----KEKT---QQLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1619 QLEDALVSRRKIEEeihiiriqLEKTTAHKAKSEAELQELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAED 1695
Cdd:PRK10246 494 EAQRAQLQAGQPCP--------LCGSTSHPAVEAYQALEPGVnqsRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1696 ELKRKSDAEKEAAKQKQRAL----------DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT-QLQTKAMS 1764
Cdd:PRK10246 566 EAQSLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQ 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1765 FSEQTTKLEESLKKEQGNVLKL---QEEADKLKKQQKEANTAREEAEQ---------------------ELEIWRQKANE 1820
Cdd:PRK10246 646 LLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQQltplletlpqsddlphseetvALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1821 ALRL-------RLQAEEEAQKKSHAQ---EEAEKQKLEAERDAKKRGKAEEAAL----KQKENAEKELDKQRKFAEQiAQ 1886
Cdd:PRK10246 726 CLSLhsqlqtlQQQDVLEAQRLQKAQaqfDTALQASVFDDQQAFLAALLDEETLtqleQLKQNLENQRQQAQTLVTQ-TA 804
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1887 QKLSAEQ----ECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQL-EDELNkvRSEMDSLLQ 1949
Cdd:PRK10246 805 QALAQHQqhrpDGLDLTVTVEQIQQELAQLA---QQLRENTTRQGEIRQQLkQDADN--RQQQQALMQ 867
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1641-2146 |
3.01e-08 |
|
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: 60.62 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1641 LEKTTAHKAKSEAELQElrdraaeaEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQK 1720
Cdd:pfam12128 258 LRLSHLHFGYKSDETLI--------ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1721 YKMQAEEAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEA 1800
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQ--SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1801 NTAREEAEQELEiwrqkaneALRLRLQAEEEAQKKShAQEEAEKQKLEAErDAKKR---GKAEEAALKQKENAEKELDKQ 1877
Cdd:pfam12128 407 DRQLAVAEDDLQ--------ALESELREQLEAGKLE-FNEEEYRLKSRLG-ELKLRlnqATATPELLLQLENFDERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1878 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ------------RKQL---EDELNKV-- 1940
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKVis 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1941 -----RSEMD------------SLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAarmRSVAEEAKKQ------- 1996
Cdd:pfam12128 557 pellhRTDLDpevwdgsvggelNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA---REKQAAAEEQlvqange 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1997 --RQIAEEEAARQrseAEKILKEKLAaineatRLKTEAEMALKAKEAENERLKRQAEEE----AYQRKLLEDqaaQHKQD 2070
Cdd:pfam12128 634 leKASREETFART---ALKNARLDLR------RLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDK---KHQAW 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2071 IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKA--SKEKADLESELKKLkGIaDETQKSKLKAE 2146
Cdd:pfam12128 702 LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG-AKAelKALETWYKRDLASL-GV-DPDVIAKLKRE 776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1646-2080 |
3.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1646 AHKAKSEAELQELRDRAA--EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELK----RKSDAEKEAAKQKQRALDDLQ 1719
Cdd:COG4913 265 AAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDalreELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEEslkkeqgnvlKLQEEADKLKKQQ 1797
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEefAALRAEAAALLEALEEELE----------ALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1798 KEANTAREEAEQELEIWRQKAN----EALRLRLQAEEEAQKKS------------HAQEE-----AEK------------ 1844
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEaelpfvgelievRPEEErwrgaIERvlggfaltllvp 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1845 ----------------------QKLEAERDAKKRGKAEEAALKQK----EN-----AEKELDKQRKFA-----EQIAQQK 1888
Cdd:COG4913 495 pehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkPHpfrawLEAELGRRFDYVcvdspEELRRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1889 LSAEQEC-IRLKAD-FEH---------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK 1951
Cdd:COG4913 575 RAITRAGqVKGNGTrHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1952 ------INAEKASMVNTEKSKQL--LESEALKMKQLADEaarmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEklaaIN 2023
Cdd:COG4913 655 eyswdeIDVASAEREIAELEAELerLDASSDDLAALEEQ-------LEELEAELEELEEELDELKGEIGRLEKE----LE 723
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2024 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT 2080
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1527-1768 |
3.29e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.43 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1527 DEKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvakaeQEalelkmKMKEEASKRQdvaADAEKQKQNIQQElqhlk 1606
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE----------QE------RLKQLEKERL---AAQEQKKQAEEAA----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1607 slsdQEIKSKNQQLEDAlvsrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1686
Cdd:PRK09510 125 ----KQAALKQKQAEEA------------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1687 TQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevAQKSAATQLQTKAMSFS 1766
Cdd:PRK09510 183 AKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA--------AEKAAAAKAAEKAAAAK 254
|
..
gi 1389908274 1767 EQ 1768
Cdd:PRK09510 255 AA 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1539-1807 |
3.57e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.50 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1539 RRKMAEIQAELDKQKQMAEAHA-KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQ--KQNIQQELQHLKSLSDQEIKS 1615
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAkkKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1616 KNQQLEDALvsrrKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAErlrkqvAEETQRKKNAED 1695
Cdd:COG2268 271 AEANAEREV----QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE------AEAIRAKGLAEA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1696 ELKRksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAeeEKIRQIRVVEEVAQKSAATQLQTKAMsfseqtTKLEES 1775
Cdd:COG2268 341 EGKR---ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPL--EKIDKITIIDGGNGGNGAGSAVAEAL------APLLES 409
|
250 260 270
....*....|....*....|....*....|..
gi 1389908274 1776 LKKEQGnvLKLQEEADKLKKQQKEANTAREEA 1807
Cdd:COG2268 410 LLEETG--LDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1702-2019 |
3.60e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.50 E-value: 3.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1702 DAEKEAAKQKQRalddlqkykmQAEEAERRMKQaEEEKIRQIRVVEEVAQKSAATQLQTKAMS----------FSEQTTK 1771
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSgqggldeeeaFLDRTAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1772 LEESLKKEQGNVLKLQEEADKLKKQQKE--ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShaQEEAEKQKLEA 1849
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKEsvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--KEYQENKWSTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRglldnelqRLKNEVNSTEKQ 1929
Cdd:pfam02029 149 VRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLDQK--------RGHPEVKSQNGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1930 RKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEK-------SKQLLESEAL-KMKQLADEAA-----------RMRSVA 1990
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQkleelrrRRQEKESEEFeKLRQKQQEAEleleelkkkreERRKLL 293
|
330 340
....*....|....*....|....*....
gi 1389908274 1991 EEAKKQRQIAEEEAARQRSEAEKILKEKL 2019
Cdd:pfam02029 294 EEEEQRRKQEEAERKLREEEEKRRMKEEI 322
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4212-4248 |
3.94e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.10 E-value: 3.94e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 4212 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4248
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
208-315 |
4.14e-08 |
|
third 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 55.01 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 278
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908274 279 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 315
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1770-2131 |
4.25e-08 |
|
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: 59.52 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1770 TKLEESLKkEQGNVLKLQEEADKLKKQQKEAntaREEAEQELEIWRQkaneALRLRLQ-AEEEAQKKSHAQEEAEKQKLE 1848
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKEKER---YKRDREQWERQRR----ELESRVAeLKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1849 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEK 1928
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1929 QRKQLEDELNKVRSEMD----SLLQMKINAEKASMVNTEKSKQLLESEALKmkqladeaARMRSVAEEAKKQRQIAE--- 2001
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL--------EELRSLQERLNASERKVEglg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2002 ---EEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA----ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEK 2074
Cdd:pfam07888 258 eelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2075 ITQLQtSSDSELGRQKNIveeTLKQKKVVEEEIHIIKINFHKASKEKADLESELKKL 2131
Cdd:pfam07888 338 RMERE-KLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1561-2221 |
5.20e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1561 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQ---ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHII 1637
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1638 RIQLEKTTAHKAKSEAELQELRDRAAEAEK-------LRKAAQDEAERLRKQVAEETQRKKNAEDELKRK-SDAEKEAA- 1708
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKmilafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEiNDKEKQVSl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1709 -----KQKQRALDDLQkykMQAEEAERRMKQAEEEKIRQIRVVEEVAQKS--AATQLQTKAMSFSEQTTK---LEESLKK 1778
Cdd:pfam05483 245 lliqiTEKENKMKDLT---FLLEESRDKANQLEEKTKLQDENLKELIEKKdhLTKELEDIKMSLQRSMSTqkaLEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1779 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL---RLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1855
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1856 RGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLkadFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLED 1935
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1936 ELNK----------------------VRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMK--QLADEaarMRSVAE 1991
Cdd:pfam05483 479 ELEKeklknieltahcdklllenkelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemNLRDE---LESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1992 EAKKQRQ-------IAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE---AENERLKRQAEEE-----AYQ 2056
Cdd:pfam05483 556 EFIQKGDevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEelhQENKALKKKGSAEnkqlnAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2057 RKL--LEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 2134
Cdd:pfam05483 636 IKVnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2135 ADETQKSKlkaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaEKEAEK 2214
Cdd:pfam05483 716 YDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL--------------KMEAKE 778
|
....*..
gi 1389908274 2215 QVVLAKE 2221
Cdd:pfam05483 779 NTAILKD 785
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1707-1879 |
5.44e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.86 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1707 AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvVEEVAQKSAAtqLQTKAMSFSEQTTKLEESLKKEQGNVLKL 1786
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1787 QEEADKLKKQQKEANTARE--EAEQELEIW--RQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKrgKAEEA 1862
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK--AELDE 149
|
170
....*....|....*..
gi 1389908274 1863 ALKQKENAEKELDKQRK 1879
Cdd:COG1579 150 ELAELEAELEELEAERE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1587-1846 |
6.25e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1587 VAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1666
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1667 KLRKAAQDEAERLRKQVAEE--TQRKKNAEDELKRKSDAEkeAAKQKQRALDDLQKYkmqaeeAERRMKQAEEekirqir 1744
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYL------APARREQAEE------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1745 vveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1824
Cdd:COG4942 155 ------LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 1389908274 1825 --RLQAEEEAQKKSHAQEEAEKQK 1846
Cdd:COG4942 229 iaRLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1719-1929 |
6.39e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.28 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1719 QKYKMQAEEAERRMKQAEEEKirqirvvEEVAQKSAATQLQTKAMsfsEQTTKLEESLKKEQGNVLKL----QEEADKLK 1794
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQaalkQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1795 KQQKEANTAREEAEQE-LEIWRQKANEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAeEAALKQKENAEK 1872
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEA-EAKKKAAAEAKK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 1873 ELDKQRKFAEQ--IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ 1929
Cdd:PRK09510 218 KAAAEAKAAAAkaAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1567-1903 |
6.98e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.73 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1567 EQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLS------DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQ 1640
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGqggldeEEAFLDRTAKREE---RRQKRLQEALERQKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1641 LEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDELKRKSDAEKEAAKQKQralddlQK 1720
Cdd:pfam02029 89 FDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK--EYQENKWSTEVRQAEEEGE------EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1721 YKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEA 1800
Cdd:pfam02029 160 EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1801 NTAREEAEQELEIWRQKANEAlrlrlqAEEEAQKKSHAQEEAEkqkLEAERDAKKRgkaeeaalKQKENAEKELDKQRKF 1880
Cdd:pfam02029 240 AEVFLEAEQKLEELRRRRQEK------ESEEFEKLRQKQQEAE---LELEELKKKR--------EERRKLLEEEEQRRKQ 302
|
330 340
....*....|....*....|...
gi 1389908274 1881 AEqiAQQKLSAEQECIRLKADFE 1903
Cdd:pfam02029 303 EE--AERKLREEEEKRRMKEEIE 323
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1532-1889 |
7.73e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.62 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1532 EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEaskRQDVAADAEKQKQNIQQELQhlkslsdq 1611
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY---RQELEEQIEEREQKRQEEYE-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1612 eiksknQQLEDALVSRRKIEEEIHIIRIQLEKttahKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1691
Cdd:pfam13868 95 ------EKLQEREQMDEIVERIQEEDQAEAEE----KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1692 NAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKamsfsEQTTK 1771
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIA-------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA-----EKKAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1772 LEESLKKEQgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAlrlRLQAEEEAQKKSHAQEEAEKQKLEAER 1851
Cdd:pfam13868 233 QRQELQQAR-----EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE---QEEAEKRRMKRLEHRRELEKQIEEREE 304
|
330 340 350
....*....|....*....|....*....|....*...
gi 1389908274 1852 dakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1889
Cdd:pfam13868 305 ---QRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1862-2084 |
8.72e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1862 AALKQKENAEKELdkqrkfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVR 1941
Cdd:COG4942 17 AQADAAAEAEAEL-------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1942 SEMDSLlQMKINAEKASMvntekSKQLleSEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAA 2021
Cdd:COG4942 90 KEIAEL-RAELEAQKEEL-----AELL--RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2022 INEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS 2084
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1528-1738 |
8.90e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1528 EKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvAADAEKQKQNiqqelqhlks 1607
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAKE---------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1608 lsdqeiKSKNQQLEDALVSrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDE----AERLRKQV 1683
Cdd:TIGR02794 147 ------EAAKQAEEEAKAK---------------AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 1684 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1738
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1773-1932 |
9.66e-08 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 58.09 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEeeAQKKSHAQEEAEKQKLEAERD 1852
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1853 AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsaeqecirlkadfeHAEQQRGLLD--NELQRLKNEVNSTEKQR 1930
Cdd:pfam05262 287 QIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEAQPTSL 351
|
..
gi 1389908274 1931 KQ 1932
Cdd:pfam05262 352 NE 353
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1773-2133 |
1.05e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQGNVLKLQEEADklkkQQKEANTAREEAEQELEIWRQKANEALRL-----RLQAE-EEAQKKSHAQEEA--EK 1844
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQqekieRYQADlEELEERLEEQNEVveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1845 QKLEAERDAKKRgKAEEAAL---KQKENAEKELDKQRKFAEQI--AQQKLSAEQECIRLK-----------ADFEHAEQQ 1908
Cdd:PRK04863 375 DEQQEENEARAE-AAEEEVDelkSQLADYQQALDVQQTRAIQYqqAVQALERAKQLCGLPdltadnaedwlEEFQAKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1909 rglLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkINAEKASmvntEKSKQLLEsEALKMKQLADEAARMRS 1988
Cdd:PRK04863 454 ---ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAW----DVARELLR-RLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1989 VAEEAKkQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALkakeaenERLKRQAEEEAYQRKLLEDQAAQHK 2068
Cdd:PRK04863 521 RLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2069 QDIEE---KITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKG 2133
Cdd:PRK04863 593 ARIQRlaaRAPAWLAAQDA-LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1859-2107 |
1.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1859 AEEAALKQKENAEKeLDKQRKFAEQIAQQKLSAE-QECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDEL 1937
Cdd:COG4913 240 AHEALEDAREQIEL-LEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1938 NKVRSEMDSLLQmkinaekasmvntekskQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE 2017
Cdd:COG4913 319 DALREELDELEA-----------------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2018 KLAAINEATRLKTEAemalkakeaenERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdselGRQKNIVEETL 2097
Cdd:COG4913 382 FAALRAEAAALLEAL-----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLE-------RRKSNIPARLL 443
|
250
....*....|
gi 1389908274 2098 KQKKVVEEEI 2107
Cdd:COG4913 444 ALRDALAEAL 453
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1882-2540 |
1.23e-07 |
|
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: 58.70 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1882 EQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQ----RLKNEVNSTEKQRKQLEDELN-----------KVRSEMDS 1946
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNgelsaadaavaKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1947 LLQMKINAEKAsmvNTEKSKQLLESEALKMKQLADEAARM-------RSVAEEAKKQRQIAEEEAARQRSEaekiLKEKL 2019
Cdd:pfam12128 327 LEDQHGAFLDA---DIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2020 AAINEA-TRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKItqlqtssdselgrqknIVEETL 2097
Cdd:pfam12128 400 AKIREArDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT----------------ATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2098 KQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkriTAAE 2177
Cdd:pfam12128 464 LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--------------------SALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2178 EEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvVLAKEAAQKC------TAAEQKAQDVLSKNKEDVLA----- 2246
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLRKEAPDWEQSIGK---------VISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2247 ----QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKqkkaaENEAAKQAKAQND------TEKQRKEAEEE 2316
Cdd:pfam12128 595 waasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKNARldlrrlFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2317 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQ-----LDETDKQKVLLDQELQRVKGEVNDAF 2391
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqvvEGALDAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2392 KQ-KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-----------------QKLLAEEAEKMKSLAEEAGR 2453
Cdd:pfam12128 750 KAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQevlryfdwyqetwlqrrPRLATQLSNIERAISELQQQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2454 LSVEAEETARQRQIAESNLAEQRALAEKIlkekmqaIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRL 2528
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGLRCEMSKLATLKedansEQAQGSIGERLAQLEDLKLKR 902
|
730
....*....|..
gi 1389908274 2529 DKETEGFQKSLE 2540
Cdd:pfam12128 903 DYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1762-1985 |
1.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1762 AMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKSHAQEE 1841
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1842 AEKQKLEAERD--------AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLD 1913
Cdd:COG4942 94 ELRAELEAQKEelaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 1914 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAAR 1985
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2051-2771 |
1.40e-07 |
|
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: 58.26 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2051 EEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKqkkvVEEEIhiikinFHKASKEKADLESELKK 2130
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETEL------CAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2131 LKGIADETQKsklKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaAEEEAARQcKAAQEEVE---RLKKKAEDankqkek 2207
Cdd:pfam01576 73 LEEILHELES---RLEEEEERSQQLQNEKKKMQQHIQDLEEQL--DEEEAARQ-KLQLEKVTteaKIKKLEED------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2208 aekeaekqvVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKlrdefENAKKLAQEAEKAKEKAEKEAALLRQKA---EE 2284
Cdd:pfam01576 140 ---------ILLLEDQNSKLSKERKLLEERISEFTSNLAEEE-----EKAKSLSKLKNKHEAMISDLEERLKKEEkgrQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2285 AEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL 2364
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2365 QLDETDKQKVLLDQELQRVKGEVNDAFkQKSQVEVELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQK------LLA 2438
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMRQKhtqaleELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2439 EEAEKMK-----------SLAEEAGRLSVE-------AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEA 2500
Cdd:pfam01576 363 EQLEQAKrnkanlekakqALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2501 EKLQKQKDQAQETAKRLQEDK-------QQIQQRLDKETEgfQKSLEAERKRQLeasaEAEKLKLRvkelslAQTKAEDE 2573
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETR--QKLNLSTRLRQL----EDERNSLQ------EQLEEEEE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 AKK-FKKQADEVKAQLQRTEKHTTEI--VVQKLETQRLQSTREADDLKSaiadleeerkklkkeaeelQRKSKEMAnaqQ 2650
Cdd:pfam01576 511 AKRnVERQLSTLQAQLSDMKKKLEEDagTLEALEEGKKRLQRELEALTQ-------------------QLEEKAAA---Y 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2651 EQIEQQKAELQQSfLTEKGLLLKREKEV----EGEKKRFEKQLEDEmkKAKALKDEQERQRKLMEEERKKLQAI-----M 2721
Cdd:pfam01576 569 DKLEKTKNRLQQE-LDDLLVDLDHQRQLvsnlEKKQKKFDQMLAEE--KAISARYAEERDRAEAEAREKETRALslaraL 645
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2722 DEAVRKQKEAEEEMKNKQREMDVLDKKR---------LEQEKQLAEEN-KKLREQLQTFE 2771
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKddvgknvheLERSKRALEQQvEEMKTQLEELE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1649-1879 |
1.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1649 AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaekeaaKQKQRALDDLQKykmQAEEA 1728
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-----------EALQAEIDKLQA---EIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1729 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNVLKLQEEA-DKLKKQQKEANTARE 1805
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSalSKIADADADLLEELKADkAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 1806 EAEQeleiwRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1879
Cdd:COG3883 158 ELEA-----LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1641-1991 |
1.84e-07 |
|
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: 58.04 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1641 LEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQrkknAEDELKRKsdaekeaAKQKQRALDDLQK 1720
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ----ALDVQQTR-------AIQYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1721 YKMQAEEAERRMKQAEeekirqirvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKlkkqQKEA 1800
Cdd:COG3096 425 ARALCGLPDLTPENAE----------DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAG----EVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1801 NTAREEAEQELEIWRQKANEALRLR-LQAE-EEAQKKSHAQEEAEKQkleAERDAKKRGKAEEAALkQKENAEKELDKQR 1878
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERL---LEEFCQRIGQQLDAAE-ELEELLAELEAQL 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1879 kfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLL----------DNELQRLKNEVNSTekqrkqLEDelnkvRSEMDSLL 1948
Cdd:COG3096 567 ---EELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQSGEA------LAD-----SQEVTAAM 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1389908274 1949 QMKINAEKASMVNTEKS---KQLLESEALKMKQLA-DEAARMRSVAE 1991
Cdd:COG3096 633 QQLLEREREATVERDELaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1594-1889 |
1.91e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 56.97 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1594 QKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTtAHKAKSEAELQELRDR----AAEAEKLR 1669
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE-QRKARLGREERRRADRrekqVIEKESRW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQ-----VAEETQRKKNAEDELKrksdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirQIR 1744
Cdd:pfam15558 97 REQAEDQENQRQEkleraRQEAEQRKQCQEQRLK-----EKEEELQALREQNSLQLQERLEEACHKRQLKEREE---QKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1745 VVEEVAQKSAATQLQTKAMSFSEQTTK------LEESLKKEQGN--------VLKLQEEADKLKKQQKEANTAREEAEQE 1810
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQAKAEEllrrlsLEQSLQRSQENyeqlveerHRELREKAQKEEEQFQRAKWRAEEKEEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1811 LEIWrqkanealrLRLQAEEEAQKKSHAQEEAEKQKLE-AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1889
Cdd:pfam15558 249 RQEH---------KEALAELADRKIQQARQVAHKTVQDkAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1593-2154 |
2.15e-07 |
|
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: 57.34 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1593 KQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAA 1672
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1673 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIR---QIRVVEEV 1749
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1750 AQKSaaTQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADK-------LKKQQKEANTAREEAEQELEIWRQK----- 1817
Cdd:TIGR04523 210 IQKN--KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKKikele 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1818 ------ANEALRLRLQAEEEAQKKSHAQ-EEAEKQKLEAERDAKKRGKA------------EEAALKQKENAEK--ELDK 1876
Cdd:TIGR04523 288 kqlnqlKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIisqlneqisqlkKELTNSESENSEKqrELEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1877 QRKFAEQIAQQKLSAEQECIRLKAD-------FEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1949
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQindleskIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1950 mKINAEKASMVNTEKSKQLLESealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAINEATRLK 2029
Cdd:TIGR04523 448 -QDSVKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2030 TEAEMALKAKEAENERLKRQAEEE------AYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVV 2103
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDElnkddfELKKENLEKEIDEKNKEIEE-LKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2104 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 2154
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1562-2132 |
2.23e-07 |
|
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: 57.44 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1562 SVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQL 1641
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKR-IRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1642 EktTAHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAE---ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1718
Cdd:pfam05557 86 E--ALNKKLNEKESQL-----ADAREVISCLKNELSELRRQIQRaelELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1719 QKYKMQAEEAERRMKQAEEEkirqirvveevAQKSAATQLQTKAMsfseqttkleeslKKEQGNVLKLQEEADKLKKQQK 1798
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFE-----------IQSQEQDSEIVKNS-------------KSELARIPELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1799 EANTAREEAeqelEIWRQKANEaLRLRLQAEEEAQKKShAQEEAEKQKLEAERDA-KKRGKAEEAALKQKENAekeldkq 1877
Cdd:pfam05557 215 HLNENIENK----LLLKEEVED-LKRKLEREEKYREEA-ATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDL------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1878 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE-------LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1950
Cdd:pfam05557 282 SRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1951 KINAEKaSMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRS-----EAEKILKEKLAAINEA 2025
Cdd:pfam05557 362 LESYDK-ELTMSNYSPQLLE----RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQqaqtlERELQALRQQESLADP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2026 TRLKTEAEmALKAK----EAENERLKRQAEE---EAYQRKLLEDQ--------------AAQHKQDIEEKITQLQtssdS 2084
Cdd:pfam05557 437 SYSKEEVD-SLRRKletlELERQRLREQKNElemELERRCLQGDYdpkktkvlhlsmnpAAEAYQQRKNQLEKLQ----A 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1389908274 2085 ELGRQKNIVEE-TLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 2132
Cdd:pfam05557 512 EIERLKRLLKKlEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQ 560
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1511-2717 |
2.23e-07 |
|
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: 57.75 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1511 NQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEAL--ELKMKMKEEA------- 1581
Cdd:TIGR01612 616 NEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALynELSSIVKENAidntedk 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1582 SKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIriQLEKTTAHKAKSEAEL-QELRD 1660
Cdd:TIGR01612 696 AKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKILEDFKNKEKELsNKIND 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1661 RAAEAEKLRKAAQDEAErLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqaeeAERRMKQAEEEKI 1740
Cdd:TIGR01612 774 YAKEKDELNKYKSKISE-IKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFK-------IINEMKFMKDDFL 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1741 RQIRVVEEVaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLklQEEADKLKKQQKEANTAREEAEQELEIWRqKANE 1820
Cdd:TIGR01612 846 NKVDKFINF-ENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDY--EKKFNDSKSLINEINKSIEEEYQNINTLK-KVDE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1821 ALRLrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK-----ENAEKELDKqrKFAEQIAQQKLSAEQEC 1895
Cdd:TIGR01612 922 YIKI-CENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKfdntlIDKINELDK--AFKDASLNDYEAKNNEL 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1896 IRLKADFehaeqQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKI-NAEKASMVNTEKSKQLLES 1971
Cdd:TIGR01612 999 IKYFNDL-----KANLGKNKENMLYHQFDEKEKATNDIEqkiEDANKNIPNIEIAIHTSIyNIIDEIEKEIGKNIELLNK 1073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1972 EALKMKQLAdeAARMRSVAEEAKKQR--QIAEEEAARQRSEAEKI------LKEKL-AAINEATRLKTEAEMALKAKEAE 2042
Cdd:TIGR01612 1074 EILEEAEIN--ITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIkddiknLDQKIdHHIKALEEIKKKSENYIDEIKAQ 1151
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2043 NERLKRQAEEEAYQrklledqaaQHKQDIEEKITQLQTSSDselgRQKNIVEETlkqKKVVEEeihIIKInfhkaSKEKA 2122
Cdd:TIGR01612 1152 INDLEDVADKAISN---------DDPEEIEKKIENIVTKID----KKKNIYDEI---KKLLNE---IAEI-----EKDKT 1207
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2123 DLEselkKLKGIADETQKS--KLKAEEEAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAED 2200
Cdd:TIGR01612 1208 SLE----EVKGINLSYGKNlgKLFLEKIDEEKKK----------------------SEHMIKAMEAYIEDLDEIKEKSPE 1261
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2201 ANKQKEKAEKEAEKQVVLakeaaqKCTAAEQKAQDVLSKNKEdvlaqEKLRDEFENAKKLAQEAEKAKEKaekeaallrq 2280
Cdd:TIGR01612 1262 IENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHD-----ENISDIREKSLKIIEDFSEESDI---------- 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2281 kaeeaekqkkaaeneaakqakaqNDTEKQRkeaeeeaarraaaeaaalkQKQQADAEmsKHKKEAEQALQQKSQVEKELT 2360
Cdd:TIGR01612 1321 -----------------------NDIKKEL-------------------QKNLLDAQ--KHNSDINLYLNEIANIYNILK 1356
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2361 VVKLQ--LDETDKQKVLLDQELQRVKGEVNdafkqKSQVEVELARVRIQMEELvklKLKIEEEnrrLMQKDKDSTQKLLA 2438
Cdd:TIGR01612 1357 LNKIKkiIDEVKEYTKEIEENNKNIKDELD-----KSEKLIKKIKDDINLEEC---KSKIEST---LDDKDIDECIKKIK 1425
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2439 EEaeKMKSLAEEAGRLSV--EAEETARQRQIAESNLAEQRALAEKILK-EKMQAIQEA----TKLKAEAEKLQKQKDQAQ 2511
Cdd:TIGR01612 1426 EL--KNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKiKKDNATNDHdfniNELKEHIDKSKGCKDEAD 1503
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2512 ETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA-EAEKLKLRVKEL----SLAQTKAEDEAKKFKKQADEVKA 2586
Cdd:TIGR01612 1504 KNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKkDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIED 1583
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2587 QLQRTEKHTTEIV-----VQKLETQRLQST----------READDLKSAIA----DLEEERKKLKKEAEELQRKSKEMAN 2647
Cdd:TIGR01612 1584 DAAKNDKSNKAAIdiqlsLENFENKFLKISdikkkindclKETESIEKKISsfsiDSQDTELKENGDNLNSLQEFLESLK 1663
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2648 AQQEQIEQQKAELQQsfLTEKglLLKREKEVEGEKKRFEKQLEDEMKK-AKALKDEQERQRKLMEEERKKL 2717
Cdd:TIGR01612 1664 DQKKNIEDKKKELDE--LDSE--IEKIEIDVDQHKKNYEIGIIEKIKEiAIANKEEIESIKELIEPTIENL 1730
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2431-2623 |
2.55e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2431 DSTQKLLAEEAEKMKSLA---EEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEKLQKQ 2506
Cdd:COG4913 238 ERAHEALEDAREQIELLEpirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2507 KDQAQEtakRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAqtkAEDEAKKFKKQADEVKA 2586
Cdd:COG4913 318 LDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*....
gi 1389908274 2587 QLQRTEKHTTEIVVQ--KLETQRLQSTREADDLKSAIAD 2623
Cdd:COG4913 392 LLEALEEELEALEEAlaEAEAALRDLRRELRELEAEIAS 430
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1673-2072 |
2.98e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.80 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1673 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAER-----RMKQAEEEKIRqirvve 1747
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1748 evaqksaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADKLkkqqkeANTAREEAEQELEIWRQKANEALRLRLQ 1827
Cdd:pfam02029 78 -----------------------RLQEALERQKEFDPTIADEKESV------AERKENNEEEENSSWEKEEKRDSRLGRY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1828 AEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQ 1907
Cdd:pfam02029 129 KEEETEIRE--KEYQENKWSTEVRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1908 QRglldnelqRLKNEVNStekqrKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKmkqladeaarmr 1987
Cdd:pfam02029 200 QK--------RGHPEVKS-----QNGEEEVTKLKVTTKRRQGGLSQSQERE----EEAEVFLEAEQKL------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1988 svaEEAKKQRQIAEEEaarqrsEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnERLKRQAEEEAYQRKllEDQAAQH 2067
Cdd:pfam02029 251 ---EELRRRRQEKESE------EFEKLRQKQQEAELELEELKKKREERRKLLEEE-EQRRKQEEAERKLRE--EEEKRRM 318
|
....*
gi 1389908274 2068 KQDIE 2072
Cdd:pfam02029 319 KEEIE 323
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2329-2816 |
3.10e-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: 57.05 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEvNDAFKQKS-----QVEVELA 2402
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTE-RDQFSQESgnlddQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2403 RVRIQMEELVKLKlkieEENRRLMQKDKDSTQKLlaeeaekmkslaeeaGRLSVEAEETARQRQIAESNLAEQRALAEKI 2482
Cdd:pfam15921 385 DLHKREKELSLEK----EQNKRLWDRDTGNSITI---------------DHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2483 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED---KQQIQQRLDKETEGFQKSLEaERKRQLEAS-AEAEKLKL 2558
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2559 RV----KELSLAQTKaEDEAKKFKKQADEVKAQLQRTEKhTTEIVVQKLE--TQRL-QSTREADDLKSaiadleeerkkl 2631
Cdd:pfam15921 525 RVdlklQELQHLKNE-GDHLRNVQTECEALKLQMAEKDK-VIEILRQQIEnmTQLVgQHGRTAGAMQV------------ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2632 kkeaeelqrkskEMANAQQEqIEQQKAELQQSfltekgLLLKREKEveGEKKRFEKQLED-EMKKAKALKDEQERQRKLM 2710
Cdd:pfam15921 591 ------------EKAQLEKE-INDRRLELQEF------KILKDKKD--AKIRELEARVSDlELEKVKLVNAGSERLRAVK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2711 EEERKKlqaimDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEK 2790
Cdd:pfam15921 650 DIKQER-----DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
490 500
....*....|....*....|....*.
gi 1389908274 2791 LVAVtTVGTSKGVLNGSTEVDGVKKE 2816
Cdd:pfam15921 725 AMKV-AMGMQKQITAKRGQIDALQSK 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1856 |
3.24e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1581 ASKRQDVAADAEKQKQNIQQELQHLKSlsdqeiksknqqledalvsrrkieeeihiiriQLEKTTAHKAKSEAELQELRD 1660
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEK--------------------------------ELAALKKEEKALLKQLAALER 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1661 RAAEAEKLRKAAQDEAERLRKQVAEETQRkknaEDELKRKSDAEKEAAKQKQRALddlqkYKMQAEEAERRMKQAEE--E 1738
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKE----IAELRAELEAQKEELAELLRAL-----YRLGRQPPLALLLSPEDflD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1739 KIRQIRVVEEVAQksaatQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKA 1818
Cdd:COG4942 134 AVRRLQYLKYLAP-----ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908274 1819 NEalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1856
Cdd:COG4942 209 AE-----LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2480-2765 |
3.73e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.50 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2480 EKILKEKMQAIQEATKLKAEAEKLQKQKDqAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2559
Cdd:pfam15709 214 ESKAEKKSELISKGKKTGAKRKRTQKERN-LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2560 VKELSLAQtkaedeakkfkkQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQ 2639
Cdd:pfam15709 293 IDGRSSPT------------QTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2640 RKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRfekQLEDEMKKAKALKDEQERQRKLMEEERKKLQA 2719
Cdd:pfam15709 361 RRLQQ---EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQAAQERARQQQEEFRRKLQE 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908274 2720 IMDEavRKQKEAEEEMKNKQRemdvldkkRLEQEKQLAEENKKLRE 2765
Cdd:pfam15709 435 LQRK--KQQEEAERAEAEKQR--------QKELEMQLAEEQKRLME 470
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1652-2016 |
3.76e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKrksDAEKEAAKQKQRALDDLQKykmQAEEAERR 1731
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELK---PSGQGGLDEEEAFLDRTAK---REERRQKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1732 MKQAEEEkirqirvveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTaREEAEQEl 1811
Cdd:pfam02029 79 LQEALER------------QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE-KEYQENK- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1812 eiWRQKANealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQklsA 1891
Cdd:pfam02029 145 --WSTEVR-------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1892 EQECIRLKadFEHAEQQRGLLDNELQRLKNEV-----NSTEKQRKQLEDelnKVRSEMDSLLQMKINAE------KASMv 1960
Cdd:pfam02029 213 EEEVTKLK--VTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAEleleelKKKR- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1961 ntEKSKQLLESEALKMKQLADEaarmRSVAEEAKKQRQiaEEEAARQRSEA-EKILK 2016
Cdd:pfam02029 287 --EERRKLLEEEEQRRKQEEAE----RKLREEEEKRRM--KEEIERRRAEAaEKRQK 335
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
799-891 |
4.37e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.18 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 799 HAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTA 878
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1389908274 879 ALQTQWSWLLQLC 891
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4315-4343 |
4.93e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.86 E-value: 4.93e-07
10 20
....*....|....*....|....*....
gi 1389908274 4315 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4343
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2417-2766 |
5.12e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.17 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2417 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeEAGRLSVEAEETARQRQIAESNlAEQRALAEKILKEKMQ---AIQEA 2493
Cdd:NF033838 69 KILSEIQKSLDKRKHTQNVALNKKLSDIKT---EYLYELNVLKEKSEAELTSKTK-KELDAAFEQFKKDTLEpgkKVAEA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2494 TKLKAEAEKlqKQKDQAQEtakrlqedkqqiqQRLDKETEGFqKSLEAERkrqleasAEAEkLKLRVKELSLAQTKAEDE 2573
Cdd:NF033838 145 TKKVEEAEK--KAKDQKEE-------------DRRNYPTNTY-KTLELEI-------AESD-VEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 AKKFKKQADEVKAQLQRTEKHTTEivvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ--E 2651
Cdd:NF033838 201 RDEEKIKQAKAKVESKKAEATRLE----KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2652 QIEQQKAELQQSFLTEKGL---LLKREKEV-EGEKKRFEKQledemKKAKALKDEQERQ-----RKLMEEE--------- 2713
Cdd:NF033838 277 DKKENDAKSSDSSVGEETLpspSLKPEKKVaEAEKKVEEAK-----KKAKDQKEEDRRNyptntYKTLELEiaesdvkvk 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2714 RKKLQAIMDEAVR-----KQKEAEEEMKNKQREMDVLD------KKRLEQEKQLAEENKKLREQ 2766
Cdd:NF033838 352 EAELELVKEEAKEprneeKIKQAKAKVESKKAEATRLEkiktdrKKAEEEAKRKAAEEDKVKEK 415
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1870-2066 |
5.25e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1870 AEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1949
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1950 -MKINAEKASMVNtekskQLLESE--------ALKMKQLAD-------EAARMRSVAEEAKKQRQIAEEEAARQRSEAEK 2013
Cdd:COG3883 94 aLYRSGGSVSYLD-----VLLGSEsfsdfldrLSALSKIADadadlleELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2014 ILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ 2066
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2278-2782 |
5.29e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2278 LRQKAEEAEKQKKAAENEAAKQAKAQndtEKQRKEaeeeaarraaaeaaalkqkqqadaeMSKHKKEAEQALQQKSQVEK 2357
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKEL---EEELKE-------------------------AEEKEEEYAELQEELEELEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2358 ELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKdkdstQKLL 2437
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLEE---LEERLEELRELEEEL-----EELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2438 AEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2517
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2518 QEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtt 2596
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2597 eivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ--QEQIEQQKAELQQSF-------LTE 2667
Cdd:COG4717 314 ----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQEIAALLAEAgvedeeeLRA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2668 KGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2747
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1389908274 2748 -----KRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2782
Cdd:COG4717 468 dgelaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1905-2075 |
5.65e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1905 AEQQRGLLDneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1984
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1985 RMRSVAEEAKKQRQIA-----EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKL 2059
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1389908274 2060 LEDQAAQHKQDIEEKI 2075
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1787-1922 |
5.73e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.65 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1787 QEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShAQEEAEKQ-KLEAERDAKKRGKAEEAALK 1865
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET-ARAEAEAAyEIAEANAEREVQRQLEIAER 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 1866 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADfEHAEQQ----RGLLDNELQRLKNE 1922
Cdd:COG2268 289 EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1504-1787 |
6.56e-07 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 56.38 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1504 SELMTLTNQYIKFIID---AQRRLEDDEKA---SEKLKEEERRKMAEI---QAEL---DKQKQMAEAHAKSVA-KAEQEA 1570
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLestDQNALETNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1571 L--ELKMKMKE-EASKRQDVAAD----------AEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIeeeihii 1637
Cdd:NF012221 1618 VtkELTTLAQGlDALDSQATYAGesgdqwrnpfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDA------- 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1638 riqLEKTTAHKAKSEAELQELRDRAAEAEKlrKAAQDEAERLRKQvaeetQRKKNAEdelkrkSDAEKEAAKQKQRALDD 1717
Cdd:NF012221 1691 ---VAKSEAGVAQGEQNQANAEQDIDDAKA--DAEKRKDDALAKQ-----NEAQQAE------SDANAAANDAQSRGEQD 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1718 LQKYKMQAEEAE---RRMKQAEEEKIRQIRV-----------VEEVAQKSAA--TQLQTKAMS-FSEQTTKLE-ESLKKE 1779
Cdd:NF012221 1755 ASAAENKANQAQadaKGAKQDESDKPNRQGAagsglsgkaysVEGVAEPGSHinPDSPAAADGrFSEGLTEQEqEALEGA 1834
|
....*...
gi 1389908274 1780 QGNVLKLQ 1787
Cdd:NF012221 1835 TNAVNRLQ 1842
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1494-1873 |
6.83e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1494 QEYVNLRTRYSELMTLTNQyIKFIIDAQRRLEDDEKASEKLKEEERR------KMAEIQAELDKQKQMAEAHAKSVAKAE 1567
Cdd:COG4717 102 EELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPERleeleeRLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1568 QEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQ------- 1640
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ----EELEELEEELEQLENELEAAALEERLKEARlllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1641 ----LEKTTAHKAKSEAELQEL-----------RDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEK 1705
Cdd:COG4717 257 allaLLGLGGSLLSLILTIAGVlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1706 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQ-----IRVVEEVAQKSAATQLQtKAMSFSEQTTKLEESLKKEQ 1780
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1781 GNVLKLQEEADK--LKKQQKEANTAREEAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1856
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREElaELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
410
....*....|....*..
gi 1389908274 1857 GKAEEAALKQKENAEKE 1873
Cdd:COG4717 496 KLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2416-2771 |
7.04e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2416 LKIEEENRRL------MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLA---EQRALAEKI---- 2482
Cdd:PRK04863 275 MRHANERRVHleealeLRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2483 ---------LKEKMQAIQEATKLKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEA-ERKRQLEA 2549
Cdd:PRK04863 355 adleeleerLEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQLADYQQALDvqqTRAIQYQQAVQAlERAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2550 SAeaeklklrvkelSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtteivvqkletQRLQSTREADD-------LKSAIA 2622
Cdd:PRK04863 432 LP------------DLTADNAEDWLEEFQAKEQEATEELLSLE-------------QKLSVAQAAHSqfeqayqLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2623 DLEEERKKLKKEAEELQRKSKEMANAQQ-EQIEQQKAELQQS-------------FLTEKGLLLKREKEVEGEKKRFEKQ 2688
Cdd:PRK04863 487 GEVSRSEAWDVARELLRRLREQRHLAEQlQQLRMRLSELEQRlrqqqraerllaeFCKRLGKNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2689 LED---EMKKAKALKDEQERQRKLMEEERKKLQAI------MDEAV-RKQKEAEEEMKNKQREMDVLdKKRLEQEKQLAE 2758
Cdd:PRK04863 567 LESlseSVSEARERRMALRQQLEQLQARIQRLAARapawlaAQDALaRLREQSGEEFEDSQDVTEYM-QQLLERERELTV 645
|
410
....*....|...
gi 1389908274 2759 ENKKLREQLQTFE 2771
Cdd:PRK04863 646 ERDELAARKQALD 658
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2378-2735 |
7.21e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2378 QELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL---MQKDKDSTQKLLAEEAEKMKSLAEEAGRL 2454
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldrTAKREERRQKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2455 SVEAEETARQRQIAESNLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQqiqqrldketeg 2534
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKE---EKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2535 fqKSLEAERKRQLEASAEAEKLKLRVKELslaqtKAEDEAKKF---KKQADEVKAQlqRTEKHTTEIVVQKLETQRLQST 2611
Cdd:pfam02029 162 --KSEEAEEVPTENFAKEEVKDEKIKKEK-----KVKYESKVFldqKRGHPEVKSQ--NGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2612 READDLKSAiadlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELqqsfltEKGLLLKREKEVEGEKKRFEKQLED 2691
Cdd:pfam02029 233 SQEREEEAE----VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAEL------ELEELKKKREERRKLLEEEEQRRKQ 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1389908274 2692 EMKKAKALKDEQERQRKlMEEERKKLQAimdeAVRKQKEAEEEM 2735
Cdd:pfam02029 303 EEAERKLREEEEKRRMK-EEIERRRAEA----AEKRQKLPEDSS 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2329-2520 |
7.43e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 7.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQA--LQQKSQVE----KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkQKSQVEVELA 2402
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2403 RVRIQMEELVKLKLKIEEENRRLMQKDKDSTQ----KLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRAL 2478
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA-------EAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908274 2479 AEKilkeKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2520
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2146-2533 |
8.29e-07 |
|
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: 55.29 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2146 EEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQK 2225
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2226 ctaaeqkaQDVLSKNKEDvlAQEKLRDEFENAKKLAQEAEKAKEKAEKeaalLRQKAEEAEKQKKAAENE-AAKQAKAQN 2304
Cdd:pfam07888 117 --------KDALLAQRAA--HEARIRELEEDIKTLTQRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2305 dTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKkeaeQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVK 2384
Cdd:pfam07888 183 -TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2385 GEVNDAFKQKSQVEVELARVRIQMEE----LVKLKLKIEEENRRlMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEE 2460
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRAR-WAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2461 TARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETE 2533
Cdd:pfam07888 337 ERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1249-2139 |
8.40e-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: 55.82 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1249 LTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEEtlkNYEARLRDVSK--------VPSEQKEVEKHRSQMKSMRSEAE 1320
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKE---AQLESSREIVKsyeneldpLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1321 ADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYRQLVNGLLERwqaVFAQIELRLRELDLLGRHMNSYRDSYEWLI 1400
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER---ELVDCQRELEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1401 RWLT-EARQRQEKIQAvpiSDSRALREQLTDEKKLLGEIEKNKDKIDDCHK--------NAKAYIDSVKDYEFQILTYKA 1471
Cdd:TIGR00606 350 GRLQlQADRHQEHIRA---RDSLIQSLATRLELDGFERGPFSERQIKNFHTlvierqedEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1472 LQDPIasplkKPKMECASDDIIQEYVNLRTRYSELmtltnqyiKFIIDAQRRLEDDEKASEKLKEEERRKMAEIqaELDK 1551
Cdd:TIGR00606 427 QADEI-----RDEKKGLGRTIELKKEILEKKQEEL--------KFVIKELQQLEGSSDRILELDQELRKAEREL--SKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1552 QKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIE 1631
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ--MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1632 EEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQR------KKNAEDELKRKSDAEK 1705
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1706 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSaaTQLQTKAMSFSEQTTKLEESLKKE------ 1779
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI--SDLQSKLRLAPDKLKSTESELKKKekrrde 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1780 -------QGNVL--------KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--------RLQAEEEAQKKS 1836
Cdd:TIGR00606 728 mlglapgRQSIIdlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERK 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1837 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD---FEHAEQQRGLLD 1913
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1914 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkiNAEKASMVNTEKSKQLLESEALKmKQLADEAARMRSVAEEa 1993
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISSKETSNKKAQDKVNDIK-EKVKNIHGYMKDIENK- 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1994 kkqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmalkakeaENERLKRQAEEEAYQR-KLLEDQAAQHKqdIE 2072
Cdd:TIGR00606 964 ------IQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN--------EDMRLMRQDIDTQKIQeRWLQDNLTLRK--RE 1027
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2073 EKITQLQTSSDSELGR--QKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQ 2139
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEmgQMQVLQMKQEHQK-LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1643-1940 |
8.78e-07 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 55.53 E-value: 8.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1643 KTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD----AEKEAAKQKQRALDDL 1718
Cdd:pfam09731 94 QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDdaiqAVKAHTDSLKEASDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1719 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTkleESLKKEQGNVLKLQEEADKLKKQQK 1798
Cdd:pfam09731 174 EISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLP---EHLDNVEEKVEKAQSLAKLVDQYKE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1799 EANTAREEAEQELE---------------IWRQKAN----------EALRLRLQaEEEAQKKSHAQEEAEKQKLE----- 1848
Cdd:pfam09731 251 LVASERIVFQQELVsifpdiipvlkednlLSNDDLNsliahahreiDQLSKKLA-ELKKREEKHIERALEKQKEEldkla 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1849 -----------AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLS---AEQEcIRLKADF-----EHAEQQR 1909
Cdd:pfam09731 330 eelsarleevrAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKdvlVEQE-IELQREFlqdikEKVEEER 408
|
330 340 350
....*....|....*....|....*....|....
gi 1389908274 1910 GLLDNELQRLKNEVNSTEKQ---RKQLEDELNKV 1940
Cdd:pfam09731 409 AGRLLKLNELLANLKGLEKAtssHSEVEDENRKA 442
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1602-1936 |
9.35e-07 |
|
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: 54.90 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1602 LQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK 1681
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1682 QVAEEtqrkknaedelKRKSDAEKEAAKQKQRALDDLQK---YKMQAEEAE-RRMKQAEEEKIRQIRVVEEVAQKSAATQ 1757
Cdd:pfam07888 112 ELSEE-----------KDALLAQRAAHEARIRELEEDIKtltQRVLERETElERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1758 LQTKA--MSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR---------QKANEALRLRL 1826
Cdd:pfam07888 181 QQTEEelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqerlnasERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1827 qaEEEAQKKSHAQEEAEKQKLEAE-------------RDAKKRGKAEEAALKQkeNAEKELDKQRKFAEQIAQ-QKLSAE 1892
Cdd:pfam07888 261 --SSMAAQRDRTQAELHQARLQAAqltlqladaslalREGRARWAQERETLQQ--SAEADKDRIEKLSAELQRlEERLQE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1893 QECIRLKADFEHAEQ------QRGLLDNELQRLKNEVNSTEKQRKQLEDE 1936
Cdd:pfam07888 337 ERMEREKLEVELGREkdcnrvQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1418-1851 |
9.39e-07 |
|
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: 55.41 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1418 ISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDyefQILTYKALQDPIASPL--KKPKMECASDDIIQE 1495
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT---QLNQLKDEQNKIKKQLseKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1496 YVNLRTRYSELMTLTNQYIKfiiDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKM 1575
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQ---DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1576 KMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSD--QEIKSKNQQLEDALvsrRKIEEEIHIIRIQLEKTTAHKAKSEA 1653
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkiQNQEKLNQQKDEQI---KKLQQEKELLEKEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1654 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaeKEAAKQKQRALDDLQKYKMQAEEAERRMK 1733
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1734 QAEEEKIRQIRVVEevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQ--GNVLKLQEEADKLKKQQKEANTAREEAEQEL 1811
Cdd:TIGR04523 517 KKISSLKEKIEKLE-----SEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1389908274 1812 EiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER 1851
Cdd:TIGR04523 592 D---QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2386-2574 |
1.03e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 55.01 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2386 EVNDAFKQKSQVEVELARVRIQMEELvklklKIEEENRRLMQKDKDSTQKllAEEAEKMKSLAEEAGRLSVEAEETARQR 2465
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKER-----ESQEDAKRAQQLKEELDKK--QIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2466 QIAESNLAEQRALAEKILKEKMQAIQeatklKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGF--QKSLEAER 2543
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEaeDKELEAQK 328
|
170 180 190
....*....|....*....|....*....|.
gi 1389908274 2544 KRqLEASAEAEKLKLRVKelslAQTKAEDEA 2574
Cdd:pfam05262 329 KR-EPVAEDLQKTKPQVE----AQPTSLNED 354
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1656-1958 |
1.11e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1656 QELRDRAAEAEKLRKAAQDEAERLRKQVA------EETQRK--------KNAEDELKRKSDAEKEAAKQKQRALddlqky 1721
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangelEKASREetfartalKNARLDLRRLFDEKQSEKDKKNKAL------ 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1722 kmqaeeaERRMKQAEeekirqirvveevaqksaatqlqtkamsfsEQTTKLEESLKKeqgNVLKLQEEADKLKKQQKEAN 1801
Cdd:pfam12128 674 -------AERKDSAN------------------------------ERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1802 TAREEAEQELEIWRQKANEALRLRLQAEEEAQKkshAQEEAEKQklEAERDAKKRGKAEEAALKQK---ENAEKELDKQR 1878
Cdd:pfam12128 714 TEKQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALET--WYKRDLASLGVDPDVIAKLKreiRTLERKIERIA 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1879 KFAEQIAQ----QKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-----------NSTEKQRKQLEDELNKVRSE 1943
Cdd:pfam12128 789 VRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTklrraklemerKASEKQQVRLSENLRGLRCE 868
|
330
....*....|....*
gi 1389908274 1944 MDSLLQMKINAEKAS 1958
Cdd:pfam12128 869 MSKLATLKEDANSEQ 883
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1518-1826 |
1.12e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1518 IDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN 1597
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1598 IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAE 1677
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1678 RLRKQVAEETQRKKNAEdelkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQ 1757
Cdd:pfam13868 205 ELRAKLYQEEQERKERQ--------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 1758 LQtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1826
Cdd:pfam13868 277 EQ-------EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2451-2793 |
1.19e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.14 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2451 AGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKL----------KAEAEKLQKQKDQAQETAKRLQED 2520
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2521 KQQI--------QQRLDKETEGFQKSLE--AERKRQLEASAEAEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQL 2588
Cdd:pfam07111 138 SQREleeiqrlhQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2589 QRTE---KHTTEIVVQKLETQRLQSTREA--DDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE--QQKAELQ 2661
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQEllDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRkiQPSDSLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2662 QSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQRKLMEEERKklQAIMDEAVR-KQKEAEEE---M 2735
Cdd:pfam07111 298 PEFPKKCRSLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsA 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2736 KNKQREMDVLDKKRLEQEKQLAEENKKLReqlqtFEISSKTVSQTK-ESQTVSVEKLVA 2793
Cdd:pfam07111 376 KGLQMELSRAQEARRRQQQQTASAEEQLK-----FVVNAMSSTQIWlETTMTRVEQAVA 429
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2278-2768 |
1.31e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2278 LRQKAEEAEKQKKA---AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQA-DAEMSKHKKEAEQALQQKS 2353
Cdd:COG4913 240 AHEALEDAREQIELlepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2354 QVEKELTVVKLQLDETDkqkvllDQELQRVKGEVNDAFKQKSQVEVELARvriQMEELVKLKLKIEEEnRRLMQKDKDST 2433
Cdd:COG4913 320 ALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRAR---LEALLAALGLPLPAS-AEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2434 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI---LKEKMQAIQEATKLKAE-----AEKLQ- 2504
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAelpfvGELIEv 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2505 KQKDQAQETA----------------KRLQE-----DKQQIQQRLDkeTEGFQKSLEAERKRQLEASAEAEKLKLRVKEL 2563
Cdd:COG4913 470 RPEEERWRGAiervlggfaltllvppEHYAAalrwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2564 S------LAQTKA------EDEAKKFKK---QADEVKAQLQRTEKHTTEIV-------------VQKLETQRLQSTREAD 2615
Cdd:COG4913 548 RawleaeLGRRFDyvcvdsPEELRRHPRaitRAGQVKGNGTRHEKDDRRRIrsryvlgfdnrakLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2616 DLKSAIADLEEERKKLKKEAEELQRKSK--------EMANAQQEQIEQQKAELQQSF--LTEkglLLKREKEVEGEKKRF 2685
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSddLAA---LEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2686 EKQLEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE 2765
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
...
gi 1389908274 2766 QLQ 2768
Cdd:COG4913 781 RLN 783
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1657-2043 |
1.37e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 54.34 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1657 ELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKK--------NAEDELKRKSDAEKEAakqkQRALDDLQKYKMQAeea 1728
Cdd:pfam03528 5 DLQQRVAELEKENA----EFYRLKQQLEAEFNQKRakfkelylAKEEDLKRQNAVLQEA----QVELDALQNQLALA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1729 errmkQAEEEKIRQIRVVEEVAQKSAATQLQTKamsFSEQTTKLEeSLKKEQGNVLKLQEEAdKLKKQQKEANTAREEAE 1808
Cdd:pfam03528 74 -----RAEMENIKAVATVSENTKQEAIDEVKSQ---WQEEVASLQ-AIMKETVREYEVQFHR-RLEQERAQWNQYRESAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1809 QELEIWRQKANEAlrlrlQAEEEAQKK-SHAQEEAEKQkleaeRDAKKRGKAEEAALKQK-ENAEKELDKQRKFAEQIAQ 1886
Cdd:pfam03528 144 REIADLRRRLSEG-----QEEENLEDEmKKAQEDAEKL-----RSVVMPMEKEIAALKAKlTEAEDKIKELEASKMKELN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1887 QKLSAEQECirlKADFEhaeQQRGLLDNELQRLKNEvnsTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvntekSK 1966
Cdd:pfam03528 214 HYLEAEKSC---RTDLE---MYVAVLNTQKSVLQED---AEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-------ND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1967 QLLESEALKMKQLadeaARMRSV--------AEEAKKQRQIAEEEA-ARQRSEAEKILKEKLAAINEATRLKTEAEMALK 2037
Cdd:pfam03528 278 QFLESQRLLMRDM----QRMESVltseqlrqVEEIKKKDQEEHKRArTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
....*.
gi 1389908274 2038 AKEAEN 2043
Cdd:pfam03528 354 SNVEEQ 359
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1640-1922 |
1.43e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.77 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVaEETQRKKNAEDELKRKSDAEKeaakqKQRALDDLQ 1719
Cdd:pfam13868 60 EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEK-----QRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1799
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREEDERIL--------EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1800 ANTAREEAEQElEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------KAEEAALKQKENAEKE 1873
Cdd:pfam13868 206 LRAKLYQEEQE-RKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEfermlrKQAEDEEIEQEEAEKR 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1874 LDKQRKFAEQIAQQKLSAEQECIRLKAD-FEHAEQQRGLLDNELQRLKNE 1922
Cdd:pfam13868 285 RMKRLEHRRELEKQIEEREEQRAAEREEeLEEGERLREEEAERRERIEEE 334
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2006-2614 |
1.52e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2006 RQRSEAEKILKEKLAAINEatrlKTEAEMALKAKEAENERLKRQAEEEAYQRKllEDQAAQHKQDIEEKITQLqtssdse 2085
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE----KEEKDLHERLNGLESELAELDEEIERYEEQ--REQARETRDEADEVLEEH------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2086 lgrqknivEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEklkklaaeeerrrke 2165
Cdd:PRK02224 247 --------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2166 aeekvkrITAAEEEAArqcKAAQEEVERLKKKAEDAnkqkekaekeAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL 2245
Cdd:PRK02224 304 -------LDDADAEAV---EARREELEDRDEELRDR----------LEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2246 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEa 2325
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2326 aalkQKQQADAEMSKHkKEAEQALQQKSQVEKeltvvklqLDETDKQKVLLDQELQRVKGEVNDafkqksqVEVELARVr 2405
Cdd:PRK02224 443 ----EEAEALLEAGKC-PECGQPVEGSPHVET--------IEEDRERVEELEAELEDLEEEVEE-------VEERLERA- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2406 iqmEELVKLKLKIE--EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNlAEQRALAEKIL 2483
Cdd:PRK02224 502 ---EDLVEAEDRIErlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAEL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2484 KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKslEAERKRQLEASAEA---EKLKLRV 2560
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE--KRERKRELEAEFDEariEEAREDK 655
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2561 KELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREA 2614
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1654-2128 |
1.71e-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: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1654 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEdelKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMK 1733
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAE---LARLEAELERLEARLDALRE------ELDELEAQIR 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1734 QAEEEKIRQIRvvEEVAQK-SAATQLQTKAMSFSEQTTKLEeslkkeqgnvLKLQEEADKLKKQQKEANTAREEAEQELE 1812
Cdd:COG4913 334 GNGGDRLEQLE--REIERLeRELEERERRRARLEALLAALG----------LPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1813 IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQK------LEAERDAKKR--GKAEEAA--------LKQKEN-----AE 1871
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparLLALRDALAEalGLDEAELpfvgelieVRPEEErwrgaIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1872 KEL-----------DKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQ------------------RGLLDNELQRLKNE 1922
Cdd:COG4913 482 RVLggfaltllvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPrldpdslagkldfkphpfRAWLEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 --VNSTEkqrkQLEDE-----------LNKVRSEMD------SLLQM------KINAEKASMVNTEKSKQLLESEALKMK 1977
Cdd:COG4913 562 vcVDSPE----ELRRHpraitragqvkGNGTRHEKDdrrrirSRYVLgfdnraKLAALEAELAELEEELAEAEERLEALE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1978 QLADEAARMRSVAEEAKKQR--QIAEEEAARQRSEaekiLKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY 2055
Cdd:COG4913 638 AELDALQERREALQRLAEYSwdEIDVASAEREIAE----LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKG 713
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 2056 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ---KKVVEEEIHIIKINFHKASKEKADLESEL 2128
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2242-2726 |
1.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2242 EDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRA 2321
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2322 AAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKV-LLDQELQRVKGEVNDAFKQKSQVEVE 2400
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2401 LARVRiqmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAE 2480
Cdd:COG4717 208 LAELE---EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2481 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLR 2559
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2560 VKE--------LSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkkl 2631
Cdd:COG4717 365 LEEleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2632 kkeaeelqRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKL 2709
Cdd:COG4717 438 --------EEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|....*..
gi 1389908274 2710 MEEerkKLQAIMDEAVR 2726
Cdd:COG4717 510 REE---RLPPVLERASE 523
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1665-2019 |
1.78e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.38 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1665 AEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRksdaEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIR 1744
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK----EEERKEERKRYRQELEE---QIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1745 VVEEVAQKsaatqlqtkamsfseqttkleeslkkeqgnvLKLQEEADKLKKQQKEANTARE--EAEQELEIWRQKANEAL 1822
Cdd:pfam13868 102 QMDEIVER-------------------------------IQEEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1823 RLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqrkfAEQIAQQKLSAEQECIRLKADF 1902
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE------RDELRAKLYQEEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1903 EHAEQQRGLLDNELQRLKNEVnstEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADE 1982
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQI---ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908274 1983 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 2019
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2000-2768 |
2.19e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 54.35 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2000 AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 2079
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID---LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2080 TSSdSELGRQKNIVEETLKQKKV--------------VEEEIHIIKINFHKASKEKA----------------------- 2122
Cdd:pfam15921 149 NTV-HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIyehdsmstmhfrslgsaiskilr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2123 DLESELKKLKG--IADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR---QCKAAQEEVERLKKK 2197
Cdd:pfam15921 228 ELDTEISYLKGriFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSarsQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2198 AEDANKQKEKAEKEAEKQVvlakeaaqkctaaeqkaqdvlsknkedvlaqEKLRDEFENAKKLAQeaekakekaekeaal 2277
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTV-------------------------------SQLRSELREAKRMYE--------------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2278 lrQKAEEAEKQKKAAENEAAkQAKAQNDTEKQRKEAEEeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEK 2357
Cdd:pfam15921 342 --DKIEELEKQLVLANSELT-EARTERDQFSQESGNLD-------------DQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2358 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNdAFKQKSQVEVELARVRIQ-----MEELVKLKLKIEEENRRLMQKDKDS 2432
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLEALLK-AMKSECQGQMERQMAAIQgknesLEKVSSLTAQLESTKEMLRKVVEEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2433 T-QKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNLAEQRALAEkiLKekmqaIQEATKLKAEAEKLQKQkdQAQ 2511
Cdd:pfam15921 485 TaKKMTLESSERTVS------DLTASLQEKERAIEATNAEITKLRSRVD--LK-----LQELQHLKNEGDHLRNV--QTE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2512 ETAKRLQ-EDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLaqtkaedEAKKFKKQADEVKAQLQR 2590
Cdd:pfam15921 550 CEALKLQmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL-------ELQEFKILKDKKDAKIRE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2591 TEKHTTEIVVQKLE-----TQRLQSTREA--------DDLKSAIADLEEERKKLKKEAEELQRKSKEM---ANAQQEQIE 2654
Cdd:pfam15921 623 LEARVSDLELEKVKlvnagSERLRAVKDIkqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2655 QQKAELQQSFLTEKGL----------LLKREKEVEGEKKRFEKqLEDEMKKAKALKDEQERQRKLMEEERKKL-QAIMDE 2723
Cdd:pfam15921 703 SAQSELEQTRNTLKSMegsdghamkvAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLsQELSTV 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2724 AVRKQKEA---------EEEMKNKQREMDV-LDKKRLE----QEKQLAEENKKLREQLQ 2768
Cdd:pfam15921 782 ATEKNKMAgelevlrsqERRLKEKVANMEVaLDKASLQfaecQDIIQRQEQESVRLKLQ 840
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2232-2516 |
2.36e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.88 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2232 KAQDVLSKNKEDvLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEK--- 2308
Cdd:pfam05667 204 VVPSLLERNAAE-LAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAElls 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2309 ------QRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSqvEKELTVVKLQLDETDKQKVLLDQELQR 2382
Cdd:pfam05667 283 sfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2383 VKGEVndafkqkSQVEVELARVRIQMEEL---VKLK------LKIEEENRRLMQKD-KDSTQKL--LAEEAEKMKS-LAE 2449
Cdd:pfam05667 361 LESSI-------KQVEEELEELKEQNEELekqYKVKkktldlLPDAEENIAKLQALvDASAQRLveLAGQWEKHRVpLIE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2450 EAGRLSVeaeetarqrQIAESNLAEQRALAE-KILKEKMQAIQEATKLKAEAEK-LQKQKDQAQETAKR 2516
Cdd:pfam05667 434 EYRALKE---------AKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEELYKqLVAEYERLPKDVSR 493
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1652-1908 |
2.53e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.45 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRkAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR 1731
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEE-ARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1732 MKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQEL 1811
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1812 EIWRQKANEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAL-KQKEN-----AEKELDKQRKFAE 1882
Cdd:PRK07735 163 EKAKAKAAAAAKAKaaaLAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALaKQKASqgngdSGDEDAKAKAIAA 242
|
250 260
....*....|....*....|....*.
gi 1389908274 1883 QIAQQKLSAEQECIRLKADFEHAEQQ 1908
Cdd:PRK07735 243 AKAKAAAAARAKTKGAEGKKEEEPKQ 268
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
210-309 |
2.64e-06 |
|
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: 49.58 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 210 DRVQKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 285
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1389908274 286 LVNIRNDDIADGNPKLTLGLIWTI 309
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1652-1812 |
2.75e-06 |
|
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: 51.85 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQ-----KQRALDDLQKykmQAE 1726
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQK---EIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 EAERRMKQAEEEkirQIRVVEEVAQKSAATQLQTKAMSfseqttKLEESLKKEQGnvlKLQEEADKLKKQQKEANTAREE 1806
Cdd:COG1579 100 SLKRRISDLEDE---ILELMERIEELEEELAELEAELA------ELEAELEEKKA---ELDEELAELEAELEELEAEREE 167
|
....*.
gi 1389908274 1807 AEQELE 1812
Cdd:COG1579 168 LAAKIP 173
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1492-2149 |
3.22e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.93 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1492 IIQEYVNLRTRYSEL--MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKqkqmAEAHAKSVAKAEQE 1569
Cdd:COG5022 792 KWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGR----SLKAKKRFSLLKKE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1570 ALELKMKMKEEASKRQDVaadaEKQKQNiqQELQHLKSLS---DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQLEKtta 1646
Cdd:COG5022 868 TIYLQSAQRVELAERQLQ----ELKIDV--KSISSLKLVNlelESEIIELKKSLSS---DLIENLEFKTELIARLKK--- 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1647 HKAKSEAELQELRdraaEAEKLRKAAQD-EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1725
Cdd:COG5022 936 LLNNIDLEEGPSI----EYVKLPELNKLhEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1726 EEAERRMKQaeeekiRQIRVVEevaqksaatqlQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1805
Cdd:COG5022 1012 QESTKQLKE------LPVEVAE-----------LQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1806 -EAEQELEIWRQKANEALRLRLQA-EEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQ 1883
Cdd:COG5022 1075 nSLLDDKQLYQLESTENLLKTINVkDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1884 IA-----QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNStekqrkqLEDELNKVRSEMDSLLQMKI---NAE 1955
Cdd:COG5022 1155 ELdglfwEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVND-------LKNELIALFSKIFSGWPRGDklkKLI 1227
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1956 KASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrqiaeeeaARQRSEAEKILKEKLAAI--NEATRLKTEAE 2033
Cdd:COG5022 1228 SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNS---------IDNLLSSYKLEEEVLPATinSLLQYINVGLF 1298
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2034 MALKAKEAENERlkRQAEEEAYQRKLLEDQAAQHK-QDIEEKITQLQTSSDSELGRQKNIveETLKQKKVVEEEIHIIKI 2112
Cdd:COG5022 1299 NALRTKASSLRW--KSATEVNYNSEELDDWCREFEiSDVDEELEELIQAVKVLQLLKDDL--NKLDELLDACYSLNPAEI 1374
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908274 2113 NFHKASKEKADLESELKK--LKGIADETQKSKLKAEEEA 2149
Cdd:COG5022 1375 QNLKSRYDPADKENNLPKeiLKKIEALLIKQELQLSLEG 1413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1944-2485 |
3.43e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1944 MDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLAAI 2022
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2023 NEATRLKTEAEMALKAKEAENERLKRQAEEeayqRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKV 2102
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2103 VEEEIHIIKINFHKASKEKADLESELKKLkgiadetqKSKLKAEEEAEKLKKLAAEEERrrkeaeekvkritaaeeeAAR 2182
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLI------------------AAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2183 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQkctaAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQ 2262
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2263 EAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQrkeaeeeaarraAAEAAALKQKQQADAEMSKHK 2342
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG------------VEDEEELRAALEQAEEYQELK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2343 KEAEQAlqqKSQVEKELTVVKLQLDETDKQKvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEEN 2422
Cdd:COG4717 402 EELEEL---EEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQL--------EED 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2423 RRLMQKdkdstQKLLAEEAEKMKSLAEEAGRLSVEAE--ETARQRQIaESNLAEQRALAEKILKE 2485
Cdd:COG4717 469 GELAEL-----LQELEELKAELRELAEEWAALKLALEllEEAREEYR-EERLPPVLERASEYFSR 527
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1864-2065 |
3.88e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1864 LKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlkadfehAEQQRglldneLQRLKNEVNSTEKQRKQLEDELNKVRSE 1943
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1944 MDsllqmkiNAEKASMVNTEKSKQLLESEAlkmKQLADEAARmrsVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAIN 2023
Cdd:PRK09510 131 QK-------QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908274 2024 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 2065
Cdd:PRK09510 195 AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1522-1807 |
4.05e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1522 RRLEDDEKASEKLKE--EERrkmaeiQAELDKQKQMAEAHAKsvAKAEQEAlelkmkmkeeASKRQDVAADAEKQKQNIQ 1599
Cdd:PRK05035 439 RAIEQEKKKAEEAKArfEAR------QARLEREKAAREARHK--KAAEARA----------AKDKDAVAAALARVKAKKA 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1600 QELQhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERL 1679
Cdd:PRK05035 501 AATQ--PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1680 RKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAerRMKQAEEEKIRQIRVVEEVAQKSAATQlq 1759
Cdd:PRK05035 579 KAAVAAAIARAKA-----KKAAQQAASAEPEEQVAEVDPKKAAVAAAIA--RAKAKKAEQQANAEPEEPVDPRKAAVA-- 649
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1389908274 1760 tKAMSFSeqttkleESLKKEQGNVLKLQEEADKLKKQQKEANTAREEA 1807
Cdd:PRK05035 650 -AAIARA-------KARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2281-2613 |
4.20e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2281 KAEEAEKQKKAAENEAAKQAKAQND---TEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEK 2357
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2358 ELTVVKLQLD-ETDKQKVLLDQ-ELQRVKGEVNDAFKQKSQVEVElarvriqmEELVKLKLKIEEENRRLMQKDKDSTQK 2435
Cdd:pfam07888 128 EARIRELEEDiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2436 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQ---- 2511
Cdd:pfam07888 200 SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQRDRTQaelh 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2512 --------------ETAKRLQEDKQQIQQrldkETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKF 2577
Cdd:pfam07888 276 qarlqaaqltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGRE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908274 2578 KkqaDEVKAQLQRTEKHTTEI-----VVQKLETQRLQSTRE 2613
Cdd:pfam07888 352 K---DCNRVQLSESRRELQELkaslrVAQKEKEQLQAEKQE 389
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1690-1949 |
4.83e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 51.15 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1690 KKNAEDELKRKsdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRvvEEVAQKSAATQLQTKAMSFSEQT 1769
Cdd:pfam12795 6 EKAKLDEAAKK--KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAE-LRELR--QELAALQAKAEAAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1770 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQAEEEAQKkshAQEEAEKQKLEA 1849
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQ-IRNRLNGPAPPGE---PLSEAQRWALQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ERdakkrgkaeeAALKQkenaekELDKQRKfaeqiAQQKLSAEQECIRLKADFEHAEQQRglLDNELQRLKNEVNS---- 1925
Cdd:pfam12795 157 EL----------AALKA------QIDMLEQ-----ELLSNNNRQDLLKARRDLLTLRIQR--LEQQLQALQELLNEkrlq 213
|
250 260
....*....|....*....|....*
gi 1389908274 1926 -TEKQRKQLEDELNKVRSEMDSLLQ 1949
Cdd:pfam12795 214 eAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2362-2568 |
4.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2362 VKLQLDETDKQKVLLDQELQRVKGEVNDA------FKQKS-------QVEVELARVRIQMEELVKLKLKIEEENRRLmqk 2428
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAeaaleeFRQKNglvdlseEAKLLLQQLSELESQLAEARAELAEAEARL--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2429 dkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAES------------NLAEQRALAEKILKEKMQAIQEATK- 2495
Cdd:COG3206 243 --AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdviALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2496 ----LKAEAEKLQKQKDQAQETAKRLQEdKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2568
Cdd:COG3206 321 eleaLQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVV 396
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1652-1947 |
5.21e-06 |
|
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: 53.03 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1652 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedelkrksdaekEAAKQKQRALDDLQKYKM-------- 1723
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQL----------------------DQLKEQLQLLNKLLPQANlladetla 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1724 -QAEEAERRMKQAEEEK--IRQirvveevaQKSAATQLQTKAMSFsEQTTKLEESLKKEqgnVLKLQEEADKLKKQ---- 1796
Cdd:COG3096 893 dRLEELREELDAAQEAQafIQQ--------HGKALAQLEPLVAVL-QSDPEQFEQLQAD---YLQAKEQQRRLKQQifal 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1797 ----QKEANTAREEAEQELEIwRQKANEALRLRL-QAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKENAe 1871
Cdd:COG3096 961 sevvQRRPHFSYEDAVGLLGE-NSDLNEKLRARLeQAEEARREAREQLRQAQAQYSQY--------NQVLASLKSSRDA- 1030
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 1872 keldKQRKFAEqiAQQKLSAeqecIRLKADFEHAEQQRGlldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL 1947
Cdd:COG3096 1031 ----KQQTLQE--LEQELEE----LGVQADAEAEERARI----RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1727-2106 |
5.44e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 EAERRMKQAEEEKIRQI---RVVEEVAQKSAATQLQTKAMSFSEQTTKLE-------ESLKKEQGNVL---KLQEEADKL 1793
Cdd:NF012221 1468 DFARRAGLSTNNGIEVLwngEVVFASSGDASAWQQKTLKLTAKAGSNRLEfkgtghnDGLGYILDNVVatsESSQQADAV 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1794 KKQQKEaNTAREEAEQEleiwrQKANEALRLRLQAEEEAQ----KKSHAQEEA-EKQKLEaerdakKRGKAEEAALKQKE 1868
Cdd:NF012221 1548 SKHAKQ-DDAAQNALAD-----KERAEADRQRLEQEKQQQlaaiSGSQSQLEStDQNALE------TNGQAQRDAILEES 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1869 NA-EKELDKQRKFAEQIAQQKLSAEQECIRLKADFehAEqqrGLLDNelqrlknevnstekqrkqledelnkVRSEMDsl 1947
Cdd:NF012221 1616 RAvTKELTTLAQGLDALDSQATYAGESGDQWRNPF--AG---GLLDR-------------------------VQEQLD-- 1663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1948 lqmkiNAEKASMVNTEKSKQLLESEALKMKqlaDEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATR 2027
Cdd:NF012221 1664 -----DAKKISGKQLADAKQRHVDNQQKVK---DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQ 1735
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2028 LKTEAEMALKAKEAENERLKRQAEEEAYQrklLEDQAAQHKQDIEEKITQlQTSSDSELGRQKNIVEETLKQKKVVEEE 2106
Cdd:NF012221 1736 AESDANAAANDAQSRGEQDASAAENKANQ---AQADAKGAKQDESDKPNR-QGAAGSGLSGKAYSVEGVAEPGSHINPD 1810
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1826-2031 |
5.62e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 LQAEEEAQK-KSHAQEEAEKQKLEAERDAKkrgkaeEAALKQKENAEKEL-DKQRKFAEQiaqqklsaEQeciRLKADFE 1903
Cdd:PRK12704 34 KEAEEEAKRiLEEAKKEAEAIKKEALLEAK------EEIHKLRNEFEKELrERRNELQKL--------EK---RLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1904 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdelnKVRSEMDSLLQMKINA-EKASMVNTEKSKQLLesealkMKQLADE 1982
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEEQLQElERISGLTAEEAKEIL------LEKVEEE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1983 AarmrsVAEEAKKQRQIaEEEAarqRSEAEKILKEKLA-AIneaTRLKTE 2031
Cdd:PRK12704 167 A-----RHEAAVLIKEI-EEEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2334-2735 |
5.73e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2334 ADAEMSKHKKEAEQAlqQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK 2413
Cdd:PRK02224 307 ADAEAVEARREELED--RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRRE 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2414 LKLKIEEENRRLMQKDKDSTQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEK------------ 2481
Cdd:PRK02224 385 EIEELEEEIEELRERFGDAPVDL-GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveg 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2482 -----ILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQqRLDKETEGFQKSLEAERKRQLEASAEAEKL 2556
Cdd:PRK02224 464 sphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEEL 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2557 KLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAE 2636
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL---KERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2637 ELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLmEE 2712
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEyleqVEEKLDELREERDDLQAEIGAVENELEELEEL-RE 698
|
410 420
....*....|....*....|....*
gi 1389908274 2713 ERKKLQAIMD--EAVRKQKEAEEEM 2735
Cdd:PRK02224 699 RREALENRVEalEALYDEAEELESM 723
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
208-316 |
6.03e-06 |
|
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: 48.44 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 278
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908274 279 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1752-1949 |
6.04e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1752 KSAATQLQTKAMSFSEQTTKLEESLK--KEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANealRLRLQAE 1829
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA---ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1830 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE-KELDKQRkfAEQIAQQKLSAEQECIRLKADFEHAEQQ 1908
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQI--AALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908274 1909 RGLLDNELQRLKNEV---NSTEKQRKQLEDELNKVRSEMDSLLQ 1949
Cdd:COG3206 329 EASLQAQLAQLEARLaelPELEAELRRLEREVEVARELYESLLQ 372
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1966-2127 |
6.28e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1966 KQLLESEALKMKQLAD---EAARMRsvAEEAKKQRQI-AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 2041
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2042 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT--SSDSELGRQ--KNIVEETLKqKKVVEEEIHIIKiNFHKA 2117
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
170
....*....|
gi 1389908274 2118 SKEKADLESE 2127
Cdd:PRK12704 182 AKEEADKKAK 191
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2446-2660 |
6.32e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2446 SLAEEAGRLSvEAEETARQRQIAESNLAEQRA--LAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQ 2523
Cdd:PRK09510 59 AVVEQYNRQQ-QQQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQ----ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2524 IQQRLDKETEGFQKSLEAERKRQLEASAEAEklklrvkelSLAQTKAEDEAKKfkKQADEVKAQLQRTEKHTTEIVVQKL 2603
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---------AEAKKKAEAEAAK--KAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2604 ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2660
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2427-2597 |
6.54e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2427 QKDKDSTQKLLAE--EAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEK 2502
Cdd:PRK09510 74 AKRAEEQRKKKEQqqAEELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAAKAKAEAEA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2503 lqkqkDQAQETAKRLQEDKQQiqqrldKETEGFQKSLEAERKRQLEASAEAeklklrvkelslaqtKAEDEAKKFKKQAD 2582
Cdd:PRK09510 154 -----KRAAAAAKKAAAEAKK------KAEAEAAKKAAAEAKKKAEAEAAA---------------KAAAEAKKKAEAEA 207
|
170
....*....|....*
gi 1389908274 2583 EVKAQLQRTEKHTTE 2597
Cdd:PRK09510 208 KKKAAAEAKKKAAAE 222
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2461-2767 |
6.67e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2461 TARQRQIAEsnlAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE 2540
Cdd:pfam13868 22 KERDAQIAE---KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2541 AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvqkLETQRLQSTREADdlksa 2620
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI---LEYLKEKAEREEE----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2621 iadleeeRKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgLLLKREKEvEGEKKRFEKQLEDEMKKAKALK 2700
Cdd:pfam13868 171 -------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDE-------LRAKLYQE-EQERKERQKEREEAEKKARQRQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2701 DEQERQRKLMEEERKKLQaimdEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2767
Cdd:pfam13868 236 ELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1703-1958 |
6.88e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1703 AEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGN 1782
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1783 VLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLRLQAEEEAQkkshaqeeaekqkleAERDA---KKRGKA 1859
Cdd:COG4942 85 LAELEKEIAELRAELEA--QKEELAELLRALYRLGRQPPLALLLSPEDFLD---------------AVRRLqylKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1860 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLdneLQRLKNEVNSTEKQRKQLEDELNK 1939
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*....
gi 1389908274 1940 VRSEMDSLLQMKINAEKAS 1958
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1275-1835 |
7.02e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1275 IRNTADAEETLKNYEARL----RDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSER 1350
Cdd:PRK03918 185 IKRTENIEELIKEKEKELeevlREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1351 DADLEHYRQLVNGLLERWQAVfAQIELRLRELDLLGRHMNSYRDSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTD 1430
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1431 EKKLLGEIEKNKDKIDDchknakayidSVKDYEfqilTYKALQDPIASpLKKPKMECASDDIIQEYVNLRTRYSELMTLT 1510
Cdd:PRK03918 343 LKKKLKELEKRLEELEE----------RHELYE----EAKAKKEELER-LKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1511 NQYIKFIIDAQRRLEDDEKASEKLK---------------EEERRKMAEIQAELDK-QKQMAEAHAK-SVAKAEQEALEL 1573
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEEYTAELKRiEKELKEIEEKeRKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1574 KMKMKEEASKRQDVAadaeKQKQNIQQELqhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEA 1653
Cdd:PRK03918 488 VLKKESELIKLKELA----EQLKELEEKL---KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1654 ---ELQELRDRAAEAEK-LRKAAQDEAERLRKQVAE------ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1723
Cdd:PRK03918 561 lekKLDELEEELAELLKeLEELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1724 QAEEAERRMKQAE----EEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1799
Cdd:PRK03918 641 RLEELRKELEELEkkysEEEYEELR--------EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908274 1800 ANTArEEAEQELEIWRQKaneALRLRLQAEEEAQKK 1835
Cdd:PRK03918 713 LEKL-EKALERVEELREK---VKKYKALLKERALSK 744
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
1526-2023 |
7.42e-06 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 52.34 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1526 DDEKASEKLKEEERRKMAEIQAELDKQKQmAEAHAKSVAKAE---QEALELKMKMKEEASKRQDVAADAEKQKQNIQQEL 1602
Cdd:pfam01271 69 EASHLSSRSRDGLSDEDMQIITEALRQAE-NEPGGHSRENQPyalQVEKEFKTDHSDDYETQQWEEEKLKHMRFPLRYEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1603 QHLKSLSDQEIKSKNQQLedalvsrrkieeeIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLrkaAQDEAERLRKQ 1682
Cdd:pfam01271 148 NSEEKHSEREGELSEVFE-------------NPRSQATLKKVFEEVSRLDTPSKQKREKSDEREKS---SQESGEDTYRQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1683 --VAEETQRKKNAEDElkrksDAEKEaakqkqralddlqkyKMQAEEAERRMKQaEEEKIRQIrvvEEVAQKSAATQLQT 1760
Cdd:pfam01271 212 enIPQEDQVGPEDQEP-----SEEGE---------------EDATQEEVKRSRP-RTHHGRSL---PDESSRGGQLGLEE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1761 KAMSFSEQTTKLEESLKKEQGNVLKLqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--RLQAEEEAQKK--- 1835
Cdd:pfam01271 268 EASEEEEEYGEESRGLSAVQTYLLRL-VNARGRGRSEKRAERERSEESEEEELKRASPYEELEItaNLQIPPSEEERmlk 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1836 ----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDK--QRKFAEQIAQQ-------KLSAEQECIRLKADF 1902
Cdd:pfam01271 347 kagrSPRGRVDEAGALEALEALEEKRKLDLDHSRVFESSEDGAPRapQGAWVEALRNYlsygeegMEGKWNQQGPYFPNE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1903 EHAEQQRGLLDNELQRLKNE-------VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSkqlLESEALK 1975
Cdd:pfam01271 427 ENREEARFRLPQYLGELSNPwedpkqwKPSDFERKELTADKFLEGEEENEYTLSMKNSFPEYNYDGYEKR---VPSPGLD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 1976 MKQLADEAAR---------------MRSVAEEAKKQRQIA--EEEAARQRSEAEKILKEKLAAIN 2023
Cdd:pfam01271 504 LKRQYDPVARedqllhyrkkssefpDFYDSEEKKEPPVGAekEEDSANRQTRDEDKELENLAAMD 568
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
213-320 |
8.62e-06 |
|
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: 48.50 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 279
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908274 280 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 320
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2329-2784 |
8.94e-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: 52.48 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEaEQALQQKSQVEKELTVVKLQLDETDkqkvLLDQELQRVKGEvndafKQKSQVEVELARVRIQM 2408
Cdd:pfam01576 99 KKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKIKKLEED----ILLLEDQNSKLS-----KERKLLEERISEFTSNL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EElvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSlaEEAGRLSVEAEETARQRQIAE--SNLAEQRALAEKILKEK 2486
Cdd:pfam01576 169 AE--------EEEKAKSLSKLKNKHEAMISDLEERLKK--EEKGRQELEKAKRKLEGESTDlqEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2487 MQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQrlDKETEGFQKSLEAERKRQLEASAEAEKLKL-------- 2558
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE--DLESERAARNKAEKQRRDLGEELEALKTELedtldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2559 --------RVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREAddLKSAIADLEEERK 2629
Cdd:pfam01576 317 aqqelrskREQEVTELKKALEEETRSHEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQA--LESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2630 KLKKEAEELQRKSKEMANAQQE-QIEQQKAELQQSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQ 2706
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSELEsVSSLLNEAEGKNIKLSKDVSSLESQlQDTQ 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2707 RKLMEEERKKLQAimdeaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2784
Cdd:pfam01576 475 ELLQEETRQKLNL-----STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2942-2978 |
9.70e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.70e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 2942 RLLSAERAATGFKDPYTGAKISLFEAMNKGLIEKEQA 2978
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1275-2099 |
9.95e-06 |
|
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: 52.36 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1275 IRNTADaEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLR-KATTVHDKMT----RIHSE 1349
Cdd:TIGR01612 801 IDNIKD-EDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKeKIDSEHEQFAeltnKIKAE 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1350 -RDADLEHYRQLVNGllerwqaVFAQIELRLRELDLLGRHMNSYR--DSYEWLIRWLTEARQRQEKIQAVpisdsraLRE 1426
Cdd:TIGR01612 880 iSDDKLNDYEKKFND-------SKSLINEINKSIEEEYQNINTLKkvDEYIKICENTKESIEKFHNKQNI-------LKE 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1427 QLTDEKKLLGE---IEKN-KDKIDDCHKNAKAYID------SVKDYEFQILTYKALQDPIASPLKKPK----------ME 1486
Cdd:TIGR01612 946 ILNKNIDTIKEsnlIEKSyKDKFDNTLIDKINELDkafkdaSLNDYEAKNNELIKYFNDLKANLGKNKenmlyhqfdeKE 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1487 CASDDIIQEYVNLRTRYSELMTLTNQYIKFIID--------------------AQRRLEDDEKASEKLK--------EEE 1538
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDeiekeigkniellnkeileeAEINITNFNEIKEKLKhynfddfgKEE 1105
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1539 RRKMA----EIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADA---------EKQKQNIQQELQHL 1605
Cdd:TIGR01612 1106 NIKYAdeinKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeeiEKKIENIVTKIDKK 1185
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1606 KSLSDQ---------EIKSKNQQLEDalVSRRKIEEEIHIIRIQLEKTTAHKAKSE----------AELQELRDRAAEAE 1666
Cdd:TIGR01612 1186 KNIYDEikkllneiaEIEKDKTSLEE--VKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiEDLDEIKEKSPEIE 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1667 KLRKAAQDEAERLR-------KQVAEETQRKKNAED--ELKRKSDAEKEAAKQKQRALD---DLQKYKMQAEEAERRMKQ 1734
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDikkELQKNLLDAQKHNSDINL 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1735 AEEE--------KIRQIR-VVEEVaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlKLQEEADKLK----------- 1794
Cdd:TIGR01612 1344 YLNEianiynilKLNKIKkIIDEV--KEYTKEIEENNKNIKDELDKSEKLIKKIKDDI-NLEECKSKIEstlddkdidec 1420
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1795 -KQQKEANTAREEAEQELEIWRQKA---NEALRLRLQAEEEAQKKSHAQEEAEK-----------QKLEAERDAKKRGKA 1859
Cdd:TIGR01612 1421 iKKIKELKNHILSEESNIDTYFKNAdenNENVLLLFKNIEMADNKSQHILKIKKdnatndhdfniNELKEHIDKSKGCKD 1500
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1860 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAeqecIRLKADFEHAEQQRGLLDNELQRLKN----EVNSTEKQRKQLED 1935
Cdd:TIGR01612 1501 EADKNAKAIEKNKELFEQYKKDVTELLNKYSA----LAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKK 1576
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1936 ElnKVRSEMDSllqMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrQIAEEEAARQRSEaekiL 2015
Cdd:TIGR01612 1577 E--KFRIEDDA---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDTE----L 1645
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2016 KEKLAAINEatrLKTEAEmALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIE----EKITQLQTSSDSELGRQKN 2091
Cdd:TIGR01612 1646 KENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKE 1721
|
....*...
gi 1389908274 2092 IVEETLKQ 2099
Cdd:TIGR01612 1722 LIEPTIEN 1729
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
212-313 |
9.96e-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: 47.80 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 212 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 287
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1389908274 288 NIRNDDIADGNPKLTLGLIWTIILHF 313
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2041-2153 |
9.98e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.14 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2041 AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKI---NFHK 2116
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEaKKEADEIIKELRQlqkGGYA 602
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908274 2117 ASKEKaDLESELKKLKGIADETQKSKLKAEEEAEKLK 2153
Cdd:PRK00409 603 SVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3268-3304 |
9.99e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.99e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 3268 RLLSAEKAVSGYHDPYTGKKVSLFEALKLGLIKKDHG 3304
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1607-1779 |
1.04e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 51.54 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1607 SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAelQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1686
Cdd:pfam05262 176 SISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEEL--DKKQIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1687 TQRKKNAEDELKRKSDAEKE--AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAtQLQTKAMS 1764
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKqvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKEL-EAQKKREP 332
|
170
....*....|....*
gi 1389908274 1765 FSEQTTKLEESLKKE 1779
Cdd:pfam05262 333 VAEDLQKTKPQVEAQ 347
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2117-2777 |
1.05e-05 |
|
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: 52.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2117 ASKEKADLESELKKLKG--IADETQKSKLKaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2194
Cdd:pfam12128 249 EFNTLESAELRLSHLHFgyKSDETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2195 ---KKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA-EQKAQDVLSKNKedvlAQEKLRDEfENAKKLAQEAEKAKEK 2270
Cdd:pfam12128 328 edqHGAFLDADIETAAADQEQLPSWQSELENLEERLKAlTGKHQDVTAKYN----RRRSKIKE-QNNRDIAGIKDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2271 AekeaallrqkaEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALK--------------QKQQADA 2336
Cdd:pfam12128 403 R-----------EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2337 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkqksqvevelarvriqMEELVKLKL 2416
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL-----------------ELQLFPQAG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2417 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETA-----RQRQI-------AESNLAEQRALAEKIL- 2483
Cdd:pfam12128 535 TLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvklDLKRIdvpewaaSEEELRERLDKAEEALq 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2484 --KEKMQAIQEA-TKLKAEAEKLQKQK-------DQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEaERKRQLEasAEA 2553
Cdd:pfam12128 615 saREKQAAAEEQlVQANGELEKASREEtfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2554 EKLKLRVKELSLAQTKAEDEAKKFKKQADEVkaqLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKK 2633
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2634 EAEELQRKSKEMaNAQQEQIEQQKAE-------LQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkkaKALKDEQERQ 2706
Cdd:pfam12128 769 VIAKLKREIRTL-ERKIERIAVRRQEvlryfdwYQETWLQRRPRLATQLSNIERAISELQQQL-------ARLIADTKLR 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2707 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQR--------EMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2777
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedanseQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNV 919
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1582-1835 |
1.17e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 51.23 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1582 SKRQDVaadAEKQKqNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKseaelqeLRDR 1661
Cdd:PRK11637 51 SIQQDI---AAKEK-SVRQQQQQRASLLAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAK-------LEQQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1662 AAEAEKLRKAAQDEAERLRKQVA-------EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrmKQ 1734
Cdd:PRK11637 119 QAAQERLLAAQLDAAFRQGEHTGlqlilsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEE-----KQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1735 AEEEKIrqirvveeVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKL-QEEA---DKLKKQQKEantAREEAEQ 1809
Cdd:PRK11637 194 SQQKTL--------LYEQQAQQQKLEQARNERKKTlTGLESSLQKDQQQLSELrANESrlrDSIARAERE---AKARAER 262
|
250 260
....*....|....*....|....*.
gi 1389908274 1810 EleiwrqkANEALRLRlQAEEEAQKK 1835
Cdd:PRK11637 263 E-------AREAARVR-DKQKQAKRK 280
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4100-4138 |
1.17e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.17e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1389908274 4100 YLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTAFEL 4138
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
317-427 |
1.26e-05 |
|
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: 47.49 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 317 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVA 395
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 396 ERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 427
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1649-1739 |
1.50e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1649 AKSEAELQELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAE--------KEAAKQKQRALDDLQK 1720
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*
gi 1389908274 1721 YKM------QAEEAERRMKQAEEEK 1739
Cdd:PRK00409 599 GGYasvkahELIEARKRLNKANEKK 623
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1768-1978 |
1.69e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.61 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1768 QTTKLEESLKKEQGNVLKlQEEADKLKKQQKEANTAREEAEQELEiwRQKANEA----LRLRLQAEEEAQKKSHAQEEAE 1843
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQ-QQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQArqkeLEQRAAAEKAAKQAEQAAKQAE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1844 KQKLEAERdAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAE----QECIRLKADFEHAEQQrgllDNELQRL 1919
Cdd:TIGR02794 116 EKQKQAEE-AKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEakkkAEEAKKKAEAEAKAKA----EAEAKAK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 1920 KNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQ 1978
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1833-2042 |
1.82e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1833 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRgll 1912
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ----KQAEEAAAKAA--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1913 dnELQRLKnevnsTEKQRKQLEDELNKVRSEMDsllqmKINAEKASMVNTEKSKQLLESEAlkmKQLADEAARMRSVAEE 1992
Cdd:PRK09510 143 --AAAKAK-----AEAEAKRAAAAAKKAAAEAK-----KKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 1993 AKKQRQIAEEEAARQ-RSEAEKILKEKLAAINEATRLKTEAEMALKAKEAE 2042
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2445-2659 |
1.84e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 50.23 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2445 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKilkekmQAIQEATKLKAEAEKLQKQKD--QAQETAKRLQEDKQ 2522
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAakQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2523 QIQQRLDKETEGFQKSLEAERKRQLEA----SAEAEKLKlrvKELSLAQTKAEdEAKkfKKQADEVKAQLQRTEKHTTEI 2598
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEeaakQAEEEAKA---KAAAEAKKKAE-EAK--KKAEAEAKAKAEAEAKAKAEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2599 VVQKLETQRLQSTRE----ADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2659
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEaaakAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1791-2155 |
1.86e-05 |
|
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: 50.89 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1791 DKLKKQQKEANTAREEAEqeleiwrqkaNEALRLRLQAEEEAQKKSHAQEEAEK-QKLEAERDAKKRGKAEEAALKQK-- 1867
Cdd:pfam05557 16 NEKKQMELEHKRARIELE----------KKASALKRQLDRESDRNQELQKRIRLlEKREAEAEEALREQAELNRLKKKyl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1868 ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLkNEVNSTEKQRKQledELNKVRSEMDSL 1947
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL-QERLDLLKAKAS---EAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1948 LQMKINAEkASMVNTEKSKQLLESEALKMKQLADEAARMRSVaeEAKKQRQIAEEEAARQRSEAEKILKEKLAAINeaTR 2027
Cdd:pfam05557 162 QSSLAEAE-QRIKELEFEIQSQEQDSEIVKNSKSELARIPEL--EKELERLREHNKHLNENIENKLLLKEEVEDLK--RK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2028 LKTEAEMALKAKEAENERLKRQAEEEAYQrKLLEDQAAQHK--QDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEE 2105
Cdd:pfam05557 237 LEREEKYREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRspEDLSRRIEQLQ-QREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2106 EIHIIKINfhkASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 2155
Cdd:pfam05557 315 ELEQELAQ---YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4098-4135 |
1.91e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.91e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1389908274 4098 KKYLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTA 4135
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1543-1955 |
2.02e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1543 AEIQAELD---KQKQmAEAHAKSVAKAEQEALEL---KMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSK 1616
Cdd:PRK11281 39 ADVQAQLDalnKQKL-LEAEDKLVQQDLEQTLALldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1617 -----NQQLEDALVSRRkieeeihiiriqlekttahkakseAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1691
Cdd:PRK11281 118 lstlsLRQLESRLAQTL------------------------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1692 NAEDELKrKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM-------------KQAEEEKIRQIRVVEEVAqksaatQL 1758
Cdd:PRK11281 174 QIRNLLK-GGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKslegntqlqdllqKQRDYLTARIQRLEHQLQ------LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1759 QT----KAMSFSEQTTKLEESLKKEQgnvlklQEEADKLKKQQKEANTareEAEQELEIWRQKANEALRLRLQAeeeaqk 1834
Cdd:PRK11281 247 QEainsKRLTLSEKTVQEAQSQDEAA------RIQANPLVAQELEINL---QLSQRLLKATEKLNTLTQQNLRV------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1835 kshaqeeaeKQKLE----AERDAKKRGKAEEAAL-------KQKENAEKeLDKQRKFAEQIAQqklsaeqecIRLKAdFE 1903
Cdd:PRK11281 312 ---------KNWLDrltqSERNIKEQISVLKGSLllsrilyQQQQALPS-ADLIEGLADRIAD---------LRLEQ-FE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1904 hAEQQRGLL-------DNELQRLKNEVNSTEKQ--------RKQLEDELNKvrsEMDSLLQMKINAE 1955
Cdd:PRK11281 372 -INQQRDALfqpdayiDKLEAGHKSEVTDEVRDallqlldeRRELLDQLNK---QLNNQLNLAINLQ 434
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2376-2730 |
2.11e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.21 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2376 LDQELQRVKGEVNDAfkQKSQVEVELARVRIQMEElvklklKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEagRLS 2455
Cdd:PRK10929 28 ITQELEQAKAAKTPA--QAEIVEALQSALNWLEER------KGSLERAKQYQQVIDNFPKLSAELRQQLNNERDE--PRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2456 VEAEETARqrqiaesnlaeqrALAEKILKEKMQAIQEATKLKAEAEKLQKQKD------QAQETAKRLQEDkqqIQQRLd 2529
Cdd:PRK10929 98 VPPNMSTD-------------ALEQEILQVSSQLLEKSRQAQQEQDRAREISDslsqlpQQQTEARRQLNE---IERRL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2530 ketEGFQKSLEAERKRQLEA-SAEAEKLKLRVKELSLAQTKAED-------EAKKFKKQADEVKAQLQRTEKHTTEIVVQ 2601
Cdd:PRK10929 161 ---QTLGTPNTPLAQAQLTAlQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQALRNQLNSQRQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2602 KLEtQRLQSTR----EADDLKSAIADlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKrE 2675
Cdd:PRK10929 238 EAE-RALESTEllaeQSGDLPKSIVA-QFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQalNTLREQSQWLG-V 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 2676 KEVEGEKKRFE----------KQLEDEMKK--AKALK--DEQERQRKLMEEERKKLQA-------IMDEAVRKQKE 2730
Cdd:PRK10929 315 SNALGEALRAQvarlpempkpQQLDTEMAQlrVQRLRyeDLLNKQPQLRQIRQADGQPltaeqnrILDAQLRTQRE 390
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3638-3673 |
2.13e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.13e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1389908274 3638 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMA 3673
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
350-427 |
2.28e-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: 46.14 E-value: 2.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 350 DNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSvAERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 427
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3599-3635 |
2.32e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.32e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 3599 KLLSAEKAITGYRDPYTGNKISLFQAMKKELVLREHA 3635
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2492-2749 |
2.33e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2492 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ--QRLDKETEGFQKSL-EAERKRQLEASAEAEKLKLRVKELSLAQT 2568
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAAReRLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2569 KAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQS-TREADDLKSAIADleeerkklkkeaeelqrkskemAN 2647
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE-----LDELEAQIRGNgGDRLEQLEREIER----------------------LE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2648 AQQEQIEQQKAELQQsFLTEKGLllkrekEVEGEKKRFEKQLEdemkKAKALKDEQERQRKLMEEERkklqaimDEAVRK 2727
Cdd:COG4913 352 RELEERERRRARLEA-LLAALGL------PLPASAEEFAALRA----EAAALLEALEEELEALEEAL-------AEAEAA 413
|
250 260
....*....|....*....|..
gi 1389908274 2728 QKEAEEEMKNKQREMDVLDKKR 2749
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRK 435
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1985-2785 |
2.39e-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: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1985 RMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlKAKEAENERLKRQaeeeayQRKLLEDQA 2064
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKNR------LKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2065 AQHKqdIEEKITQLQTSsdsELGRQKNIVEETLKQKKV---VEEEIHIIKINFHKASKEK----ADLESELKKLkgiade 2137
Cdd:TIGR00606 263 KIMK--LDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKerelVDCQRELEKL------ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2138 TQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVV 2217
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR------DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2218 LAKEAAQKCTaaeqkaqDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAA 2297
Cdd:TIGR00606 406 EAKTAAQLCA-------DLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2298 KQAKAQNDTEKQRKEAEEEAARRAAAEAaalkQKQQADAEMSKhKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLD 2377
Cdd:TIGR00606 479 ELRKAERELSKAEKNSLTETLKKEVKSL----QNEKADLDRKL-RKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2378 QELQRV------------KGEVNDAF----KQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLaeEA 2441
Cdd:TIGR00606 554 IKSRHSdeltsllgyfpnKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF--DV 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2442 EKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRAL------------------AEKILKEKMQAIQEATKL----K 2497
Cdd:TIGR00606 632 CGSQDEESDLERLKEEIEKSSKQRAMlaGATAVYSQFITqltdenqsccpvcqrvfqTEAELQEFISDLQSKLRLapdkL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2498 AEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQksleaERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKK- 2576
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKv 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2577 ----------FKKQADEVK----AQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKS 2642
Cdd:TIGR00606 787 cltdvtimerFQMELKDVErkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKT 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2643 KEM---------ANAQQEQIEQQKAELQ---QSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLM 2710
Cdd:TIGR00606 867 NELkseklqigtNLQRRQQFEEQLVELStevQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDI 946
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 2711 EEERKKLQAIMDEAVRK-QKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQT 2785
Cdd:TIGR00606 947 KEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT 1022
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1679-2115 |
2.43e-05 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 50.67 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1679 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQ---AEEEKIRQIRVVEEVAQKSAA 1755
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKelaSQQEKRAQEKEALRKEMKKER 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1756 TQLQTKAMSFSEqttkleeslkkeqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAL-RLRLQAEEEAQK 1834
Cdd:pfam15964 399 EELGATMLALSQ--------------NVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCgEMRYQLNQTKMK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1835 KshaqEEAEKQKLEAErdaKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDN 1914
Cdd:pfam15964 465 K----DEAEKEHREYR---TKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1915 E----LQRLKNEVNSTEKQRKQLEDELNKvrsemdSLLQMKINAEKAsmVNTEKSkqLLESEALKMKQLADEAARMrsva 1990
Cdd:pfam15964 538 EkesiQQSFSNEAKAQALQAQQREQELTQ------KMQQMEAQHDKT--VNEQYS--LLTSQNTFIAKLKEECCTL---- 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1991 eeAKKQRQIAEeeaaRQRSEAEKILKEKLAAINEAtrlkteaemalkakeaenERLKRQAEEeayqrklLEDQAAQH--- 2067
Cdd:pfam15964 604 --AKKLEEITQ----KSRSEVEQLSQEKEYLQDRL------------------EKLQKRNEE-------LEEQCVQHgrm 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2068 KQDIEEKITQL----QTSSdSELGRQKNIVEETLKQKKVVEEEIHIIKINFH 2115
Cdd:pfam15964 653 HERMKQRLRQLdkhcQATA-QQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1670-2015 |
2.44e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1749
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1750 AQksaatqlqtkamsfseQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAE 1829
Cdd:COG4372 121 QK----------------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1830 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQR 1909
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1910 GLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV 1989
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*.
gi 1389908274 1990 AEEAKKQRQIAEEEAARQRSEAEKIL 2015
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4308-4336 |
2.59e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.59e-05
10 20
....*....|....*....|....*....
gi 1389908274 4308 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4336
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1599-1896 |
2.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1599 QQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1678
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1679 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1758
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1759 QTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1838
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1839 QEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECI 1896
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2549-2768 |
2.72e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2549 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKH--TTEIVVQKLETQRLQSTREADDLKSAIADlee 2626
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2627 erkklkkeaeelQRKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkrfekQLEDEMKKAKALKDEQERQ 2706
Cdd:COG4942 95 ------------LRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFL--------DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2707 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQ 2768
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2234-2792 |
2.73e-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: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2234 QDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaAKQAKAQNDTEKQRKEA 2313
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE---LKMEKVFQGTDEQLNDL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2314 EEEAARRAAAEAAALKQKQQadaEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVN-DAFK 2392
Cdd:TIGR00606 307 YHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2393 QKSQVEvelarvrIQMEELVKLKlkieeenRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL 2472
Cdd:TIGR00606 384 RGPFSE-------RQIKNFHTLV-------IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2473 AEQRALAEKILKEKMQAIQEATK-LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA 2551
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2552 EAEKLKlrvKELSLAQTKAEDEAKKFK---KQADEVKAQL---------------QRTEKHTTE-------IVVQKLETQ 2606
Cdd:TIGR00606 530 HTTTRT---QMEMLTKDKMDKDEQIRKiksRHSDELTSLLgyfpnkkqledwlhsKSKEINQTRdrlaklnKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2607 RLQSTREADDLK---SAIADLEEERKKLKKEAEELQRKSKEMANA-QQEQIEQQKAELQQSFLTEKGL-------LLKRE 2675
Cdd:TIGR00606 607 KNHINNELESKEeqlSSYEDKLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDenqsccpVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2676 KEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKL-------QAIMDEAVRKQKEAEEEMKNKQREMDVLDKK 2748
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2749 RLEQEKQLAEENKKL--------------REQLQTFEISSKTVSQTKESQTVSVEKLV 2792
Cdd:TIGR00606 767 IEEQETLLGTIMPEEesakvcltdvtimeRFQMELKDVERKIAQQAAKLQGSDLDRTV 824
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1525-1769 |
2.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1525 EDDEKASEKLKEEERRKMAEIQAELDKQKQmaeahakSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQNIQQELQH 1604
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEA-----------LQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1605 LKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAE-LQELRDRAAEAEKLRKAAQDEAERLRKQV 1683
Cdd:COG3883 77 AE----AEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSaLSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1684 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAM 1763
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....*.
gi 1389908274 1764 SFSEQT 1769
Cdd:COG3883 233 AAAAAA 238
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1640-1869 |
2.89e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRDRA-AEAEKLRkaAQDEAERLRKQVAEeTQRKKNAEDE--LKRKSDAEKEAAKQKQRA-- 1714
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADRQR--LEQEKQQQLAAISG-SQSQLESTDQnaLETNGQAQRDAILEESRAvt 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1715 ---------LDDLQKYKMQAEEAERRMKQAEEEKIRQiRVVEEV--AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNV 1783
Cdd:NF012221 1620 kelttlaqgLDALDSQATYAGESGDQWRNPFAGGLLD-RVQEQLddAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1784 LKLQEeadklKKQQKEANTAREEAEQEleiwrQKANEALRlrlqAEEEAQK-KSHAQEEAEKQKLEAERDAKKRG----- 1857
Cdd:NF012221 1699 AQGEQ-----NQANAEQDIDDAKADAE-----KRKDDALA----KQNEAQQaESDANAAANDAQSRGEQDASAAEnkanq 1764
|
250
....*....|...
gi 1389908274 1858 -KAEEAALKQKEN 1869
Cdd:NF012221 1765 aQADAKGAKQDES 1777
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2506-2813 |
3.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2506 QKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVK 2585
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA----LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2586 AQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQqsfl 2665
Cdd:COG3883 93 RALYRSGGSVSYLDV-------LLGSESFSDFLDRLSAL------------------SKIADADADLLEELKADKA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2666 tekglllkrekevegEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVL 2745
Cdd:COG3883 144 ---------------ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2746 DKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGV 2813
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2358-2757 |
3.06e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2358 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIeeenrrlmqKDKDSTQKLL 2437
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI---------KTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2438 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2517
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2518 QEDKQQIQQRLDKETE--GFQKSLEAERKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2595
Cdd:PRK01156 349 DDLNNQILELEGYEMDynSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2596 TEIvvqkleTQRLQSTRE-ADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgllLKR 2674
Cdd:PRK01156 426 SSL------NQRIRALREnLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIRE---------IEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2675 EKEVEGEKKRFEKQLEDEMKKAKAlkDEQERQRKLMEEERKKLQAIMD-EAVRKQKEAE-EEMKNKQREMDV--LDKKRL 2750
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLESEEI--NKSINEYNKIESARADLEDIKIkINELKDKHDKyEEIKNRYKSLKLedLDSKRT 568
|
....*..
gi 1389908274 2751 EQEKQLA 2757
Cdd:PRK01156 569 SWLNALA 575
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2358-2553 |
3.56e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2358 ELTVVKLQlDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRI----QMEELVKLKLKIEEENRRLMQKDKDsT 2433
Cdd:COG2268 170 ELESVAIT-DLEDENNYLDALGRRKIAEIIRDARIAEAEAERE-TEIAIaqanREAEEAELEQEREIETARIAEAEAE-L 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2434 QKLLAE---EAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2510
Cdd:COG2268 247 AKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1389908274 2511 QEtakrlqedKQQIQQRLDKETEGFQKSLEAERKRQLEASAEA 2553
Cdd:COG2268 327 AE--------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2185-2663 |
3.64e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2185 KAAQEEVERLKKKAEdankqkekaekeaekqvVLA--KEAAQKCTAAEQKA---QDVLSKNK--EDVLAQEKLRDEFENA 2257
Cdd:COG4913 238 ERAHEALEDAREQIE-----------------LLEpiRELAERYAAARERLaelEYLRAALRlwFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2258 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAE 2337
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2338 -MSKHKKEAEQALQQKSQVEKELTVvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR----------- 2405
Cdd:COG4913 381 eFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2406 ---------IQMEE------------------------------------------LVKLKLKIEEENRRLMQKDKDS-T 2433
Cdd:COG4913 458 aelpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2434 QKLLAEE----AEKMKSLAEEAGRLSVEAEET-----------------------------ARQRQIAESNlAEQRALAE 2480
Cdd:COG4913 538 GKLDFKPhpfrAWLEAELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekddrrriRSRYVLGFDN-RAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2481 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE------DKQQIQQRLDketegfqkSLEAERKRQLEASAEAE 2554
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA--------ELEAELERLDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2555 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtteivvqkLETQRLQSTREADDLKSAIADLEEERKKLKKE 2634
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ------------AEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580
....*....|....*....|....*....
gi 1389908274 2635 AEELQRKSKEMANAQQEQIEQQKAELQQS 2663
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRA 785
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1605-1754 |
3.88e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1605 LKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVA 1684
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1685 EETQRKKNAEDELKRKSDAEKEAAKQK-------QRALDDLQKY-KMQAEEA-ERRMKQAEE----EKIRQIRVVEEVAQ 1751
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEeeleeliEEQLQELERIsGLTAEEAkEILLEKVEEearhEAAVLIKEIEEEAK 183
|
...
gi 1389908274 1752 KSA 1754
Cdd:PRK12704 184 EEA 186
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
213-321 |
3.88e-05 |
|
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: 46.97 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 279
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908274 280 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 321
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3229-3265 |
3.91e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.91e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 3229 LNFLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEI 3265
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
219-309 |
4.01e-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: 45.75 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 219 KWVNKHLVKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 291
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1389908274 292 DDIADGNPKLTLGLIWTI 309
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1769-1957 |
4.72e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1769 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEaeqeleiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLE 1848
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQ---------QLKEELDKKQIDADKAQQKADFAQDNADKQRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1849 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsAEQECIRLKADFEHAEQQrglldnelqrLKNEVNSTEK 1928
Cdd:pfam05262 250 VRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE--IKKNDEEALKAKDHKAFD----------LKQESKASEK 317
|
170 180
....*....|....*....|....*....
gi 1389908274 1929 QRKQLEDELNKVRSEMDSLLQMKINAEKA 1957
Cdd:pfam05262 318 EAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1871-2025 |
4.72e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1871 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS--EMDSLL 1948
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1949 QmkinaEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 2025
Cdd:COG1579 96 K-----EIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
214-279 |
5.03e-05 |
|
first 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 first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 45.34 E-value: 5.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 214 KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 279
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2687-2769 |
5.35e-05 |
|
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: 48.99 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2687 KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQ 2766
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
...
gi 1389908274 2767 LQT 2769
Cdd:COG4942 110 LRA 112
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
1796-1873 |
5.57e-05 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 47.14 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1796 QQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQ------KKSHAQEEAEKQKLEaERDAKKRGKAEEAALKQKEN 1869
Cdd:pfam06936 62 RQRSSDHSAATVDPDLVVKRQEALEASRLRMQEELDAQaekfkeKQKQLEEEKRRQKIE-MWESMQEGKSYKGNAKLAQE 140
|
....
gi 1389908274 1870 AEKE 1873
Cdd:pfam06936 141 ETEE 144
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1666-1936 |
5.63e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 49.61 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1666 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeeAERRMKQAEEEKIRQIRv 1745
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIP---AERKGEQEGEGEIEAKE- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1746 vEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLR 1825
Cdd:TIGR00927 704 -ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1826 LQAEEEAQKKShaqEEAEKQKLEAERDAKKRGKAEEaalkqkENAEKELDKQRKFAEQIAQQKLSAEQECiRLKADFEHA 1905
Cdd:TIGR00927 783 IQAGEDGEMKG---DEGAEGKVEHEGETEAGEKDEH------EGQSETQADDTEVKDETGEQELNAENQG-EAKQDEKGV 852
|
250 260 270
....*....|....*....|....*....|...
gi 1389908274 1906 EQQRGLL--DNELQRLKNEVNSTEKQRKQLEDE 1936
Cdd:TIGR00927 853 DGGGGSDggDSEEEEEEEEEEEEEEEEEEEEEE 885
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2379-2818 |
5.65e-05 |
|
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: 49.35 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2379 ELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV---KLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLS 2455
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKAsalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2456 VEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEdkqqIQQRLDKETEGF 2535
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNE----------LSELRRQIQRAELELQSTNSELEE----LQERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2536 Q-----------------------KSLEAERKRQLEASAEAEKLK---LRVKELSLAQTKAEDEAKKF----------KK 2579
Cdd:pfam05557 149 SeaeqlrqnlekqqsslaeaeqriKELEFEIQSQEQDSEIVKNSKselARIPELEKELERLREHNKHLnenienklllKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QADEVKAQLQRTEKHTTEIVVQKLETQRLQstREADDLKSAIADLEEERkklkkeaeelqrKSKEMANAQQEQIEQQKAE 2659
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEKLE--QELQSWVKLAQDTGLNL------------RSPEDLSRRIEQLQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2660 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRK--LMEEERKKLQAIMDEAVRKQKEAEE 2733
Cdd:pfam05557 295 LKEensSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRvlLLTKERDGYRAILESYDKELTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2734 EMKNKQREMDVLDkkrLEQEKQLAEENKKLR-EQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKgvlngsTEVDG 2812
Cdd:pfam05557 375 SPQLLERIEEAED---MTQKMQAHNEEMEAQlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK------EEVDS 445
|
....*.
gi 1389908274 2813 VKKEGD 2818
Cdd:pfam05557 446 LRRKLE 451
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1519-1892 |
6.38e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1519 DAQRRLEDDEKASEKLKEEERRKMAEIQAeLDKQKQMAEAHAKSVAKAEQ----------EALELKMKMKEEASKRQDVA 1588
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALRGQLDA-LTKQLQRDESEAQSLRQEEQaltqqwqavcASLNITLQPQDDIQPWLDAQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1589 ADAEKQKQNIQQELQHLKSLSDQEikSKNQQLEDALVSRRkieeeiHIIRIQLEKTTAHKAKSEAELQELRDRAAEAeKL 1668
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAHN--QQIIQYQQQIEQRQ------QQLLTALAGYALTLPQEDEEASWLATRQQEA-QS 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1669 RKAAQDEAERLRKQVAeetqRKKNAEDELKRKSDAEKEAAKQkqrALDDLQKYKMQ--AEEAERRMKQAEEEKIRQiRVV 1746
Cdd:PRK10246 677 WQQRQNELTALQNRIQ----QLTPLLETLPQSDDLPHSEETV---ALDNWRQVHEQclSLHSQLQTLQQQDVLEAQ-RLQ 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1747 EEVAQKSAATQlqtkAMSFSEQTTKLEESLKKEqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1826
Cdd:PRK10246 749 KAQAQFDTALQ----ASVFDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTV 822
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 1827 QAEEeaqkkSHAQEEAEKQKLeaeRDAKKRGKAEEAALKQKENAEKEldkQRKFAEQIAQQKLSAE 1892
Cdd:PRK10246 823 TVEQ-----IQQELAQLAQQL---RENTTRQGEIRQQLKQDADNRQQ---QQALMQQIAQATQQVE 877
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2473-2747 |
6.43e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2473 AEQRALAEKILKEKMQAIQEATklkaeaekLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAE 2552
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQN--------LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVDLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2553 AEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI----VVQKLETQRLQSTREADDLKSaiadlee 2626
Cdd:COG3206 212 EEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspVIQQLRAQLAELEAELAELSA------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2627 erkklkkeaeELQRKSKEMANAQQE------QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkkAKALK 2700
Cdd:COG3206 285 ----------RYTPNHPDVIALRAQiaalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL------AELPE 348
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908274 2701 DEQERQRklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2747
Cdd:COG3206 349 LEAELRR--LEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2454-2592 |
6.77e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.51 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2454 LSVEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE-DKQQI--QQRLDk 2530
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlYKKGAvsQQELD- 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2531 etegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-AEDEAKKFKKQADEVKAQLQRTE 2592
Cdd:COG1566 152 -----EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAaAQAQVAQAEAALAQAELNLARTT 209
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1825-2100 |
6.90e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1825 RLQAEEEAQKKshAQEEAEKQKLEAERDAKKRGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEh 1904
Cdd:TIGR02794 54 RIQQQKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1905 AEQQRGLLDNELQRLKnevnstEKQRKQLEDElnkvrsemdsllqmkinaekasmvntekskqllesealkmkQLADEAA 1984
Cdd:TIGR02794 130 AEAKAKAEAEAERKAK------EEAAKQAEEE-----------------------------------------AKAKAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1985 RMRSVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 2064
Cdd:TIGR02794 163 EAKKKAEEAKKK---AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1389908274 2065 AQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK 2100
Cdd:TIGR02794 240 LASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2549-2822 |
7.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2549 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQSTREADDLKSAIADLeeer 2628
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-----LEALQAEIDKLQAEIAEAEAEIEER---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2629 kklkkeaeelQRKSKEMANAQQEQIEQQK-------AELQQSFLTEKGLLlkrekevegekKRFEKQLEDEMKKAKALKD 2701
Cdd:COG3883 85 ----------REELGERARALYRSGGSVSyldvllgSESFSDFLDRLSAL-----------SKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2702 EQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTK 2781
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1389908274 2782 ESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGVKKEGDSPLS 2822
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2056-2254 |
7.10e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2056 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLK---QKKVVEEEIHIIKINfHKASKEKADLESELKKLK 2132
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALK-QKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2133 GIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEkvkritaAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEA 2212
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK-------KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908274 2213 EKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEF 2254
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1625-1842 |
7.41e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.79 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1625 VSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE--------LRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDE 1696
Cdd:pfam15709 350 VERKRREQEEQRRLQQEQLERAEKMREELELEQqrrfeeirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ--QEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1697 LKRKsdaekeaakqkqraLDDLQKyKMQAEEAERrmkqAEEEKIRQirvveevaqksaatqlqtkamsfseqtTKLEESL 1776
Cdd:pfam15709 428 FRRK--------------LQELQR-KKQQEEAER----AEAEKQRQ---------------------------KELEMQL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 1777 KKEQGNVLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLrlqAEEEAQKKshAQEEA 1842
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQKQ--EAEEKARLEAEERRQKEEEAARL---ALEEAMKQ--AQEQA 520
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2686-2835 |
7.47e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2686 EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ--------KEAEEEMKNKQREMDVLDKKRLEQ--EKQ 2755
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2756 LAEENKKLREQLQTFEisSKTVSQTKESQTVSVEKLVAVTTVGtSKGvlngstEVDGVKKEGDSPLSFEGIREKVPAERL 2835
Cdd:PRK00409 609 LIEARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLG-QKG------EVLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1749-1893 |
7.68e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1749 VAQKSAATQL---QTKAMSFSEQTTKLEESLKKEQgnVLKLQEEADKLkkqqkeantaREEAEQELEIWRQKANEALRlR 1825
Cdd:PRK12704 24 VRKKIAEAKIkeaEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKL----------RNEFEKELRERRNELQKLEK-R 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1826 LQAEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQ 1893
Cdd:PRK12704 91 LLQKEENLDRK--LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1521-2202 |
7.79e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1521 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMKEeASKRQDVAADAEKQKQNIQQ 1600
Cdd:PRK04863 351 ERYQADLEELEERLEEQN-----EVVEEADEQQEENEARAEA---AEEEVDELKSQLAD-YQQALDVQQTRAIQYQQAVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1601 ELQHLKSLSD-------------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK------------------------ 1643
Cdd:PRK04863 422 ALERAKQLCGlpdltadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarel 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1644 -TTAHKAKSEAE-LQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaEKEAAKQKQRaLDDLQKY 1721
Cdd:PRK04863 502 lRRLREQRHLAEqLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDEL------EQLQEELEAR-LESLSES 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1722 KmqAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1801
Cdd:PRK04863 574 V--SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQS---GEEFEDSQDVTEYMQQLLERERELTVERD 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1802 TAREEAEQ-ELEIWR---QKANEALRLRLQAE----------------EEAQKKS-------HA----QEEAEKQKLEAE 1850
Cdd:PRK04863 649 ELAARKQAlDEEIERlsqPGGSEDPRLNALAErfggvllseiyddvslEDAPYFSalygparHAivvpDLSDAAEQLAGL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1851 RD---------------AKKRGKAEE--AALKQKENA-------------------EKELDKQRKFAEQIAQQ--KLSAE 1892
Cdd:PRK04863 729 EDcpedlyliegdpdsfDDSVFSVEEleKAVVVKIADrqwrysrfpevplfgraarEKRIEQLRAEREELAERyaTLSFD 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1893 -QECIRLKADFEH--------------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSL- 1947
Cdd:PRK04863 809 vQKLQRLHQAFSRfigshlavafeadpeaelrqLNRRRVELERALADHESQEQQQRSQLEQAKeglSALNRLLPRLNLLa 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1948 ---LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILkekLAAIN 2023
Cdd:PRK04863 889 detLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQfEQLKQDYQQAQQTQRDAKQQAFA---LTEVV 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2024 E-ATRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKiTQLQTSSDSELGRQKNIVEEtlkqkk 2101
Cdd:PRK04863 966 QrRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQE------ 1038
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2102 vveeeihiikinfhkaskekadLESELKKLKGIADETQKSKLKAEEEaeKLKKLAAEEERRRKEAEEKVKRITAAEEEAA 2181
Cdd:PRK04863 1039 ----------------------LKQELQDLGVPADSGAEERARARRD--ELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
810 820
....*....|....*....|.
gi 1389908274 2182 RQCKAAQEEVERLKKKAEDAN 2202
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAK 1115
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1897-2151 |
8.11e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 8.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1897 RLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKM 1976
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1977 KQLADEAARMRsvAEEAKKQRQIAEEEAARQRS----EAEKILKEKLAAINE-ATRLKTEAEMALKAKEAENE--RLKRQ 2049
Cdd:COG1340 98 RKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEKeLEKAKKALEKNEKLKELRAElkELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2050 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEetlKQKKVVEEEIHIIKInfhkaSKEKADLESELK 2129
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIEL-----QKELRELRKELK 247
|
250 260
....*....|....*....|..
gi 1389908274 2130 KLKGIADETQKSKLKAEEEAEK 2151
Cdd:COG1340 248 KLRKKQRALKREKEKEELEEKA 269
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1670-2155 |
8.28e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQVAEETQRKKNAEDELKRKS----------DAEKEAAKQKQRALDDLQKYKMQAEEAERRmKQAEEEK 1739
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSieynnamddyNNLKSALNELSSLEDMKNRYESEIKTAESD-LSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1740 IRQIRVVEE---------------------------VAQKSAATQLQTKAMSFSEQTTKLEEsLKKEQGNVLKLQEEADK 1792
Cdd:PRK01156 272 NNYYKELEErhmkiindpvyknrnyindyfkykndiENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1793 LKKQQKEA-------NTAREEAEQeLEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1865
Cdd:PRK01156 351 LNNQILELegyemdyNSYLKSIES-LKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1866 QKENAEKE-LDKQRKFAEQiaqqkLSAEQECIRLKADF--EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS 1942
Cdd:PRK01156 430 QRIRALREnLDELSRNMEM-----LNGQSVCPVCGTTLgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1943 EMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE------------------AKKQRQIAEEEA 2004
Cdd:PRK01156 505 RKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledldskrtswlnALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2005 ARQRSEaekilkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY----QRKLLEDQAAQhKQDIEEKITQLQT 2080
Cdd:PRK01156 585 NRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEKLRGKIDNYKK 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2081 SSDSELGRQKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 2155
Cdd:PRK01156 658 QIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1792-2154 |
8.62e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1792 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1871
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1872 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLEDELNKVRSEM 1944
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEaqiaelqSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1945 DSLLQMKINAEKASMVNtekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 2024
Cdd:COG4372 167 AALEQELQALSEAEAEQ-------------ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2025 ATRLKTEAEMALKAKEAENERLK-RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVV 2103
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVIlKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 2104 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 2154
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1657-2483 |
8.76e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1657 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD------AEKEAAKQKQRALDDLQKYKMQAEEAER 1730
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhlnlvqTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1731 RMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNVL---KLQEEADKLKK 1795
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPDLtadNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1796 QQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAERDAKKRGKAEEaaLK 1865
Cdd:PRK04863 450 KEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSE--LE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1866 QKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMD 1945
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1946 SLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 2025
Cdd:PRK04863 604 AWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQALDEEIERLSQPGGSED 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2026 TRLKTEAEmalkakeaeneRLKRQAEEEAYQRKLLEDQA--------AQHK---QDIEEKITQLQT-------------- 2080
Cdd:PRK04863 673 PRLNALAE-----------RFGGVLLSEIYDDVSLEDAPyfsalygpARHAivvPDLSDAAEQLAGledcpedlyliegd 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2081 -------SSDSELGRQKNIVEETLKQ---KKVVEEEIhiikinFHKASKEK--ADLESElkklkgiADETQKSKLKAEEE 2148
Cdd:PRK04863 742 pdsfddsVFSVEELEKAVVVKIADRQwrySRFPEVPL------FGRAAREKriEQLRAE-------REELAERYATLSFD 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2149 AEKLKKLAAEEERRRKEAEEKVkrITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2228
Cdd:PRK04863 809 VQKLQRLHQAFSRFIGSHLAVA--FEADPEAELRQLNRRRVELERALADHESQEQQQRSQ----------LEQAKEGLSA 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2229 AEQKAQDVlsknkeDVLAQEKLRDEF----------ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaak 2298
Cdd:PRK04863 877 LNRLLPRL------NLLADETLADRVeeireqldeaEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQ----- 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2299 QAKAQNDTEKQRK---------------EAEEEAARRAAAEAAALKQKQ-QADAEMSKHKKEAEQALQQKSQVEKELTvv 2362
Cdd:PRK04863 946 QAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQRLeQAEQERTRAREQLRQAQAQLAQYNQVLA-- 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2363 KLQLDETDKQKVL--LDQELQRV-----KGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEE----NRRLMQKDKD 2431
Cdd:PRK04863 1024 SLKSSYDAKRQMLqeLKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEmdnlTKKLRKLERD 1103
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2432 STQ-KLLAEEAEKMKSLAEEAGRLSvEAEETARQRQIAESNLAEQRALAEKIL 2483
Cdd:PRK04863 1104 YHEmREQVVNAKAGWCAVLRLVKDN-GVERRLHRRELAYLSADELRSMSDKAL 1155
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1865-2249 |
9.46e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 48.80 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1865 KQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSem 1944
Cdd:COG5185 142 KLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1945 dslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEaarmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 2024
Cdd:COG5185 220 ---TLLEKAKEIINIEEALKGFQDPESELEDLAQTSDK-------LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2025 ATRlKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQtssdSELGRQKNIVEEtlKQKKVVE 2104
Cdd:COG5185 290 QFE-NTKEKIAEYTKSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLT----AEIEQGQESLTE--NLEAIKE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2105 EEIHIIKINFHKASKEKAD-LESELKKLKGIADETQKSKLKAEEE-AEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR 2182
Cdd:COG5185 362 EIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2183 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAK--EAAQKCTAAEQKAQDVLSKNKEDVLAQEK 2249
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKkeDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2292-2526 |
9.61e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2292 AENEAAKQAKAQNDTEKQRKeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2371
Cdd:COG3883 14 ADPQIQAKQKELSELQAELE--------------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2372 QkvlLDQELQRVKGEVNDAFKQKSQVEVE------------LARVriqmeELVKlklKIEEENRRLMQKDKDSTQKLlae 2439
Cdd:COG3883 80 E---IEERREELGERARALYRSGGSVSYLdvllgsesfsdfLDRL-----SALS---KIADADADLLEELKADKAEL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2440 eAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE 2519
Cdd:COG3883 146 -EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*..
gi 1389908274 2520 DKQQIQQ 2526
Cdd:COG3883 225 AAAAAAA 231
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4448-4481 |
9.64e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.64e-05
10 20 30
....*....|....*....|....*....|....
gi 1389908274 4448 EETGPIAGILDTDTLEKVSVTEAIHRNLVDNITG 4481
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1706-2066 |
9.65e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.49 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1706 EAAKQKQRALDDLQK----YKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKEQG 1781
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeYKKQSEAAEAAKAQVLEELESTKRLIEE-----------------------LKLNLERAQT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1782 NVLKLQEEAD--KLKKQQKEANTAREE---AEQELEIWRQKANEALrlrlqAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1856
Cdd:pfam05701 92 EEAQAKQDSElaKLRVEEMEQGIADEAsvaAKAQLEVAKARHAAAV-----AELKSVKEELESLRKEYASLVSERDIAIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1857 gKAEEAALKQKE------------NAEKELDKQRKFAEQIAQQK-----LSAEQECIRLKADFEHAEQqrglldnELQRL 1919
Cdd:pfam05701 167 -RAEEAVSASKEiektveeltielIATKESLESAHAAHLEAEEHrigaaLAREQDKLNWEKELKQAEE-------ELQRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1920 KNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKINAEKASMVNTEKS-----------KQLLESEALKMKQLADEAAR 1985
Cdd:pfam05701 239 NQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTstsiqaalasaKKELEEVKANIEKAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1986 MRSVAE--EAKKQRQIAEEEAARQRSEAEKILKEKLAAinEATRLKTEAEMA-LKAKEAENERLK-----RQAEEEAYQR 2057
Cdd:pfam05701 319 LRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVqAKEKEAREKMVElpkqlQQAAQEAEEA 396
|
....*....
gi 1389908274 2058 KLLEdQAAQ 2066
Cdd:pfam05701 397 KSLA-QAAR 404
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2457-2768 |
1.03e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2457 EAEETARQRqiaesnlaEQRALAEKI-LKEKMQAIQEATKLKAEAEKLQKQKDQ-AQETAKRLQEDKQQIQQRLDKETEG 2534
Cdd:pfam02029 3 DEEEAARER--------RRRAREERRrQKEEEEPSGQVTESVEPNEHNSYEEDSeLKPSGQGGLDEEEAFLDRTAKREER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2535 FQKSLE--AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2612
Cdd:pfam02029 75 RQKRLQeaLERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2613 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--IEQQK-----AELQQSFLTEKGLLLKREKEVEGEKKRF 2685
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvFLDQKrghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2686 EKQLEDEMKKAKALKDEQERQR--KLMEEERKKLQaimdeavRKQKEAE---EEMKNKQ------REMDVLDKKRLEQEK 2754
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRRrqEKESEEFEKLR-------QKQQEAElelEELKKKReerrklLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1389908274 2755 QLA--EENKKLREQLQ 2768
Cdd:pfam02029 308 KLReeEEKRRMKEEIE 323
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1620-2031 |
1.06e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 48.75 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1620 LEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRA-AEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELK 1698
Cdd:pfam15964 312 LMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKAlIQCEQLKSELERQKERLEKELASQQEKRAQEKEALR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1699 RKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQIRVVEEvaqksAATQLQTKAMSFSEQTTKLEESLKK 1778
Cdd:pfam15964 392 KEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLVSQLEE-----AQKQLASQEMDVTKVCGEMRYQLNQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1779 EQgnvLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1858
Cdd:pfam15964 461 TK---MKKDEAEKEHREYRTKTGRQLEIKDQEIE----------KLGLELSESKQRLEQAQQDAARAREECLKLTELLGE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1859 AEEAALKQKEnaEKElDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQ------ 1932
Cdd:pfam15964 528 SEHQLHLTRL--EKE-SIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctla 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 --LEDELNKVRSEMDSLLQ----MKINAEKASMVNTEKSKQLLESEalKMKQladeaaRMRSVAEEAKKQRQIAEEEAAR 2006
Cdd:pfam15964 605 kkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCVQHG--RMHE------RMKQRLRQLDKHCQATAQQLVQ 676
|
410 420
....*....|....*....|....*
gi 1389908274 2007 QRSEAEKILKEKLAAINEATRLKTE 2031
Cdd:pfam15964 677 LLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2132-2352 |
1.07e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.92 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2132 KGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA--EEEAARQCKAAQEEVERLKKKAEdankqkekae 2209
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQA---------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2210 keaekqvvlaKEAAQKCTA-AEQKAQDVLSKNKEdvlaQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQ 2288
Cdd:TIGR02794 130 ----------AEAKAKAEAeAERKAKEEAAKQAE----EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2289 KKA------AENEAAKQA----KAQNDTEKQRKEAEEEAARRAAAEAAALKQKQ------QADAEMSKHKKEAEQALQQK 2352
Cdd:TIGR02794 196 AKAeaakakAAAEAAAKAeaeaAAAAAAEAERKADEAELGDIFGLASGSNAEKQggargaAAGSEVDKYAAIIQQAIQQN 275
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2328-2609 |
1.11e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEMSKHKKEaeqalqqksqVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2407
Cdd:pfam15905 61 LKKKSQKNLKESKDQKE----------LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2408 MEELVK----LKLKIEEE-NRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI 2482
Cdd:pfam15905 131 LLELTRvnelLKAKFSEDgTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2483 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRlDKETEGFQKSLEAerkRQLEASAEAEKLKLRVKE 2562
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEK-NDEIESLKQSLEE---KEQELSKQIKDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908274 2563 LslaQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQ 2609
Cdd:pfam15905 287 L---ESEKEELLREYEEKEQTLNAELEELKE---KLTLEEQEHQKLQ 327
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
213-320 |
1.18e-04 |
|
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: 45.39 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 279
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908274 280 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 320
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1805-2155 |
1.22e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1805 EEAEQELeiwRQKANEAlRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK----RGKAEEAALKQKEnAEKELDKQRKF 1880
Cdd:pfam02029 5 EEAARER---RRRAREE-RRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqGGLDEEEAFLDRT-AKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1881 AEQIAQQKlsaeqecirlkadfehaeqqrgLLDNELQRLKNEVNStEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV 1960
Cdd:pfam02029 80 QEALERQK----------------------EFDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1961 NTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA------EM 2034
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEN-FAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVksqngeEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2035 ALKAKEAENERLK-----RQAEEEAYQR----KLLEDQAAQHkQDIE----EKITQLQTSSDSELGRQKNIVEEtlkQKK 2101
Cdd:pfam02029 216 VTKLKVTTKRRQGglsqsQEREEEAEVFleaeQKLEELRRRR-QEKEseefEKLRQKQQEAELELEELKKKREE---RRK 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2102 VVEEEihiikinfhkasKEKADLESELKKLKGiadETQKSKLKAE------EEAEKLKKL 2155
Cdd:pfam02029 292 LLEEE------------EQRRKQEEAERKLRE---EEEKRRMKEEierrraEAAEKRQKL 336
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1773-1943 |
1.23e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.41 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQA-------EEEAQKKSHAQEEAEKQ 1845
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRleeerqrQEEEERKQRLQLQAAQE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1846 KLEAERDAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIaqqKLSAEQecirlKADFEHAEQQRglldNELQRLKNEvn 1924
Cdd:pfam15709 420 RARQQQEEFRRKLQELQRKKQQEEAERaEAEKQRQKELEM---QLAEEQ-----KRLMEMAEEER----LEYQRQKQE-- 485
|
170
....*....|....*....
gi 1389908274 1925 stEKQRKQLEDELNKVRSE 1943
Cdd:pfam15709 486 --AEEKARLEAEERRQKEE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1969-2196 |
1.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1969 LESEALKMKQLADEAARMRSVAEEAKKQRQIAEE-EAARQRSEAEKILKEKLAAINEATRLKTeAEMALKAKEAENERLK 2047
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2048 RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSdselGRQKNIVEETLKQKKvveeeihiikinfhkasKEKADLESE 2127
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNG----GDRLEQLEREIERLE-----------------RELEERERR 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2128 LKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2196
Cdd:COG4913 361 RARL---EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1527-1708 |
1.42e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 48.08 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1527 DEKASEKLKEEErrkmaeiQAELDKQKQMAEAHAKSvakaEQEALELKMKMKEEASKRQDVAAD-----------AEKQK 1595
Cdd:pfam05262 179 DKKVVEALREDN-------EKGVNFRRDMTDLKERE----SQEDAKRAQQLKEELDKKQIDADKaqqkadfaqdnADKQR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1596 QNIQQELQHLKSLSD----QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAkseaelQELRDRAAEAEKLRKA 1671
Cdd:pfam05262 248 DEVRQKQQEAKNLPKpadtSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKA------FDLKQESKASEKEAED 321
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908274 1672 AQDEAERLRKQVAEETQRKKNaedELKRKSDAEKEAA 1708
Cdd:pfam05262 322 KELEAQKKREPVAEDLQKTKP---QVEAQPTSLNEDA 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2466-2607 |
1.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2466 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------------KETE 2533
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2534 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQrTEKHTTEIVVQKLETQR 2607
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEELEAER 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1403-1629 |
1.54e-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: 47.45 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1403 LTEARQRQEKIQAVPISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKK 1482
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1483 PKMECAsDDIIQEYVNlrTRYSELMTLTNQyiKFIIDAQRRLEDDEKASEKLKEEeRRKMAEIQAELDKQKQMAEAHAKS 1562
Cdd:COG4942 102 QKEELA-ELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQ-AEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1563 VAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSlSDQEIKSKNQQLEDALVSRRK 1629
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAE 241
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1670-2088 |
1.64e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.26 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQVA-----EETQRKKnAEDELKRKSDAEKEAAKQKQRA---------LDDLQKYKMQAEEAERRMKQA 1735
Cdd:PRK10246 194 KSARTELEKLQAQASgvallTPEQVQS-LTASLQVLTDEEKQLLTAQQQQqqslnwltrLDELQQEASRRQQALQQALAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1736 EEEKIRQIRVVEeVAQksAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR 1815
Cdd:PRK10246 273 EEKAQPQLAALS-LAQ--PARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1816 QKANEALRLRLQAEEEA--------QKKSHAQEE-------AEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-- 1878
Cdd:PRK10246 350 TWLAEHDRFRQWNNELAgwraqfsqQTSDREQLRqwqqqltHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRlv 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1879 ----------KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNeVNSTEKQRKQLEDELNKVRSEMDSLL 1948
Cdd:PRK10246 430 alhgqivpqqKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRAQLQAGQPCPL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1949 -----QMKINAEKASMVNTEKSKQL-LESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAI 2022
Cdd:PRK10246 509 cgstsHPAVEAYQALEPGVNQSRLDaLEKE---VKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE-EQALTQQWQAV 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2023 NEATRLKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDI---EEKITQLQTSSDSELGR 2088
Cdd:PRK10246 585 CASLNITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQGQIAAHNQQIiqyQQQIEQRQQQLLTALAG 652
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1394-1837 |
1.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1394 DSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTDEKKLLG------EIEKNKDKIDDCHKNAKAYIDSVKDYEFQIL 1467
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPlyqeleALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1468 TYKALQDPIASPLKKpKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRkmAEIQA 1547
Cdd:COG4717 167 ELEAELAELQEELEE-LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1548 ELDKQKQMAEAHAksvakaeqEALELKMKMKEEASKRQDVAADAekqkQNIQQELQHLKSLSDQEIKSKNQQLEDALVSR 1627
Cdd:COG4717 244 RLKEARLLLLIAA--------ALLALLGLGGSLLSLILTIAGVL----FLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1628 RKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaedeLKRKSDAEKEA 1707
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-----LAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1708 AKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQ 1787
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-AELEQL 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1788 EEADKLKKQQKEANTAREEAEQELEIWRqkaneALRLRLQAEEEAQKKSH 1837
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYR 510
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2686-2768 |
1.67e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 46.80 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2686 EKQLEDEMKKAKALkdeqERQRKLMEEERKKLQAIMDEAVRKQKEA--------EEEMKNKQREMD-VLDKKRLEQEKQL 2756
Cdd:cd16269 197 EKEIEAERAKAEAA----EQERKLLEEQQRELEQKLEDQERSYEEHlrqlkekmEEERENLLKEQErALESKLKEQEALL 272
|
90
....*....|..
gi 1389908274 2757 AEENKKLREQLQ 2768
Cdd:cd16269 273 EEGFKEQAELLQ 284
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1565-2069 |
1.88e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1565 KAEQEALElkmKMKEEASkrqDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKT 1644
Cdd:PRK10246 194 KSARTELE---KLQAQAS---GVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1645 TAHKAKSEAELQELRDRAAE-AEKLRKAaqdeAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDdlQKYKM 1723
Cdd:PRK10246 268 QALAAEEKAQPQLAALSLAQpARQLRPH----WERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAK--QSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1724 QAEEAERRMKQAEEEKIRQIRvvEEVA--------QKSAATQLQTKAMSFSEQTTKL-------------EESLKKEQGN 1782
Cdd:PRK10246 342 QAQQQSLNTWLAEHDRFRQWN--NELAgwraqfsqQTSDREQLRQWQQQLTHAEQKLnalpaitltltadEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1783 --------VLKLQEEADKLKKQQKEANTAREEAEQELeiwrQKANEALRLRLQ-----AEEEAQKKSHAQEEAEKQKLEA 1849
Cdd:PRK10246 420 eqrplrqrLVALHGQIVPQQKRLAQLQVAIQNVTQEQ----TQRNAALNEMRQrykekTQQLADVKTICEQEARIKDLEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ERDAKKRGK-------AEEAALKQKENAEKELDKQRKfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1922
Cdd:PRK10246 496 QRAQLQAGQpcplcgsTSHPAVEAYQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VNSTEKQRKQLEDELNKVRSEMDSL----------------------LQMKINAEKASMVN----TEKSKQLLESE---- 1972
Cdd:PRK10246 574 EQALTQQWQAVCASLNITLQPQDDIqpwldaqeeherqlrllsqrheLQGQIAAHNQQIIQyqqqIEQRQQQLLTAlagy 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1973 ALKMKQLADEAARMRSVAEEAKK-QRQIAEEEAARQRSEAEKILKEKLAAINEATrlkTEAEMAL--KAKEAENERLKRQ 2049
Cdd:PRK10246 654 ALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTPLLETLPQSDDLP---HSEETVAldNWRQVHEQCLSLH 730
|
570 580
....*....|....*....|.
gi 1389908274 2050 AEEEAYQRKL-LEDQAAQHKQ 2069
Cdd:PRK10246 731 SQLQTLQQQDvLEAQRLQKAQ 751
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1578-1809 |
1.95e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 47.15 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1578 KEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1657
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL--EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1658 lrdrAAEAEKLRKAaqdEAERLRKQvAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqAEEAERRmKQAEE 1737
Cdd:TIGR02794 127 ----KQAAEAKAKA---EAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEAK-AKAEE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 1738 EKIRQirvveEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE-EADKLKKQQKEANTAREEAEQ 1809
Cdd:TIGR02794 194 AKAKA-----EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGlASGSNAEKQGGARGAAAGSEV 261
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1785-1892 |
1.95e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 44.78 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1785 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKSHAQEEAEKQKLEAERDAKKRgKAEEAAL 1864
Cdd:COG0711 35 KIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII-------AEARKEAEAIAEEAKAEAEAEAERIIA-QAEAEIE 106
|
90 100 110
....*....|....*....|....*....|...
gi 1389908274 1865 KQKENAEKELDKQ-----RKFAEQIAQQKLSAE 1892
Cdd:COG0711 107 QERAKALAELRAEvadlaVAIAEKILGKELDAA 139
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3895-3928 |
2.00e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.00e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908274 3895 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3928
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2453-2767 |
2.02e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2453 RLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKEt 2532
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2533 egfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2612
Cdd:COG4372 93 ---QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2613 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDE 2692
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2693 MKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2767
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2329-2579 |
2.02e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQK---SQVEVELARVR 2405
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2406 IQMEELVklkLKIEEEnRRLMQKDKDSTQKLlaEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKE 2485
Cdd:COG1340 123 WRQQTEV---LSPEEE-KELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2486 KMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASaeaeklklRVKELSL 2565
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLRKKQRALK--------REKEKEE 264
|
250
....*....|....
gi 1389908274 2566 AQTKAEDEAKKFKK 2579
Cdd:COG1340 265 LEEKAEEIFEKLKK 278
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2132-2356 |
2.02e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2132 KGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERL-----KKKAEDANKQKE 2206
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQ-----------------------QKQAAEQERLKQLEKERLaaqeqKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2207 KAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEdvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEaallRQKAEEAE 2286
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEAKKKAEAEAAA----KAAAEAKK 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2287 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAaeaaalkqkqqADAEMSKHKKEAEQALQQKSQVE 2356
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA-----------AEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2344-2662 |
2.05e-04 |
|
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: 48.02 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2344 EAEQALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAfkqkSQVEVELARVRIQMEELVKLKlkieEENR 2423
Cdd:COG3096 358 ELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADY----QQALDVQQTRAIQYQQAVQAL----EKAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2424 RLMQKDkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKE--KMQAIQEATKLKAEAE 2501
Cdd:COG3096 427 ALCGLP-DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEveRSQAWQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2502 KLQKQKDQAQETAKRLQEDKQQI--QQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2579
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QADEVKAQLQRTEK-----HTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKeaeelqrkSKEMANAQQEQIE 2654
Cdd:COG3096 586 QLEQLRARIKELAArapawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATV--------ERDELAARKQALE 657
|
....*...
gi 1389908274 2655 QQKAELQQ 2662
Cdd:COG3096 658 SQIERLSQ 665
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1521-2118 |
2.05e-04 |
|
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: 48.02 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1521 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMK--EEASKRQDVAADAEKQKQNI 1598
Cdd:COG3096 350 ERYQEDLEELTERLEEQE-----EVVEEAAEQLAEAEARLEA---AEEEVDSLKSQLAdyQQALDVQQTRAIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1599 QQELQHLKSLSD----------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK--------------TTAHKAKSE-- 1652
Cdd:COG3096 422 LEKARALCGLPDltpenaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageverSQAWQTAREll 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 ----------AELQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksDAEKEAAKQKQRALDDLQkyk 1722
Cdd:COG3096 502 rryrsqqalaQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEEL----EELLAELEAQLEELEEQA--- 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1723 mqAEEAERRMK-QAEEEKIRQiRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1801
Cdd:COG3096 574 --AEAVEQRSElRQQLEQLRA-RIKELAARAPAWLAAQDALERLREQS---GEALADSQEVTAAMQQLLEREREATVERD 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1802 TAREEAEQ-ELEIWRQKA---NEALRLRLQAE----------------EEAQKKS-------HA----QEEAEKQKLEA- 1849
Cdd:COG3096 648 ELAARKQAlESQIERLSQpggAEDPRLLALAErlggvllseiyddvtlEDAPYFSalygparHAivvpDLSAVKEQLAGl 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1850 ----------ERD----------AKKRGKAEEAALKQKE---------------NAEKELDKQRKFAEQIAQQ--KLSAE 1892
Cdd:COG3096 728 edcpedlyliEGDpdsfddsvfdAEELEDAVVVKLSDRQwrysrfpevplfgraAREKRLEELRAERDELAEQyaKASFD 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1893 -QECIRLKADFEH--------------------AEQQRglldNELQRLKNEVNSTEKQRKQ------------------- 1932
Cdd:COG3096 808 vQKLQRLHQAFSQfvgghlavafapdpeaelaaLRQRR----SELERELAQHRAQEQQLRQqldqlkeqlqllnkllpqa 883
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1933 -------LEDELNKVRSEMDSLLQ----MKINAEKASMVntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ----- 1996
Cdd:COG3096 884 nlladetLADRLEELREELDAAQEaqafIQQHGKALAQL--EPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQifals 961
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1997 ---------------RQIAE------------EEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK-----EAENE 2044
Cdd:COG3096 962 evvqrrphfsyedavGLLGEnsdlneklrarlEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKqqtlqELEQE 1041
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2045 --RLKRQAEEEAyqrkllEDQAAQHKQDIEEKITQLQ---TSSDSELGRQKNIVEETLKQKKVVEEEIHIIK--INFHKA 2117
Cdd:COG3096 1042 leELGVQADAEA------EERARIRRDELHEELSQNRsrrSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEReqVVQAKA 1115
|
.
gi 1389908274 2118 S 2118
Cdd:COG3096 1116 G 1116
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2344-2617 |
2.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2344 EAEQALQQKSQVEKEltvVKLQLDETDKQKVLLDQELQRVKGEVND-------------AFKQKSQVeVELARVRIQMEE 2410
Cdd:PRK04863 359 ELEERLEEQNEVVEE---ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtraiQYQQAVQA-LERAKQLCGLPD 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2411 LV--KLKLKIEEenrrLMQKDKDSTQKLLAEE-----AEKMKSLAEEAGRL------SVEAEETARQRQIAESNLAEQRA 2477
Cdd:PRK04863 435 LTadNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2478 LAEKI--LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEK 2555
Cdd:PRK04863 511 LAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2556 LKLRVKEL------------SLAQTKAEDEAKKFKKQA-DEVKAQLQRTEKHTTEiVVQKLETQRLQSTREADDL 2617
Cdd:PRK04863 591 LQARIQRLaarapawlaaqdALARLREQSGEEFEDSQDvTEYMQQLLERERELTV-ERDELAARKQALDEEIERL 664
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3194-3229 |
2.14e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.54 E-value: 2.14e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1389908274 3194 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETAL 3229
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1677-1862 |
2.16e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.30 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1677 ERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEvAQKSAAT 1756
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERES---QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-KQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1757 QLQTKAMSFSEQTTKLEESLKKEqgnVLKLQEEAdklkkqQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS 1836
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKRE---IEKAQIEI------KKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|....*.
gi 1389908274 1837 HAQEEaEKQKLEAERDAKKRGKAEEA 1862
Cdd:pfam05262 331 EPVAE-DLQKTKPQVEAQPTSLNEDA 355
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1973-2202 |
2.23e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1973 ALKMKQLADEAARMRSvaeEAKKQRQIAEEEA--ARQRSEAEKILKEKLAAINEA-TRLK-----------TEAEMALKA 2038
Cdd:PRK05035 440 AIEQEKKKAEEAKARF---EARQARLEREKAAreARHKKAAEARAAKDKDAVAAAlARVKakkaaatqpivIKAGARPDN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2039 KEAENERLKRQAEEEAYQRKLLEDQAAQHKQD-IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhKA 2117
Cdd:PRK05035 517 SAVIAAREARKAQARARQAEKQAAAAADPKKAaVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK--KA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2118 SKEKADLESELKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2197
Cdd:PRK05035 595 AQQAASAEPEEQVA---EVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEE 671
|
....*
gi 1389908274 2198 AEDAN 2202
Cdd:PRK05035 672 AEDPK 676
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2905-2938 |
2.29e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.29e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908274 2905 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPE 2938
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1968-2202 |
2.38e-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: 47.07 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1968 LLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 2047
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2048 RQAEEeayqrklLEDQAAQHKQDIEEKITQLQTSSDSE----LGRQKNIVE-----ETLKQ-KKVVEEEIHIIKINFHKA 2117
Cdd:COG4942 90 KEIAE-------LRAELEAQKEELAELLRALYRLGRQPplalLLSPEDFLDavrrlQYLKYlAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2118 SKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2197
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*
gi 1389908274 2198 AEDAN 2202
Cdd:COG4942 243 TPAAG 247
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1520-1778 |
2.42e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.67 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1520 AQRRLEDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeaskrQDVAADAEKQK 1595
Cdd:pfam09787 16 AARILQSKEKLIASLKEgsgvEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTEL-------QELEAQQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1596 QNIQQELQHLKSlsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkakseaeLQE-LRDRAAEAEKlrkaaqd 1674
Cdd:pfam09787 89 ESSREQLQELEE--QLATERSARREAEAELERLQEELRYLEEELRRSKAT---------LQSrIKDREAEIEK------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1675 eaerLRKQVAEETQrKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYK----MQAEEAERRMKQAEEEKIRQIRVVEEVA 1750
Cdd:pfam09787 151 ----LRNQLTSKSQ-SSSSQSELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGI 225
|
250 260
....*....|....*....|....*...
gi 1389908274 1751 QKSAATQLQTKAMSFSEQTTKLEESLKK 1778
Cdd:pfam09787 226 SDGEGTRLRNVPGLFSESDSDRAGMYGK 253
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1500-1912 |
2.43e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1500 RTRYSELMTLTNQYIKF---IIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMK 1576
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1577 MKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQ 1656
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1657 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRkkNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAE 1736
Cdd:COG5278 266 ALLALAALLLALAAAAALAAAAALELAAAEALA--LAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1737 EEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1816
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1817 KANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECI 1896
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLAL 503
|
410
....*....|....*.
gi 1389908274 1897 RLKADFEHAEQQRGLL 1912
Cdd:COG5278 504 ALAALLLAAAEAALAA 519
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1996-2679 |
2.50e-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: 47.53 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1996 QRQIAEEEAARQrsEAEKILKEKLAA--------INEATRLKTEAEMALKAKEAENERLKRQA----EEEAYQRKLLEDQ 2063
Cdd:pfam12128 271 ETLIASRQEERQ--ETSAELNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2064 AAQHKQDIE--EKITQLQTSSDSEL-----GRQKNIVEETLKQKKVVEEEIHIIKinfHKASKEKADLESELKKLKG-IA 2135
Cdd:pfam12128 349 LPSWQSELEnlEERLKALTGKHQDVtakynRRRSKIKEQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESeLR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2136 DETQKSKLKAEEEAEKLKklaaeeeRRRKEAEEKVKRITAAEEEAARQcKAAQEEVERLKKKAEDANKQKEkaekeaekq 2215
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLK-------SRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVE--------- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2216 vvlakeAAQKctaaEQKAQDVLSKNKEDVLAQEKLRDEfENAKKLAQEAEKAKEKAEKEAALLRQkaeEAEKQKKAAENE 2295
Cdd:pfam12128 489 ------RLQS----ELRQARKRRDQASEALRQASRRLE-ERQSALDELELQLFPQAGTLLHFLRK---EAPDWEQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2296 AAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSkhkkeaEQALQQK-SQVEKELTVVKLQLDETDKQKV 2374
Cdd:pfam12128 555 ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAAS------EEELRERlDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2375 LLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKDKDSTQKLLAE----EAEKMKSLAEE 2450
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQS---EKDKKNKALAERKDSANERLNSLEAQlkqlDKKHQAWLEEQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2451 AGRLSVEAEETARQRQIAESNLAEQRA-LAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2529
Cdd:pfam12128 706 KEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2530 KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtEKHTTEivvqKLETQRLQ 2609
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM-ERKASE----KQQVRLSE 860
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2610 STREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQ--IEQQKAELQQSFLTEKGLLLKREKEVE 2679
Cdd:pfam12128 861 NLRGLRCEMSKLATL------------------KEDANSEQAQgsIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3969-4005 |
2.71e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.71e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 3969 LRLLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKET 4005
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3562-3595 |
2.73e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908274 3562 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPE 3595
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1521-1754 |
2.90e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1521 QRRLEDdekasEKLKEEERRKMAEiqAELDKQKQMAEAHAKSVAKAEQEALELKMKMK-EEASKRQDVAADAEKQKQNIQ 1599
Cdd:PRK05035 459 QARLER-----EKAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAATQPIVIKaGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1600 QELQhlKSLSDQEIKSKNQQLEDALV-SRRKIEEEIHIIRIQLEKTTAHKAKSEAELqelrdraAEAeKLRKAAQDEAER 1678
Cdd:PRK05035 532 ARQA--EKQAAAAADPKKAAVAAAIArAKAKKAAQQAANAEAEEEVDPKKAAVAAAI-------ARA-KAKKAAQQAASA 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1679 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD--DLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSA 1754
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEpvDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1794-1947 |
2.95e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.32 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1794 KKQQKEANTAREEAEQE----LEiwRQKanealrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKEN 1869
Cdd:PTZ00491 662 KSQEAAARHQAELLEQEargrLE--RQK------MHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAE 733
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1870 AEKELDKQRKFAEQIAQQklsAEQECIRLKADFEHAEQQRgllDNELQRlknevnstEKQRKQLEDELNKVRSEMDSL 1947
Cdd:PTZ00491 734 AEVEQAELRAKALRIEAE---AELEKLRKRQELELEYEQA---QNELEI--------AKAKELADIEATKFERIVEAL 797
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1963-2193 |
3.23e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1963 EKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAe 2042
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEE- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2043 nerLKRQAEEEAyqrKLLEDQAAQHKQDIEEKITqlqtssdselgrqknivEETLKQKKVVEEeihiikinfhKASKEKA 2122
Cdd:TIGR02794 148 ---AAKQAEEEA---KAKAAAEAKKKAEEAKKKA-----------------EAEAKAKAEAEA----------KAKAEEA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 2123 DLESELKKLKGIADetqksklkAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEE--AARQCKAAQEEVER 2193
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--------AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGsnAEKQGGARGAAAGS 259
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2465-2614 |
3.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2465 RQIAESNLAEQRALAEKILKE---KMQAIQEATKLKAEaEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEA 2541
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEakkEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2542 ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ--------ADEVKAQ-LQRTE---KHTTEIVVQKLETQ-RL 2608
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEIlLEKVEeeaRHEAAVLIKEIEEEaKE 184
|
....*.
gi 1389908274 2609 QSTREA 2614
Cdd:PRK12704 185 EADKKA 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1778-2358 |
3.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1778 KEQGNVLK-LQEEADKLKKQQKEANTARE--------EAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQK 1846
Cdd:COG4913 248 REQIELLEpIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAEleELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1847 LEAERDAKKrGKAEEAALKQKENAEKELDKQR----KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1922
Cdd:COG4913 328 LEAQIRGNG-GDRLEQLEREIERLERELEERErrraRLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VNSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvntEKSKQLLESEALKM-KQLADE----AARMRSVAEEAkkqr 1997
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASL---------------ERRKSNIPARLLALrDALAEAlgldEAELPFVGELI---- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1998 QIAEEEAARQRSeAEKILKeklaaiNEATRLKTEAEMALKAKEA-ENERLKRQ-------AEEEAYQRKLLEDQAAQHKQ 2069
Cdd:COG4913 468 EVRPEEERWRGA-IERVLG------GFALTLLVPPEHYAAALRWvNRLHLRGRlvyervrTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2070 DIEEkiTQLQTSSDSELGRQKNIV----EETLKQ-KKVVEEEIHIikinfhKASKEKADleselkklKGIADETQKSKLK 2144
Cdd:COG4913 541 DFKP--HPFRAWLEAELGRRFDYVcvdsPEELRRhPRAITRAGQV------KGNGTRHE--------KDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2145 AEEEAEKLKKLAAEeerrrkeaeekVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEaekqvVLAKEAAQ 2224
Cdd:COG4913 605 GFDNRAKLAALEAE-----------LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2225 KCTAAEQKAQDvLSKNKEDVLAQEKLRDEfenakklaqeaekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQN 2304
Cdd:COG4913 669 EIAELEAELER-LDASSDDLAALEEQLEE------------------------LEAELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2305 DTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKKEAEQALQQKSQVEKE 2358
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERELRENLEERIDALRA 780
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2435-2760 |
3.45e-04 |
|
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: 47.25 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2435 KLLAEEAEkmkSLAEEAGRLSVEAEETARQRQIAESNLAEQRALA-----EKILKEKMQAIQEATK-LKAEAEKLQKQKD 2508
Cdd:COG3096 788 EELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELEReLAQHRAQEQQLRQ 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2509 QAQETAKRLQE-----------DKQQIQQRLDKETEGFQKSLEAER--KRQLEASAEAEKL--KLRVKELSLAQTKAEDE 2573
Cdd:COG3096 865 QLDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLvaVLQSDPEQFEQLQADYL 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 akkfkkQADEVKAQLQRTEKHTTEIVvqkletQRLQ--STREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQE 2651
Cdd:COG3096 945 ------QAKEQQRRLKQQIFALSEVV------QRRPhfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQA 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2652 QIEQQKAELQQ---SFLTEKGLLlkreKEVEGEKKRFEKQLEDEMK-KAKALKDE------QERQRK-LMEEERKKLQAI 2720
Cdd:COG3096 1013 QYSQYNQVLASlksSRDAKQQTL----QELEQELEELGVQADAEAEeRARIRRDElheelsQNRSRRsQLEKQLTRCEAE 1088
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908274 2721 MDEAVRKQKEAEEEMKNkQREMDVLDKKRLEQEKQLAEEN 2760
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQ-EREQVVQAKAGWCAVLRLARDN 1127
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1756-2078 |
3.61e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1756 TQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKK 1835
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1836 SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE 1915
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1916 LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK 1995
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1996 QRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKI 2075
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
...
gi 1389908274 2076 TQL 2078
Cdd:COG4372 368 ADG 370
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1508-1784 |
3.72e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1508 TLTNQYIKFIIDAQRrlEDDEKASEKLKEEerrkMAEIQAELDKqkqmaeahaksvakAEQEALELKMKMKEEASKRQdv 1587
Cdd:COG3206 156 ALAEAYLEQNLELRR--EEARKALEFLEEQ----LPELRKELEE--------------AEAALEEFRQKNGLVDLSEE-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1588 AADAEKQKQNIQQELQHLKSLSdQEIKSKNQQLEDALvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEK 1667
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAEL-AEAEARLAALRAQL-GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1668 LRKAAQDEAERLRKQVAEETQRkknaedeLKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQIRVVE 1747
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQR-------ILASLEAELEALQAREASLQA------QLAQLEARLAELPELEAELRRLER 358
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908274 1748 EV-AQKSAATQLQTKAmsfseQTTKLEESLKKEQGNVL 1784
Cdd:COG3206 359 EVeVARELYESLLQRL-----EEARLAEALTVGNVRVI 391
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2328-2494 |
3.81e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.63 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEMSKHKKEA-EQALQQKSQVEKELTVVKLQLDETDKQKVLLD-QELQRvkgEVNDAFKQKSQVEVELARVR 2405
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQR---EEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2406 IQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaEEAEKMKS---LAEEAGRLSVEAEETARQR--QIAESNLAEQRALAE 2480
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRvkKIEEEADLEAERKAQ 179
|
170
....*....|....
gi 1389908274 2481 KILKEKMQAIQEAT 2494
Cdd:PRK12705 180 NILAQAMQRIASET 193
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2287-2553 |
3.86e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.14 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2287 KQKKAAENEAAKQAKAQNDteKQRkeaeeeaarraaaeaaaLKQ-KQQADAEMSKHKKEAE----QALQQKSQVEKEltV 2361
Cdd:NF012221 1552 KQDDAAQNALADKERAEAD--RQR-----------------LEQeKQQQLAAISGSQSQLEstdqNALETNGQAQRD--A 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2362 VKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELA---RVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLla 2438
Cdd:NF012221 1611 ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglLDRVQ-EQLDDAKKISGKQLADAKQRHVDNQQKV-- 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2439 eeaekMKSLAE-EAGrlsveAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLK----AEAEKLQKQKDQAQET 2513
Cdd:NF012221 1688 -----KDAVAKsEAG-----VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAEsdanAAANDAQSRGEQDASA 1757
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908274 2514 AK----RLQEDKQQIQQRLDK--ETEGFQKSLEAERKRQLEASAEA 2553
Cdd:NF012221 1758 AEnkanQAQADAKGAKQDESDkpNRQGAAGSGLSGKAYSVEGVAEP 1803
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1747-1930 |
4.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1747 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR--- 1823
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1824 -------------------------LRLQAEEEAQKK-----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKE 1873
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 1874 LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1930
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3194-3228 |
4.09e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.09e-04
10 20 30
....*....|....*....|....*....|....*
gi 1389908274 3194 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETA 3228
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2979-3015 |
4.47e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.47e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908274 2979 TKFLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADM 3015
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2427-2786 |
4.48e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2427 QKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ 2506
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2507 KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA 2586
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2587 QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLT 2666
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2667 EKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLD 2746
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908274 2747 KKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTV 2786
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2460-2661 |
4.52e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2460 ETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQ-KQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKS 2538
Cdd:pfam17045 57 EIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2539 LEAERKR----QLEASAEAEKlKLRVKELSLAQTKAEDEAKKFKKQADE-VKAQLQR----TEKHTTEIVVQKLETQRLQ 2609
Cdd:pfam17045 137 LEWEQQRlqyqQQVASLEAQR-KALAEQSSLIQSAAYQVQLEGRKQCLEaSQSEIQRlrskLERAQDSLCAQELELERLR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2610 StreaddLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQ 2661
Cdd:pfam17045 216 M------RVSELGDSNRKLLEEQQRLLEELRMSQRQLQVLQNELMELKATLQ 261
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2241-2558 |
4.56e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2241 KEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARR 2320
Cdd:COG5185 261 QNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2321 AAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAF--------K 2392
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLedtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2393 QKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNL 2472
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR------SVRSKKEDLNEELTQIESRV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2473 AEqralaekiLKEKMQaiQEATKLKAEAEKLQKQKDQAQETAKRLqEDKQQIQQRLDKETE----GFQKSLEAERKRQLE 2548
Cdd:COG5185 495 ST--------LKATLE--KLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLipasELIQASNAKTDGQAA 563
|
330
....*....|
gi 1389908274 2549 ASAEAEKLKL 2558
Cdd:COG5185 564 NLRTAVIDEL 573
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2466-2660 |
4.82e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2466 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfQKSLEAERKR 2545
Cdd:TIGR02794 36 EIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA--AKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2546 QLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLE 2625
Cdd:TIGR02794 114 AEEKQKQAEEAKA--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA---KKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1389908274 2626 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2660
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1561-1807 |
4.87e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.58 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1561 KSVAKAEQEALELKMK----MKEEASKRQDVAadaekqkqniQQELQ-HLKSLSDQeiksKNQQLEDalvsrrkieeeih 1635
Cdd:pfam10168 524 KLSSPSPQECLQLLSRatqvFREEYLKKHDLA----------REEIQkRVKLLKLQ----KEQQLQE------------- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1636 iiriqlekttahkakseaeLQELRDraaEAEKLRKAAQDEAERLR----KQvaEETQRK-----KNAEDELKRKSDAEKE 1706
Cdd:pfam10168 577 -------------------LQSLEE---ERKSLSERAEKLAEKYEeikdKQ--EKLMRRckkvlQRLNSQLPVLSDAERE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1707 AAKQKQRALDDLQKYKMQAEEAerRMKQaeEEKIRQIRVVEEVAQKSAAtqlqtkamsfseqttkleeSLKKEQGNVLK- 1785
Cdd:pfam10168 633 MKKELETINEQLKHLANAIKQA--KKKM--NYQRYQIAKSQSIRKKSSL-------------------SLSEKQRKTIKe 689
|
250 260
....*....|....*....|...
gi 1389908274 1786 -LQEEADKLKKQQKEANTAREEA 1807
Cdd:pfam10168 690 iLKQLGSEIDELIKQVKDINKHV 712
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1524-1941 |
4.95e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1524 LEDDEKASEKLKE-EERRKMAEiQAELDKQKqmaeaHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQEL 1602
Cdd:PRK04863 886 LLADETLADRVEEiREQLDEAE-EAKRFVQQ-----HGNALAQLEPIVSVLQSDPEQFEQLKQDYQQ-AQQTQRDAKQQA 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1603 QHLKSLsdqeiksknqqledalVSRRkieeeihiiriqlekttAHKAKSEA--------ELQE-LRDRAAEAEKLRKAAQ 1673
Cdd:PRK04863 959 FALTEV----------------VQRR-----------------AHFSYEDAaemlaknsDLNEkLRQRLEQAEQERTRAR 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1674 DEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKqkqraldDLQKYKMQA-EEAERRMKQAEEEKIRQIRvveevAQK 1752
Cdd:PRK04863 1006 EQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQ-------ELQDLGVPAdSGAEERARARRDELHARLS-----ANR 1073
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1753 SAATQLQTkamsfseQTTKLEESLKKEQGnvlklqeeadKLKKQQKEANTAREEAEQeleiwrQKANEALRLRLQAEEEA 1832
Cdd:PRK04863 1074 SRRNQLEK-------QLTFCEAEMDNLTK----------KLRKLERDYHEMREQVVN------AKAGWCAVLRLVKDNGV 1130
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1833 QKKSHAQEEAEkQKLEAERDAkkRGKAEEAALKQKENAEKELDKQR-----KFAEQIAQ------QKLS--AEQECIRLK 1899
Cdd:PRK04863 1131 ERRLHRRELAY-LSADELRSM--SDKALGALRLAVADNEHLRDVLRlsedpKRPERKVQfyiavyQHLRerIRQDIIRTD 1207
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 1900 ADFEHAEQqrglLDNELQRLKNEVNSTEKQ------------RKQLEDELNKVR 1941
Cdd:PRK04863 1208 DPVEAIEQ----MEIELSRLTEELTSREQKlaissesvaniiRKTIQREQNRIR 1257
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1642-1877 |
4.97e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1642 EKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK---------NAEDELKRKSDAEKEAAKQKQ 1712
Cdd:pfam05667 255 QLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEklqftneapAATSSPPTKVETEEELQQQRE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1713 RALDDLQKykmQAEEAERRMKQAEEE------KIRQirVVEEVAQKSAATQLQTKAMSFSEQTTKLeesLKKEQGNVLKL 1786
Cdd:pfam05667 335 EELEELQE---QLEDLESSIQELEKEikklesSIKQ--VEEELEELKEQNEELEKQYKVKKKTLDL---LPDAEENIAKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1787 QEEADKLKkqQKEANTAREeaeqeleiWrqkanEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALK 1865
Cdd:pfam05667 407 QALVDASA--QRLVELAGQ--------W-----EKHRVPLIEEYRALKEAKSNKEDEsQRKLEEIKELREKIKEVAEEAK 471
|
250
....*....|..
gi 1389908274 1866 QKENAEKELDKQ 1877
Cdd:pfam05667 472 QKEELYKQLVAE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2646-2793 |
5.28e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2646 ANAQQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALkdeQERQRKLmEEERKKLQAIMDEAV 2725
Cdd:COG1196 237 LEAELEELEAELEELEA----ELEELEAELAELEAELEELRLELEELELELEEA---QAEEYEL-LAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2726 RKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2793
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
213-310 |
5.48e-04 |
|
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: 43.42 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNKHLVKAQ--RHV-------TDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 279
Cdd:cd21292 25 EKVAFVNWINKNLGDDPdcKHLlpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1389908274 280 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 310
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1982-2199 |
5.52e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1982 EAARMRSVAEEAKKQRQIAEEEAARQRSEAE---KILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRK 2058
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKE---LSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2059 LLEDQAAQHKQDIEE------KITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 2132
Cdd:pfam07888 119 ALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2133 GIADETQKSKLKAEEEAEKLKKLAAEEerrrkeaeekvKRITAAEEEAARQCKAAQEEVERLKKKAE 2199
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTLTQKLTTA-----------HRKEAENEALLEELRSLQERLNASERKVE 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1905-2187 |
5.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1905 AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKvrsemdslLQMKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1984
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------LERRIAALARRIRALEQELAALEAE---LAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1985 RMRsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 2064
Cdd:COG4942 94 ELR--AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2065 AQHKQDIEEKITQLQtssdselgrqkniveetlkqkkvveeeihiikinfhKASKEKADLESELKKLKGIADETQKSKLK 2144
Cdd:COG4942 167 AELEAERAELEALLA------------------------------------ELEEERAALEALKAERQKLLARLEKELAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1389908274 2145 AEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKAA 2187
Cdd:COG4942 211 LAAELAELQQ-------EAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1656-1778 |
5.58e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 45.75 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1656 QELRDRAAEAEKLRKAAQDEAERLRKQVAEEtqRKKNAEDELKRKSDAEKEAAKQKQRALddlqkyKMQAEEAERRMKQA 1735
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLERVLEKIAES--AATAEAREEKRKTKAQRNKEKRRKEEE------REAKEEKALKKKLA 269
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1389908274 1736 EEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1778
Cdd:pfam07767 270 QLERLKEIA--KEIAEKEKEREEKAEARKREKRKKKKEEKKLR 310
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2278-2793 |
5.82e-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: 46.27 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2278 LRQKAEEAEKQKKAAEN-----EAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQK 2352
Cdd:pfam05557 23 LEHKRARIELEKKASALkrqldRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2353 SQV----EKELTVVKLQLDETDKQKVLLDQELQRVKgEVNDAFKQK-SQVEVELARVRIQMEELVKLKLKIEEENRRLMQ 2427
Cdd:pfam05557 103 REVisclKNELSELRRQIQRAELELQSTNSELEELQ-ERLDLLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2428 KDKDSTQ-KLLAEEAEKMKSLAEEAGRLSVEAE---ETARQRQIAESNLAEQRALAEKilKEKMQAiqEATKLKAEAEKL 2503
Cdd:pfam05557 182 QEQDSEIvKNSKSELARIPELEKELERLREHNKhlnENIENKLLLKEEVEDLKRKLER--EEKYRE--EAATLELEKEKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2504 QKQ----KDQAQETA------KRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASaeaekLKLRVKELSLAQTKAEDE 2573
Cdd:pfam05557 258 EQElqswVKLAQDTGlnlrspEDLSRRIEQLQQR--EIVLKEENSSLTSSARQLEKA-----RRELEQELAQYLKKIEDL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 AKKFKKQaDEVKAQLQRT---------------EKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEEL 2638
Cdd:pfam05557 331 NKKLKRH-KALVRRLQRRvllltkerdgyrailESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 QRKSKEMANAQQEQIE---QQKAELQQSFLTEKGLLLKRE-KEVEGEKKRFEKQledemkkakalKDEQErqrklMEEER 2714
Cdd:pfam05557 410 LGGYKQQAQTLERELQalrQQESLADPSYSKEEVDSLRRKlETLELERQRLREQ-----------KNELE-----MELER 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2715 KKLQAIMDEAVRKQKEAEEEMKNKQREmdvldkKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2793
Cdd:pfam05557 474 RCLQGDYDPKKTKVLHLSMNPAAEAYQ------QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVL 546
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1682-1849 |
5.84e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.70 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1682 QVAEETQRKKNAEDELKRKSDAEKE---AAKQKQRalddlqKYKMQAEEAERRMKQAEEEKiRQirvveEVAQKSAATQL 1758
Cdd:pfam13904 34 QSSSLTYARKLEGLKLERQPLEAYEnwlAAKQRQR------QKELQAQKEEREKEEQEAEL-RK-----RLAKEKYQEWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1759 QTKAmsfsEQTTKLEESLKKEQGNvLKLQEEADKLKKQQKEantarEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1838
Cdd:pfam13904 102 QRKA----RQQTKKREESHKQKAA-ESASKSLAKPERKVSQ-----EEAKEVLQEWERKKLEQQQRKREEEQREQLKKEE 171
|
170
....*....|.
gi 1389908274 1839 QEEAEKQKLEA 1849
Cdd:pfam13904 172 EEQERKQLAEK 182
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1640-2066 |
5.94e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.05 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRkknaedelKRKSDAEKEAAKQKQRALDDLQ 1719
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL--------LALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1799
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1800 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1879
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1880 FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASM 1959
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1960 VNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK 2039
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1389908274 2040 EAENERLKRQAEEEAYQRKLLEDQAAQ 2066
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1903-2039 |
6.26e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1903 EHAEQQ-RGLLdnELQRLKNEVnSTEKQRKQLedelnkvrsemdslLQMKinAEKASMVNTEKSKQ--LLESEALKMKQL 1979
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRTKL--------------LELQ--AESAAVESSGQSRAeaLAEAEARLIEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1980 AD-EAARMRSVAE------EAKKQRQIAEEEAARQRSEAE-KILKEKLAAINEATRLK---------TEAEMA-----LK 2037
Cdd:PTZ00491 734 AEvEQAELRAKALrieaeaELEKLRKRQELELEYEQAQNElEIAKAKELADIEATKFErivealgreTLIAIAragpeLQ 813
|
..
gi 1389908274 2038 AK 2039
Cdd:PTZ00491 814 AK 815
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
348-429 |
6.35e-04 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 42.29 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 348 RCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQ-AFSVAE--RELGVTKLLDPEDVDVPHPDEksIITYV 424
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPEDIVSGNPRL--NLAFV 109
|
....*
gi 1389908274 425 SSLYD 429
Cdd:cd21218 110 ATLFN 114
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2432-2730 |
6.59e-04 |
|
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: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2432 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE-QRAL--AEKI-------------LKEKMQAIQEATK 2495
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALrqQEKIeryqedleelterLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2496 LKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD-KETEGFQKsleaerkRQ-LEASAEAEKLkLRVKELSLAQtkAEDE 2573
Cdd:COG3096 376 QLAEAEA---RLEAAEEEVDSLKSQLADYQQALDvQQTRAIQY-------QQaVQALEKARAL-CGLPDLTPEN--AEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2574 AKKFKKQADEVKAQLQRTEkhtteivvQKL---ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ 2650
Cdd:COG3096 443 LAAFRAKEQQATEEVLELE--------QKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2651 EQIEQQKAELQQsfltekglLLKREKEVEGEKKRFEKQ----------LEDEMKKAKALKDEQERQRKLMEEERKKLQAI 2720
Cdd:COG3096 515 QQLRAQLAELEQ--------RLRQQQNAERLLEEFCQRigqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330
....*....|
gi 1389908274 2721 MDEAVRKQKE 2730
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2656-2771 |
6.70e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.97 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2656 QKAELQQSFLTEKglllkreKEVEGEKKRFEKQL---EDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE-- 2730
Cdd:pfam02841 173 KAEEVLQEFLQSK-------EAVEEAILQTDQALtakEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEhv 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2731 ------AEEEMKNKQREMD-VLDKKRLEQEKQLAE----ENKKLREQLQTFE 2771
Cdd:pfam02841 246 kqliekMEAEREQLLAEQErMLEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2420-2528 |
6.91e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.60 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2420 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2499
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1389908274 2500 AEKLQKQKDQAQETAKRLQEDKQQIQQRL 2528
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2420-2679 |
7.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2420 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAgrlsvEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatkLKAE 2499
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSE----------LESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2500 AEKLQKQKDQAQEtakRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEAsaeaekLKLRVKELSLAQTKAEDEAKKFKK 2579
Cdd:COG3206 228 LAEARAELAEAEA---RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE------LEAELAELSARYTPNHPDVIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2580 QADEVKAQLQRTekhtTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeeLQRKSKEMANAQQEQIE-QQKA 2658
Cdd:COG3206 299 QIAALRAQLQQE----AQRILASLEAELEALQAREASLQAQLAQ--------------LEARLAELPELEAELRRlEREV 360
|
250 260
....*....|....*....|.
gi 1389908274 2659 ELQQSFLTEkglLLKREKEVE 2679
Cdd:COG3206 361 EVARELYES---LLQRLEEAR 378
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1767-2194 |
7.21e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1767 EQTTKLEESLKKeQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrQKANEALRLRlqaeEEAQKKSHAQEEAEK-- 1844
Cdd:pfam10174 158 ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLD---QKEKENIHLR----EELHRRNQLQPDPAKtk 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1845 --QKLEAERDAK----KRG--KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAE---QECIRLKADFEHAEQQRGLLD 1913
Cdd:pfam10174 230 alQTVIEMKDTKisslERNirDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1914 NELQRLKNEvNSTEKQRKQLEDELNKVRSEMDSLLQMKINA------EKASMVNtEKSKQLLE---------SEALKMKQ 1978
Cdd:pfam10174 310 TKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDAlrlrleEKESFLN-KKTKQLQDlteekstlaGEIRDLKD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1979 LADEAARMRSVAEeaKKQRQIAEEEAARQRSEAEkiLKEKLAAI-----NEATRLKTeAEMALKAKEAENERLKRQAEEE 2053
Cdd:pfam10174 388 MLDVKERKINVLQ--KKIENLQEQLRDKDKQLAG--LKERVKSLqtdssNTDTALTT-LEEALSEKERIIERLKEQRERE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2054 AYQRKLLEDQAAQHKQDIEEKITQLQT------SSDSELGRQKNIVEETLKQKkvvEEEIHIIKINFHKASKEKADLESE 2127
Cdd:pfam10174 463 DRERLEELESLKKENKDLKEKVSALQPeltekeSSLIDLKEHASSLASSGLKK---DSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2128 LKKLKGIADETQKSklkaEEEAEKLKKLAaeeerrrkeaeekvKRITAAEEEAARqckaAQEEVERL 2194
Cdd:pfam10174 540 LKKAHNAEEAVRTN----PEINDRIRLLE--------------QEVARYKEESGK----AQAEVERL 584
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1655-1887 |
7.26e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.97 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1655 LQELRDRAAEAEK------LRKAAQDEAERLRKQVAEETQRKKnaeDELKRKSdaEKEAAKQKQRALDDLqkykmqAEEA 1728
Cdd:pfam02841 67 LQELLDLHRDCEKeaiavfMKRSFKDENQEFQKELVELLEAKK---DDFLKQN--EEASSKYCSALLQDL------SEPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1729 ERRMKQAEEEK-------IRQIRVVEEVAQKSAATQLQTKAM--SFSEQTTKLEESLkkeqgnvLKLQEEADKLKKQQKE 1799
Cdd:pfam02841 136 EEKISQGTFSKpggyklfLEERDKLEAKYNQVPRKGVKAEEVlqEFLQSKEAVEEAI-------LQTDQALTAKEKAIEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1800 ANTAREEAEQELEIWRQKANEalrlrLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1878
Cdd:pfam02841 209 ERAKAEAAEAEQELLREKQKE-----EEQMMEAQERSYQEHVKQlIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
|
....*....
gi 1389908274 1879 KFAEQIAQQ 1887
Cdd:pfam02841 284 TEAESLQKE 292
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1923-2257 |
7.28e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1923 VNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvNTEKSKQLLESEALKMKQLADEAA----RMRSVAEEAKKQRQ 1998
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAR-----------EVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1999 IAEEEAARqrsEAEKILKEKLAAinEATRLKtEAEMALKAKEAENERLkRQAEEEAYQRKLLEDQaaQHKQDIEEKITQL 2078
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERV-RQELEAARKVKILEEE--RQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2079 QTSSDSELGRQKNIveETLKQKKVVEEEihiikinfhKASKEKADLESELKKLKgiADETQKSKLKAEEEAEKLKKLAAE 2158
Cdd:pfam17380 424 QIRAEQEEARQREV--RRLEEERAREME---------RVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2159 EERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA--EQKAQDV 2236
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAteERSRLEA 570
|
330 340
....*....|....*....|....
gi 1389908274 2237 LSKNKE---DVLAQEKLRDEFENA 2257
Cdd:pfam17380 571 MEREREmmrQIVESEKARAEYEAT 594
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2037-2297 |
7.52e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.22 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2037 KAKEAENERLKRQAEEEAyqrklleDQAAQHKQDIEEKITQLQTSSDSELGRQKNiveetLKQKKVVEEEihiikinfhK 2116
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA-------KKEQERQKKLEQQAEEAEKQRAAEQARQKE-----LEQRAAAEKA---------A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2117 ASKEKADLESELKKlkgiadeTQKSKLKAEEEAEKLKKLAaeeerrrkeaeekvkritAAEEEAARQCKAAQEEVERLKK 2196
Cdd:TIGR02794 105 KQAEQAAKQAEEKQ-------KQAEEAKAKQAAEAKAKAE------------------AEAERKAKEEAAKQAEEEAKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2197 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2276
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260
....*....|....*....|.
gi 1389908274 2277 LlrQKAEEAEKQKKAAENEAA 2297
Cdd:TIGR02794 240 L--ASGSNAEKQGGARGAAAG 258
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1559-1929 |
7.79e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1559 HAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIR 1638
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1639 IQLEKTtahkaksEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1718
Cdd:COG4372 80 EELEEL-------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1719 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1798
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1799 EANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1878
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 1879 -KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ 1929
Cdd:COG4372 313 lEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2279-2623 |
7.88e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.90 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2279 RQKAEEAEKQKKAAENEAAK----QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK-----------K 2343
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLpkseQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKeasdtaeisreK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2344 EAEQALQQKSQVEKEL--TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElarvriQMEELVKLKLKI-EE 2420
Cdd:pfam09731 180 ATDSALQKAEALAEKLkeVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKA------QSLAKLVDQYKElVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2421 ENRRLMQKDKDST-QKLLAEEAEKMKSLAEEAGRL--SVEAEETARQRQIAESNLAEQRALAEKILKekmqaiQEATKLK 2497
Cdd:pfam09731 254 SERIVFQQELVSIfPDIIPVLKEDNLLSNDDLNSLiaHAHREIDQLSKKLAELKKREEKHIERALEK------QKEELDK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2498 AEAEKLQKQKDQaqetakrLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ---------- 2567
Cdd:pfam09731 328 LAEELSARLEEV-------RAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIelqreflqdi 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2568 -TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV---QKLETQRLQSTREA--DDLKSAIAD 2623
Cdd:pfam09731 401 kEKVEEERAGRLLKLNELLANLKGLEKATSSHSEvedENRKAQQLWLAVEAlrSTLEDGSAD 462
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2519-2759 |
7.95e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.71 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2519 EDKQQIQQRLdKETEGFQKSLEAERKRQleasAEAEKLKLRVKELslaqtkaedeakkfkKQADEVKAQLQRTEKHTTEI 2598
Cdd:pfam15709 329 EQEKASRDRL-RAERAEMRRLEVERKRR----EQEEQRRLQQEQL---------------ERAEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2599 VvqKLETQRLQSTREaddlksaiadleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEV 2678
Cdd:pfam15709 389 I--RLRKQRLEEERQ-------------------------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2679 E-GEKKRFEKQLEDEMKKAkaLKDEQERQRKLMEEERKKLQaimdeavRKQKEAEE----EMKNKQREMDVLDKKRLEQE 2753
Cdd:pfam15709 442 EeAERAEAEKQRQKELEMQ--LAEEQKRLMEMAEEERLEYQ-------RQKQEAEEkarlEAEERRQKEEEAARLALEEA 512
|
....*.
gi 1389908274 2754 KQLAEE 2759
Cdd:pfam15709 513 MKQAQE 518
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1711-2076 |
8.06e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1711 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEA 1790
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1791 DKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENA 1870
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1871 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1950
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1951 KINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKT 2030
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1389908274 2031 EAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 2076
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
208-316 |
8.23e-04 |
|
third 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 third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 42.28 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 208 ERDRVQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 278
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908274 279 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 316
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1648-1720 |
8.24e-04 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 8.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 1648 KAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQK 1720
Cdd:cd06503 53 LAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2639-2762 |
8.35e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 QRKSKEMANAQQE---QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERK 2715
Cdd:PRK09510 68 QQQQKSAKRAEEQrkkKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1389908274 2716 KLQAIMDEAVRKQKEAEEEMKnKQREMDVLDKKRLEQEKQLAEENKK 2762
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2639-2759 |
8.41e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.25 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 QRKSKEMANAQQEQiEQQKAELQQSflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKAlkdeqERQRKLMEEERKKLQ 2718
Cdd:COG2268 208 AERETEIAIAQANR-EAEEAELEQE--REIETARIAEAEAELAKKKAEERREAETARAEA-----EAAYEIAEANAEREV 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908274 2719 AIMDEAVRKQKEAEEEMKNKQREMDVLD---KKRLEQEKQLAEE 2759
Cdd:COG2268 280 QRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQAAEA 323
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
206-314 |
8.64e-04 |
|
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: 42.29 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 206 ADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 281
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1389908274 282 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 314
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1847-2293 |
8.79e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1847 LEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNST 1926
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1927 EKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAAR 2006
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2007 QRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSEL 2086
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2087 GRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEA 2166
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2167 EEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLA 2246
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908274 2247 QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE 2293
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2432-2736 |
9.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2432 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKEKMQAIqEATKLKAEAEKLQKQKDQAQ 2511
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD----ALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2512 ETAKRLQEDKQQIQqrldketegfqksleaerkrqlEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRT 2591
Cdd:COG4913 682 ASSDDLAALEEQLE----------------------ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2592 EKHTTEIVVQKLETQRLQSTREA--DDLKSAIADleeerkklkkeaeeLQRKSKEMANAQQEQIEQQKAELQQSFLTEKG 2669
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAveRELRENLEE--------------RIDALRARLNRAEEELERAMRAFNREWPAETA 805
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908274 2670 LLLKREKEVEGEKKRFEKQLEDEMKKAKAlkDEQERQRKLMEEERKKLQAIMDEAVRkqkEAEEEMK 2736
Cdd:COG4913 806 DLDADLESLPEYLALLDRLEEDGLPEYEE--RFKELLNENSIEFVADLLSKLRRAIR---EIKERID 867
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1646-1720 |
9.94e-04 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 42.85 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1646 AHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAEETQR-----KKNAEDELKR-KSDAEKEAAKQKQRALDDLQ 1719
Cdd:COG0711 43 AERAKEEAEAAL-----AEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELR 117
|
.
gi 1389908274 1720 K 1720
Cdd:COG0711 118 A 118
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1528-1762 |
1.08e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1528 EKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvAKAEQEALELKMKMKEEASKRQDVAADAEK-QKQNIQQELQHlk 1606
Cdd:pfam15709 331 EKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREELELEQQRRFEEIRlRKQRLEEERQR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1607 slsdQEIKSKNQQLEdalvsrrkieeeihiirIQLEKTTAHKAKSE--AELQELRdraaeaeklRKAAQDEAERlrkqVA 1684
Cdd:pfam15709 403 ----QEEEERKQRLQ-----------------LQAAQERARQQQEEfrRKLQELQ---------RKKQQEEAER----AE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1685 EETQRKKNAEDELKRKSDAEKEAAKQKQralddlQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKA 1762
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEER------LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
207-310 |
1.14e-03 |
|
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: 42.05 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 207 DERDRVQkktFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETL-------PREKGRM--RFHK 268
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908274 269 LQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 310
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1697-1920 |
1.27e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1697 LKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEkirqirvVEEVAQKSAATQLQTKAMSFSEQTTKLEESL 1776
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEAA-------LEEFRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1777 KKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-LRLRLQAEEEAQKKSH-------AQEEAEKQKLE 1848
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeLEAELAELSARYTPNHpdvialrAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 1849 AERDAKKRG-KAEEAALKQKENA-EKELDKQRKFAEQIAQQklsaEQECIRLKADFEHAEQqrgLLDNELQRLK 1920
Cdd:COG3206 309 QEAQRILASlEAELEALQAREASlQAQLAQLEARLAELPEL----EAELRRLEREVEVARE---LYESLLQRLE 375
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1521-1838 |
1.32e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1521 QRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmKMKEEASKRQdvaadaekQKQNIQQ 1600
Cdd:pfam15558 61 EQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERA-RQEAEQRKQC--------QEQRLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1601 ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahKAKSEAELQELRDRAAEAEKLRKA--------A 1672
Cdd:pfam15558 132 KEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSE--LLNHQARKVLVDCQAKAEELLRRLsleqslqrS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1673 QDEAERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDdlQKYKMQAEEAERRMKQAEEekirqirVVEEVAQK 1752
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRA---KWRAEEKEEERQ--EHKEALAELADRKIQQARQ-------VAHKTVQD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1753 SAAtqlqtkamsfseqttkleeslKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEA 1832
Cdd:pfam15558 278 KAQ---------------------RARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEA 336
|
....*.
gi 1389908274 1833 QKKSHA 1838
Cdd:pfam15558 337 RKTARA 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1609-1836 |
1.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1609 SDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE--- 1685
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1686 ETQRKKNAEDEL-------------------KRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvv 1746
Cdd:COG3883 94 ALYRSGGSVSYLdvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1747 eevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1826
Cdd:COG3883 166 ----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|
gi 1389908274 1827 QAEEEAQKKS 1836
Cdd:COG3883 242 AAASAAGAGA 251
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2426-2581 |
1.41e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2426 MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL--AEQRALAEKILKEKMQAIQEATKLKAEAEKL 2503
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRerEELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 2504 QKQKDQAQETAKRLQEDKQQIQQRLdKETEGF-QKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQA 2581
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNEL-YRVAGLtPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1653-1856 |
1.42e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 AELQELRDRAAEAEKLRKAAQDEAERL---RKQVAEETQRKKNAEDELKRKSD---AEKEAAKQKQRALDDLQkYKMQAE 1726
Cdd:COG1340 50 AQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAelnKAGGSIDKLRKEIERLE-WRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 ----EAERR-MKQAE--EEKIRQIRVVEEVAQK-----SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLK 1794
Cdd:COG1340 129 vlspEEEKElVEKIKelEKELEKAKKALEKNEKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 1795 KQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1856
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
213-310 |
1.43e-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: 41.36 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 213 QKKTFTKWVNKHLVK---------AQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 278
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1389908274 279 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 310
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1520-1623 |
1.47e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1520 AQRRLEDDEKAseklkEEERRKMAEIQAELDKQKQ--MAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAE--KQK 1595
Cdd:PTZ00491 684 ERQKMHDKAKA-----EEQRTKLLELQAESAAVESsgQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAEleKLR 758
|
90 100
....*....|....*....|....*...
gi 1389908274 1596 QNIQQELQHLKSLSDQEIKsKNQQLEDA 1623
Cdd:PTZ00491 759 KRQELELEYEQAQNELEIA-KAKELADI 785
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2219-2391 |
1.53e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2219 AKEAAQKCTAAEQKAQDVlskNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAK 2298
Cdd:PRK09510 89 AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2299 QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQ-----KSQVEKELTVVKLQLDETDKQK 2373
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKaaaeaKAAAAKAAAEAKAAAEKAAAAK 245
|
170
....*....|....*...
gi 1389908274 2374 VLLDQELQRVKGEVNDAF 2391
Cdd:PRK09510 246 AAEKAAAAKAAAEVDDLF 263
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1568-1831 |
1.71e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1568 QEALElKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ--EIKSKNQQLEDALVSRRKIEEEihiiriqLEKTt 1645
Cdd:COG2433 379 EEALE-ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQveRLEAEVEELEAELEEKDERIER-------LERE- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1646 AHKAKSEAELQELRDRaaEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1725
Cdd:COG2433 450 LSEARSEERREIRKDR--EISRLDR----EIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEA 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1726 -EEAERRMKQAEeekiRQIRVVEEV--AQKSAATQL---QTKAMSFSEQT-TKLEESLKKEQGNVLKLQE----EADKLk 1794
Cdd:COG2433 524 iRRLEEEYGLKE----GDVVYLRDAsgAGRSTAELLaeaGPRAVIVPGELsEAADEVLFEEGIPVLPAEDvtiqEVDDL- 598
|
250 260 270
....*....|....*....|....*....|....*..
gi 1389908274 1795 kqqkeANTAREEAEQELEIWRQKANEalRLRLQAEEE 1831
Cdd:COG2433 599 -----AVVDEEELEAAIEDWEERAEE--RRREKKAEM 628
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1578-1892 |
1.73e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.67 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1578 KEEASKRQDVAADAEKQKQNIQQEL-----------QHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA 1646
Cdd:pfam04747 14 QQLTNRRKNLGRVAKSQRNQFRQWLltavlpnsindQRKEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1647 HKAKSEAELqelrdRAAEAEKLRKAAQdeaerlrkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlQKYKMQAE 1726
Cdd:pfam04747 94 AKKAAEKEA-----RRAEAEAKKRAAQ-----------EEEHKQWKAEQERIQKEQEKKEADLKKLQA----EKKKEKAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1727 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1806
Cdd:pfam04747 154 KAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1807 AEQELEIWRQKANEALRlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1886
Cdd:pfam04747 234 VEQVVEQPKVVTEEPHQ---QAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQKKNKKDKKKSESEKVVE 310
|
....*.
gi 1389908274 1887 QKLSAE 1892
Cdd:pfam04747 311 EPVQAE 316
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2497-2748 |
1.76e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2497 KAEAeKLQKQKDQAQETAKRLQEDKqqiQQRLDKEtegfqkslEAERKRQLEASAEAeklklRVKELSLAQTKAEDEAKK 2576
Cdd:PRK05035 435 KAEI-RAIEQEKKKAEEAKARFEAR---QARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2577 FKKQADEVKAQLQRTEKHTTEIVVQ--------KLETQRLQSTREADDLKSAIA---------DLEEERKKLKKEAEELQ 2639
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIAArearkaqaRARQAEKQAAAAADPKKAAVAaaiarakakKAAQQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2640 RKSK---EMANAQQEQIEQQKAELQQSfltekglllkrekEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK 2716
Cdd:PRK05035 578 KKAAvaaAIARAKAKKAAQQAASAEPE-------------EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPR 644
|
250 260 270
....*....|....*....|....*....|...
gi 1389908274 2717 LQAIMDEAVR-KQKEAEEEMKNKQREMDVLDKK 2748
Cdd:PRK05035 645 KAAVAAAIARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1737-1988 |
1.80e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 43.66 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1737 EEKIRQIRVVeeVAQKSAATQLQTKAMSFSEQTTklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1816
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIR--EEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1817 KANEALRLRLQAEEEAQKKS--HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQE 1894
Cdd:pfam17045 85 KLQEELSKLKRSYEKLQRKQlkEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1895 CIRLKADF----EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL--QMKINAEKasmvntEKSKQL 1968
Cdd:pfam17045 165 SLIQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGdsNRKLLEEQ------QRLLEE 238
|
250 260
....*....|....*....|
gi 1389908274 1969 LESEALKMKQLADEAARMRS 1988
Cdd:pfam17045 239 LRMSQRQLQVLQNELMELKA 258
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2345-2596 |
1.81e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2345 AEQALQQKSQVEKeltvvkLQLDETDKQKVLLDQELQRvkGEVNDAFKQKSQVEVELAR-VRIQMEELVKLKLKIEEENR 2423
Cdd:PRK11637 39 SAHASDNRDQLKS------IQQDIAAKEKSVRQQQQQR--ASLLAQLKKQEEAISQASRkLRETQNTLNQLNKQIDELNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2424 RL--MQKDKDSTQKLLAEEAEKMKSLAEEAG-RLSVEAEETARQRQIaesnLAEQRALAekilkekmQAIQEA-TKLKAE 2499
Cdd:PRK11637 111 SIakLEQQQAAQERLLAAQLDAAFRQGEHTGlQLILSGEESQRGERI----LAYFGYLN--------QARQETiAELKQT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2500 AEKLQKQKD---QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAerkrqLEASAEAEK---LKLRVKELSLAQT--KAE 2571
Cdd:PRK11637 179 REELAAQKAeleEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTG-----LESSLQKDQqqlSELRANESRLRDSiaRAE 253
|
250 260 270
....*....|....*....|....*....|
gi 1389908274 2572 DEAK----KFKKQADEVKA-QLQRTEKHTT 2596
Cdd:PRK11637 254 REAKaraeREAREAARVRDkQKQAKRKGST 283
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
811-891 |
1.82e-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: 40.76 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 811 WLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTAALQTQWSWLLQL 890
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1389908274 891 C 891
Cdd:pfam00435 96 A 96
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1785-1867 |
1.84e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 42.07 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1785 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLRLQAEEEAQK-----KSHAQEEAEKQKLEAERDAKKRGKA 1859
Cdd:PRK05759 39 KIADGLAAAERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQiieeaKAEAEAEAARIKAQAQAEIEQERKR 115
|
....*...
gi 1389908274 1860 EEAALKQK 1867
Cdd:PRK05759 116 AREELRKQ 123
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1697-2001 |
1.85e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1697 LKRKSDAEKEAAKQ----KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKL 1772
Cdd:COG5185 248 LAQTSDKLEKLVEQntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1773 EESLKKEQGNVLKLQEEADKLKKQQKEA-NTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQK 1846
Cdd:COG5185 328 EESKRETETGIQNLTAEIEQGQESLTENlEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESldeipQNQRGYAQEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1847 LEAERDAKKRGKAE---------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQecirlKADFEHAEQQRGL 1911
Cdd:COG5185 408 LATLEDTLKAADRQieelqrqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAY-----DEINRSVRSKKED 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1912 LDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEA--LKMKQLADEAARMRSV 1989
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLipASELIQASNAKTDGQA 562
|
330
....*....|..
gi 1389908274 1990 AEEAKKQRQIAE 2001
Cdd:COG5185 563 ANLRTAVIDELT 574
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2444-2781 |
1.86e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.29 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2444 MKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEkilkEKMQAIQEATKLKAEAEKLQKQKDQAQ------ETAKRL 2517
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNE----ELTSLAEEAQALKDEMDILRESSDKVKkleatvETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2518 QED----KQQIQQRLDKETEGFQK--SLEAERKRQLEASAEAEKLKLRVKELslaQTKAEDEAKKFKKQADEVKaqlQRT 2591
Cdd:pfam05622 144 LEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK---KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2592 EKHTTeivVQKlETQRLQSTREA-----DDLKSAIADLEEERKKLKkeaeelqrkskeMANAQQEQIEQQKAELQQSFLT 2666
Cdd:pfam05622 218 EKLEA---LQK-EKERLIIERDTlretnEELRCAQLQQAELSQADA------------LLSPSSDPGDNLAAEIMPAEIR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2667 EKGLLLKREKEVEGEKKrfEKQLEDEMKKAKALKDE-QERQRKLMEEERKKLQAIMD--EAVRKQKEAEEEMKNKQREMD 2743
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQ--EGSYRERLTELQQLLEDaNRRKNELETQNRLANQRILElqQQVEELQKALQEQGSKAEDSS 359
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908274 2744 VLDKKRLEQEKQLAE---ENKKLREQLQTFEISSKTVSQTK 2781
Cdd:pfam05622 360 LLKQKLEEHLEKLHEaqsELQKKKEQIEELEPKQDSNLAQK 400
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1720-2044 |
1.97e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERrmKQAEEEKIR----QIRVVEEVAQKSAAtqLQTKAmsfseqttkleESLKKEQGNVLKLQEEADKLKK 1795
Cdd:PRK05035 435 KAEIRAIEQEK--KKAEEAKARfearQARLEREKAAREAR--HKKAA-----------EARAAKDKDAVAAALARVKAKK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1796 QQKEANTArEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAerdAKKRGKAEEAALKQK--ENAEKE 1873
Cdd:PRK05035 500 AAATQPIV-IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAA---AIARAKAKKAAQQAAnaEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1874 LDKQRKFAEQIAqqklsaeqeciRLKAdfEHAEQQrglldnelqrlkNEVNSTEKQRKQLEDELNKVRSEMdsllqmkin 1953
Cdd:PRK05035 576 DPKKAAVAAAIA-----------RAKA--KKAAQQ------------AASAEPEEQVAEVDPKKAAVAAAI--------- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1954 aEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaarqrsEAEKILKEKLAAineatrlkteAE 2033
Cdd:PRK05035 622 -ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE------EAEDPKKAAVAA----------AI 684
|
330
....*....|.
gi 1389908274 2034 MALKAKEAENE 2044
Cdd:PRK05035 685 ARAKAKKAAQQ 695
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
350-410 |
1.98e-03 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 39.98 E-value: 1.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 350 DNFTTSWRDGKLFSAIIHKHRPALIDMNQV--YRQSNQE----NLEQAFSVAERELGVTKL-LDPEDV 410
Cdd:pfam11971 14 EDLLRDLSDGCALAALIHFYCPQLIDLEDIclKESMSLAdslyNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1690-1802 |
1.98e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 41.47 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1690 KKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR-----MKQAEE-EKIRQIRvvEEVAQ-KSAATQLQTKA 1762
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyerelVLHAEDiKALQALR--EELNElKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1389908274 1763 MSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANT 1802
Cdd:pfam07926 81 ESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNE 117
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2119-2580 |
2.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2119 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKA 2198
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2199 EDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlL 2278
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-L 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2279 RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKE 2358
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2359 LTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRI-----QMEELVKLKLKIEEENRRLMQKD-KDS 2432
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLREAEELEEELQLEElEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2433 TQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILkekmqAIQEATKLKAEAEKLQKQKDQAQE 2512
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2513 TAKRLQEDKQQIQQRLdKETEGFQKSLEAERKRQlEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2580
Cdd:COG4717 447 ELEELREELAELEAEL-EQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1588-1929 |
2.03e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1588 AADAEKQKQNIQQELQHL-KSLSDQEikSKNQQLEDALvsrrkieeeihiiriqlekttahkAKSEAELQELRDRAAEAE 1666
Cdd:PRK04863 832 EADPEAELRQLNRRRVELeRALADHE--SQEQQQRSQL------------------------EQAKEGLSALNRLLPRLN 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1667 KL-RKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAK--QKQRALDDLQKYKMQAEEAERRMKQaeeekirQI 1743
Cdd:PRK04863 886 LLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQ-------QA 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1744 RVVEEVAQKSAAtqlqtkaMSFSEQttklEESLKKEQGNVlklqeeaDKLKKQQKEANTAREEAEQELEIWRQKANEALR 1823
Cdd:PRK04863 959 FALTEVVQRRAH-------FSYEDA----AEMLAKNSDLN-------EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1824 LR--LQAEEEAQKKSHAQEEAEKQKL------EAERDAKKRGKAEEAALKQKENAEKELDKQRKFAE---QIAQQKLSAE 1892
Cdd:PRK04863 1021 VLasLKSSYDAKRQMLQELKQELQDLgvpadsGAEERARARRDELHARLSANRSRRNQLEKQLTFCEaemDNLTKKLRKL 1100
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908274 1893 QEciRLKADFEHAEQQRGLLDNELQRLKNevNSTEKQ 1929
Cdd:PRK04863 1101 ER--DYHEMREQVVNAKAGWCAVLRLVKD--NGVERR 1133
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1753-2012 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1753 SAATQLQTKAmsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealrlrlQAEEEA 1832
Cdd:COG3883 13 FADPQIQAKQ----KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1833 QKKSHAQEEAEKQKLEAERDAKKRGKAE------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKA 1900
Cdd:COG3883 75 AEAEAEIEERREELGERARALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAK----KA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1901 DfehAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLA 1980
Cdd:COG3883 151 E---LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|..
gi 1389908274 1981 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 2012
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1785-1877 |
2.15e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.27 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1785 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKshAQEEAEKQKLEAERDAKK-RGKAEEAA 1863
Cdd:cd06503 34 KIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEII-------EEARKE--AEKIKEEILAEAKEEAERiLEQAKAEI 104
|
90
....*....|....
gi 1389908274 1864 LKQKENAEKELDKQ 1877
Cdd:cd06503 105 EQEKEKALAELRKE 118
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2509-2659 |
2.17e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2509 QAQETAKRLQEDKQQIQQRldketegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQL 2588
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKK--------QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2589 QRTEKHTTEIVVQKLETQRLQST-READDLKSaiaDLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2659
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKdHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
215-307 |
2.19e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.16 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 215 KTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 284
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1389908274 285 KLVNIRNDDIADGNpKLTLGLIW 307
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1642-1847 |
2.23e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 43.65 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1642 EKT--TAHKAKSEAELQELRdRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQ 1719
Cdd:pfam15905 116 EKTslSASVASLEKQLLELT-RVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1720 KYKMQAEEAERRMKQAEEEKIRQ----IRVVEEVAQKSAATQlqtKAMSFSEQTTKLEESLKKEQGNVL----KLQEEAD 1791
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEksetEKLLEYITELSCVSE---QVEKYKLDIAQLEELLKEKNDEIEslkqSLEEKEQ 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 1792 KLKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEEEAQKKSHAQEEAEKQKL 1847
Cdd:pfam15905 272 ELSKQIKDLNEKCKLLESEKEELLRE-YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4558-4595 |
2.33e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908274 4558 QRFLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTA 4595
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2328-2791 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEmsKHKKEAEQALQQKSQVEKELTVVKLQLD-------ETDKQKVLLDQELQRVKGEVNDAF-KQKSQVEV 2399
Cdd:pfam12128 331 HGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRSKIKEQNNRDIAGIKDKLaKIREARDR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2400 ELARVRIQMEELvklklkiEEENRRLMQKDKDStqklLAEEAEKMKS-LAEEAGRLS--VEAEETARQRQIAESNLAEQR 2476
Cdd:pfam12128 409 QLAVAEDDLQAL-------ESELREQLEAGKLE----FNEEEYRLKSrLGELKLRLNqaTATPELLLQLENFDERIERAR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2477 ALAEKILKEKMQAIQEATKLKA----EAEKLQKQKDQAQETAKRLQEDKQQIQQR-------LDKETEGFQKSLEAERKR 2545
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKrrdqASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVISP 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2546 QL-----------EASAEAEK----LKLRVKEL----SLAQTKA-EDEAKKFKKQADEVKAQLQRTEKHTTEIVVQkLET 2605
Cdd:pfam12128 558 ELlhrtdldpevwDGSVGGELnlygVKLDLKRIdvpeWAASEEElRERLDKAEEALQSAREKQAAAEEQLVQANGE-LEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2606 QRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKE---MANAQQEQIEQQK-----------AELQQSFLTEKGLL 2671
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErkdSANERLNSLEAQLkqldkkhqawlEEQKEQKREARTEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2672 LKREKEVEGEKKRFEKQLEDEMKKAKALKD------EQERQRKL------------MEEERKKLQAIMDEAVRKQKEAEE 2733
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKaelkalETWYKRDLaslgvdpdviakLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2734 EMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2791
Cdd:pfam12128 797 YFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2670-2784 |
2.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2670 LLLKR--EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKlmeEERKKLQAIMDEAVRKQKE--AEEEMKNKQREmDVL 2745
Cdd:PRK12704 23 FVRKKiaEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNelQKLEKRLLQKE-ENL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908274 2746 DKKRLE---QEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2784
Cdd:PRK12704 99 DRKLELlekREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1099-1682 |
2.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1099 VEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNKANQhyntmvtsaEQGEQDESVCKTYLT-QIKDLRLKLE 1177
Cdd:pfam15921 326 VSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ---------ESGNLDDQLQKLLADlHKREKELSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1178 GCENR-----------TVTRLRQPVDKEPLKACALKtSEQKKVQSELEG-LKRDLTCVSEKTEEV----LMSPQQSSSAP 1241
Cdd:pfam15921 397 KEQNKrlwdrdtgnsiTIDHLRRELDDRNMEVQRLE-ALLKAMKSECQGqMERQMAAIQGKNESLekvsSLTAQLESTKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1242 LLRSELD-LTLKKMeqvyglssvyldklktvdvvirntadaeeTLKNYEARLRDVS-KVPSEQKEVEKHRSQMKSMRSEA 1319
Cdd:pfam15921 476 MLRKVVEeLTAKKM-----------------------------TLESSERTVSDLTaSLQEKERAIEATNAEITKLRSRV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1320 EADQVMFDRLQ---DDLRKATTVHDKMTRIHSERDADLEHYRQlvngllerwqavfaQIELRLRELDLLGRhmnsyrdsy 1396
Cdd:pfam15921 527 DLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQ--------------QIENMTQLVGQHGR--------- 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1397 ewlirwlTEARQRQEKIQavpisdsraLREQLTDEKKLLGEIEKNKDKIDDCHKNAKAyidSVKDYEFQILTYKALQDPI 1476
Cdd:pfam15921 584 -------TAGAMQVEKAQ---------LEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLELEKVKLVNAGSER 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1477 ASPLKKPKMEcaSDDIIQEYVNLRtrySELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQM- 1555
Cdd:pfam15921 645 LRAVKDIKQE--RDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMe 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1556 -AEAHAKSVAKAEQ----------EALELKMKMKEEAskrqdvAADAEKQKQNIQQELQHLkslsdqeikskNQQLEDAL 1624
Cdd:pfam15921 720 gSDGHAMKVAMGMQkqitakrgqiDALQSKIQFLEEA------MTNANKEKHFLKEEKNKL-----------SQELSTVA 782
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 1625 VSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQ 1682
Cdd:pfam15921 783 TEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1670-1860 |
2.72e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1670 KAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKqaeeeKIRQirvveEV 1749
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARKQNKYDELVEE---AKTIKAEIEELTDELLNLVMDIEDPSAALN-----KLNT-----AA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1750 AQKSAATQLQTKAMSFSEQTT---KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL-- 1824
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELkn 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908274 1825 -----------------RLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAE 1860
Cdd:PHA02562 345 kistnkqslitlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2641-2808 |
2.74e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2641 KSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAi 2720
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVR-QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEI- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2721 mdeavrkQKEAEEEMKNKQREMDVLDKKRLEQEKQlaEENKKLREQLQTFEISS---KTVSQTKESQTVSVEKLVAVTTV 2797
Cdd:pfam05262 291 -------KKNDEEALKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEdlqKTKPQVEAQPTSLNEDAIDSSNP 361
|
170
....*....|.
gi 1389908274 2798 GTSKGVLNGST 2808
Cdd:pfam05262 362 VYGLKVVDPIT 372
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2399-2585 |
2.79e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2399 VELARVRIQMEELvKLKLKIE--EENRRLMQKDKDSTQKLLaEEAEKMK-SLAEEAGRLSvEAEETARQRQiaesnlaEQ 2475
Cdd:PRK00409 504 IEEAKKLIGEDKE-KLNELIAslEELERELEQKAEEAEALL-KEAEKLKeELEEKKEKLQ-EEEDKLLEEA-------EK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2476 RAlaEKILKEkmqAIQEATKLKAEAEKLQKQKDQAQeTAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQL-------- 2547
Cdd:PRK00409 574 EA--QQAIKE---AKKEADEIIKELRQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVgdevkyls 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 2548 --------------EASAEAEKLKLRVK--ELSLAQTKAEDEAKKFKKQADEVK 2585
Cdd:PRK00409 648 lgqkgevlsipddkEAIVQAGIMKMKVPlsDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| CH_PARVG_rpt2 |
cd21307 |
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ... |
214-303 |
2.81e-03 |
|
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409156 [Multi-domain] Cd Length: 122 Bit Score: 40.80 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 214 KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKgrmrFH--------KLQNVQIALDFLKHRQVK 285
Cdd:cd21307 18 KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSE----FFltpsstseMLHNVTLALELLKEGGLL 93
|
90
....*....|....*...
gi 1389908274 286 LVNIRNDDIADGNPKLTL 303
Cdd:cd21307 94 NFPVNPEDIVNGDSKATI 111
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
1762-1926 |
2.89e-03 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 43.99 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1762 AMSFS----EQTTKLEESLKKE--QGNVLKLQEEADK----LKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEE- 1830
Cdd:PRK11519 231 SLTYTgedrEQIRDILNSITRNylEQNIERKSEEASKslafLAQQLPEVRSRLDVAENKLNAFRQD-KDSVDLPLEAKAv 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1831 -------EAQKKSHAQEEAEKQKLEAerdakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFE 1903
Cdd:PRK11519 310 ldsmvniDAQLNELTFKEAEISKLYT-----KEHPAYRTLLEKRKALEDEKAKLNGRVTAMPK----TQQEIVRLTRDVE 380
|
170 180
....*....|....*....|...
gi 1389908274 1904 HAEQQRGLLDNELQRLKNEVNST 1926
Cdd:PRK11519 381 SGQQVYMQLLNKQQELKITEAST 403
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1655-1855 |
2.98e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1655 LQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedELKRKSDAEKEAAKQKQRALDDLQKYKmqaeEAERRMKQ 1734
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAA------------LLEAKELLLRERNQQRQEARREREELQ----REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1735 AEEekirqirvveevaqksaatQLQTKAmsfsEQTTKLEEslkkeqgnvlKLQEEADKLKKQQKEANTAREEAEQELE-- 1812
Cdd:PRK12705 89 KEE-------------------QLDARA----EKLDNLEN----------QLEEREKALSARELELEELEKQLDNELYrv 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1389908274 1813 --IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1855
Cdd:PRK12705 136 agLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4453-4484 |
3.07e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908274 4453 IAGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4484
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2429-2616 |
3.16e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.45 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2429 DKDSTQKLLaEEAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKilkekmqAIQEATKLKAEAEKLQKQK 2507
Cdd:pfam05262 179 DKKVVEALR-EDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2508 DQAQETAKRLQEDKQQIQQRLDKETEGFQKSlEAErKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQ 2587
Cdd:pfam05262 251 RQKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIE-KAQIEIKKNDEEAL---KAKDHKAFDLKQESKASEKEAEDKELE 325
|
170 180
....*....|....*....|....*....
gi 1389908274 2588 LQRTEKHTTEIVVQKLETQRLQSTREADD 2616
Cdd:pfam05262 326 AQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1642-1741 |
3.26e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 43.05 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1642 EKTtahKAKSEAELQELRDRAAEAEklRKAAQDEAERLRkQVAEETQRKKNAEDE-LKRKSDAEKEAAKQKQRALDDLQK 1720
Cdd:cd03406 174 EKT---KLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEMHLAREKARADAEY 247
|
90 100
....*....|....*....|.
gi 1389908274 1721 YKMqaeeaerrMKQAEEEKIR 1741
Cdd:cd03406 248 YRA--------LREAEANKLK 260
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2328-2767 |
3.28e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2328 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTvvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEV-----ELA 2402
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHerqakELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2403 RVRIQMEELvklKLKIEEENRRLMQKDkDSTQKLLaeEAEKMKSLAEEAGrlsVEAEETARQRQIAESNLAEQRALAEKI 2482
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLL--EMLQSKGLPKKSG---EEDWERTRRIAEAEMQLGHLEVLLDQK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2483 LKEKMQAiqeatklkaeAEKLQKQKDQAQETAKrlqedKQQIQQRLD-KETegfqKSLEAERK-RQLEASAEAEK----L 2556
Cdd:pfam10174 205 EKENIHL----------REELHRRNQLQPDPAK-----TKALQTVIEmKDT----KISSLERNiRDLEDEVQMLKtnglL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2557 KLRVKELSLAQTKAEDEAKKF-KKQADEVKAQLQRTEkhtTEIVV--QKLET---QRLQSTREADDLKSAIA--DLEEER 2628
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKE---SELLAlqTKLETltnQNSDCKQHIEVLKESLTakEQRAAI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2629 KKLKKEAEELQRKSKE-MANAQQEQIE---QQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2704
Cdd:pfam10174 343 LQTEVDALRLRLEEKEsFLNKKTKQLQdltEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908274 2705 RQRKLMEEERKKLQAI--MDEAVRKQKEAEEEMKnKQREMDvlDKKRLEQEKQLAEENKKLREQL 2767
Cdd:pfam10174 423 RVKSLQTDSSNTDTALttLEEALSEKERIIERLK-EQRERE--DRERLEELESLKKENKDLKEKV 484
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1520-1780 |
3.57e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1520 AQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKqni 1598
Cdd:PRK07735 28 AKHGAEISKLEEEnREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAK--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1599 QQELQHLKSLSDQEIKSknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1678
Cdd:PRK07735 105 AAALAKQKREGTEEVTE-----EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1679 LRKQVAEEtqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1758
Cdd:PRK07735 180 LAKQKAAE------AGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARA 253
|
250 260
....*....|....*....|..
gi 1389908274 1759 QTKAMSFSEQTTKLEESLKKEQ 1780
Cdd:PRK07735 254 KTKGAEGKKEEEPKQEEPSVNQ 275
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2639-2759 |
3.59e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.38 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2639 QRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQrKLMEEERKKLQ 2718
Cdd:pfam13904 67 QRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERK-VSQEEAKEVLQ 145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908274 2719 AIMDEAVRKQKEAEEEMKNKQREmdvldKKRLEQE-KQLAEE 2759
Cdd:pfam13904 146 EWERKKLEQQQRKREEEQREQLK-----KEEEEQErKQLAEK 182
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1995-2141 |
3.69e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1995 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRK------------LLED 2062
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKeeqldaraekldNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2063 Q---AAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK--KVVEEEIHIIKINFHKASKEKADLESELKKLKGIADE 2137
Cdd:PRK12705 106 QleeREKALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
....
gi 1389908274 2138 TQKS 2141
Cdd:PRK12705 186 MQRI 189
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2600-2767 |
3.89e-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: 42.22 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2600 VQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmANAQQEQIEQQKAELQQSFLTEKGLLLK----RE 2675
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2676 -----KEVEGEKKRfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEavrKQKEAEEEMKNKQREMDVLDKKRL 2750
Cdd:COG1579 91 yealqKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
170
....*....|....*..
gi 1389908274 2751 EQEKQLAEENKKLREQL 2767
Cdd:COG1579 167 ELAAKIPPELLALYERI 183
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2440-2593 |
3.94e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2440 EAEKMKSLAE---EAGRLSVEAEETARQrQIAESN--LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQK------D 2508
Cdd:COG2268 187 DALGRRKIAEiirDARIAEAEAERETEI-AIAQANreAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaraeaE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2509 QA---QETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQ---LEASAEAEKLKLRVKEL-----SLAQTKAEDEAKKF 2577
Cdd:COG2268 266 AAyeiAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadVRKPAEAEKQAAEAEAEaeaeaIRAKGLAEAEGKRA 345
|
170
....*....|....*.
gi 1389908274 2578 KKQADEVKAQLQRTEK 2593
Cdd:COG2268 346 LAEAWNKLGDAAILLM 361
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2438-2704 |
4.18e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2438 AEEAEKMKslAEEAgRLSVEAEEtARQRQIAESNLAEQRALAEKILKEKMQAIQEA-----TKLKAEAEKLQKQKDQAQE 2512
Cdd:PRK05035 440 AIEQEKKK--AEEA-KARFEARQ-ARLEREKAAREARHKKAAEARAAKDKDAVAAAlarvkAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2513 TAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTE 2592
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2593 KHTTEIVVQKLETqrlqstrEADDLKSAIAdleeerkkLKKEAEELQRKSKEMANAQQEQIEQQKAELQ------QSFLT 2666
Cdd:PRK05035 596 QQAASAEPEEQVA-------EVDPKKAAVA--------AAIARAKAKKAEQQANAEPEEPVDPRKAAVAaaiaraKARKA 660
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908274 2667 EKGLLLKREKEVEGEKKrfeKQLEDEMKKAKALKDEQE 2704
Cdd:PRK05035 661 AQQQANAEPEEAEDPKK---AAVAAAIARAKAKKAAQQ 695
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2220-2602 |
4.35e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2220 KEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKaekeaallrqKAEEAEKQKKAAENEAAKQ 2299
Cdd:pfam04747 52 KEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEA----------RRAEAEAKKRAAQEEEHKQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2300 AKAqndtEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDET---------- 2369
Cdd:pfam04747 122 WKA----EQERIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSaapapepktp 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2370 DKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAE 2449
Cdd:pfam04747 198 TNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2450 EAGRLSVEAEETARQRQiAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKL---------QKQKDQAQET-AKRLQE 2519
Cdd:pfam04747 277 TPVEPVVETTPPASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfldfvtakEEPKDEPAETpAAPVEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2520 DKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2599
Cdd:pfam04747 356 VVENVVENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKA 435
|
...
gi 1389908274 2600 VQK 2602
Cdd:pfam04747 436 VEE 438
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1666-1843 |
4.38e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1666 EKLRKAAQDEAERLRkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRV 1745
Cdd:pfam05262 184 EALREDNEKGVNFRR----DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1746 VEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEE-ADKLKKQQKEANTAREEAEQELEIWRQKANEALRl 1824
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHkAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1389908274 1825 RLQAEEEAQKKSHAQEEAE 1843
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4175-4206 |
5.02e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.02e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908274 4175 KLVSAERAVTGYKDPYSGKVISLFQAMKKGLI 4206
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1243-1720 |
5.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1243 LRSELDLTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEETLKNYEARLRDV-SKVPSEQKEVEKHRS-QMKSMRSEAE 1320
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAeSDLSMELEKNNYYKElEERHMKIIND 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1321 ADQVMFDRLQDDLRKATTVHDKmTRIHSERDADLEHYRQLVNGL---------LERWQAVFAQIELRLRELDLLGRHMNS 1391
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHAIIKKLsvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1392 YRDSYEWLIRWLTEARQRQEKIQAvPISDSRALREQLTDE-KKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYK 1470
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSA-FISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1471 A-LQDPIASPLKKPKM-ECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEK--ASEKLKE--EERRKMAE 1544
Cdd:PRK01156 447 EmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEylESEEINKsiNEYNKIES 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1545 IQAEL----DKQKQMAEAHAKSVAKAEQ------EALELK-------------------MKMKEEASKRQDvaaDAEKQK 1595
Cdd:PRK01156 527 ARADLedikIKINELKDKHDKYEEIKNRykslklEDLDSKrtswlnalavislidietnRSRSNEIKKQLN---DLESRL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1596 QNIQQELQHLKSLSDQEIKSKNQQLeDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEA---------- 1665
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEA-NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEItsrindiedn 682
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908274 1666 -EKLRKAAQD-EAERLRKQVAEETQRKKNAEDElKRKSDAEK--EAAKQKQRALDDLQK 1720
Cdd:PRK01156 683 lKKSRKALDDaKANRARLESTIEILRTRINELS-DRINDINEtlESMKKIKKAIGDLKR 740
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1980-2310 |
5.31e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1980 ADEAARMRSVAEEAKKQRQIAEEEAARQRSE----AEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY 2055
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTEsvepNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2056 QR-KLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEEtlkQKKVVEEEIHIIKINFHKASKEKADLESElkklkgi 2134
Cdd:pfam02029 84 ERqKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR---LGRYKEEETEIREKEYQENKWSTEVRQAE------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2135 aDETQKSKLKAEEEAEKLKklaaeeerrRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEK 2214
Cdd:pfam02029 154 -EEGEEEEDKSEEAEEVPT---------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2215 QVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL--AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAA 2292
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRrrRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE 303
|
330
....*....|....*...
gi 1389908274 2293 EneaaKQAKAQNDTEKQR 2310
Cdd:pfam02029 304 E----AERKLREEEEKRR 317
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1793-1922 |
5.45e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.09 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1793 LKKQQKEANTAREEAEQELeiwrQKANEALrlrlqaEEEAQKKSHAQEEAEKQKLEAERDAK-------KRGKAEEAALK 1865
Cdd:PRK07352 48 LEERREAILQALKEAEERL----RQAAQAL------AEAQQKLAQAQQEAERIRADAKARAEairaeieKQAIEDMARLK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908274 1866 QKENAEKELDKQRKFAE---QIAQQKLS-AEQEcirLKADFEHAEQQRgLLDNELQRLKNE 1922
Cdd:PRK07352 118 QTAAADLSAEQERVIAQlrrEAAELAIAkAESQ---LPGRLDEDAQQR-LIDRSIANLGGN 174
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2675-2742 |
5.47e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 5.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908274 2675 EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK----LQAIMDEAVRKQKEAEEEMKNKQREM 2742
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEkeqeLQKKEQELQQLQQKAQQELQKKQQEL 92
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1792-2056 |
5.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1792 KLKKQQKEANTAREEAEQEL----EIWRQKANEALRLRLQAE--EEAQKKSHA-----QEEAEKQKLEAERDAKKRGKAE 1860
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLrknlTVEPVKGSNVIEISYTSPdpELAAAVANAlaeayLEQNLELRREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1861 EAALKQK-ENAEKELDKQRK---------FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1930
Cdd:COG3206 184 LPELRKElEEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1931 --KQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLEsealkmKQLADEAARmrsVAEEAKKQRQIAEEEAARQR 2008
Cdd:COG3206 264 viQQLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALR------AQLQQEAQR---ILASLEAELEALQAREASLQ 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2009 SEAEKiLKEKLAAINEatrlkteaemalkaKEAENERLKRQAE--EEAYQ 2056
Cdd:COG3206 334 AQLAQ-LEARLAELPE--------------LEAELRRLEREVEvaRELYE 368
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2407-2510 |
6.09e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2407 QMEElVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRALAE---- 2480
Cdd:cd03406 170 AMEA-EKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEieDEMHLAREKARADaeyy 248
|
90 100 110
....*....|....*....|....*....|
gi 1389908274 2481 KILKEKmqaiqEATKLKAEAEKLQKQKDQA 2510
Cdd:cd03406 249 RALREA-----EANKLKLTPEYLELKKYQA 273
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
206-317 |
6.11e-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: 39.96 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 206 ADERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 281
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1389908274 282 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 317
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1541-1720 |
6.22e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1541 KMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkEEASKRQDVAADAEKQKQNIQQELQHLKSLsdqeIKSKNQQL 1620
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1621 EDALVSRrkieeeihiIRIQLEKttahkakseaELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRK 1700
Cdd:COG1579 83 GNVRNNK---------EYEALQK----------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180
....*....|....*....|
gi 1389908274 1701 SDAEKEAAKQKQRALDDLQK 1720
Cdd:COG1579 144 KAELDEELAELEAELEELEA 163
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1824-2199 |
6.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1824 LRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlkadFE 1903
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ-------LQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1904 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvnTEKSKQLLESEALKMKQLADEA 1983
Cdd:COG4372 91 AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL--------------EAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1984 ARMRSVAEEAKKQRQiaeEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQ 2063
Cdd:COG4372 157 EQLESLQEELAALEQ---ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2064 AAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 2143
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908274 2144 KAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2199
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1754-1886 |
6.53e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1754 AATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAR-EEAEQELEIWRQKANEalrlrLQAEEEA 1832
Cdd:COG0542 398 AAARVRMEIDSKPEELDELERRLEQ-------LEIEKEALKKEQDEASFERlAELRDELAELEEELEA-----LKARWEA 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1389908274 1833 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1886
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1927-2079 |
6.54e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1927 EKQRKQLEDELNKVRSEMD-SLLQMKINAEKASMVNTEKSKQLLESEALKMK-QLADEAA-RMRSVAEEAKKQRQIAEEE 2003
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQIDADKAQQKaDFAQDNAdKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2004 AARQRSEAEKILKEKLAAINEATRLKTE--AEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIEEKITQLQ 2079
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQESKA---SEKEAEDKELEAQKKREPVAEDLQ 338
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2376-2608 |
6.88e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2376 LDQELQRVKGEVNDAFKQKSQVEVELARVRIQ-----MEELVKLkLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEE 2450
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEAEEKNEeiqerIDQLYDI-LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2451 AGRLS----VEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQI-- 2524
Cdd:PRK04778 333 IDRVKqsytLNESELESVRQL-EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLrk 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2525 -QQRLDKETEGFQKSLEaERKRQLEASA-----EAEKLKLRVKELSLAQTKAEDEAKKF-----KKQADEVKAQLQRTEK 2593
Cdd:PRK04778 412 dELEAREKLERYRNKLH-EIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEEKPInmeavNRLLEEATEDVETLEE 490
|
250
....*....|....*
gi 1389908274 2594 HTTEIVVQKLETQRL 2608
Cdd:PRK04778 491 ETEELVENATLTEQL 505
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2329-2575 |
7.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2329 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2408
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2409 EELvklklkieEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQ 2488
Cdd:COG4372 132 KQL--------EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2489 AIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2568
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
....*..
gi 1389908274 2569 KAEDEAK 2575
Cdd:COG4372 284 ELEALEE 290
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1648-2057 |
7.29e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 42.37 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1648 KAKSEAELQELRDRAAEAEKLRKAAQDEAER---LRKQV---AEETQRKKNAEDELKRKS-DAEKEAAKQKQR------- 1713
Cdd:pfam05622 30 KNSLQQENKKLQERLDQLESGDDSGTPGGKKyllLQKQLeqlQEENFRLETARDDYRIKCeELEKEVLELQHRneeltsl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1714 ----------------ALDDLQKYKMQAEEAERRMKQAEEEKiRQIRVVEEvaqksaatqlqtKAMSFSEQTTKLEESLK 1777
Cdd:pfam05622 110 aeeaqalkdemdilreSSDKVKKLEATVETYKKKLEDLGDLR-RQVKLLEE------------RNAEYMQRTLQLEEELK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1778 KeqGNVLKLQEEAdkLKKQQKEANTAREEAEQELEIWRQKANealrlRLQAEEEAQKKshaqeeaEKQKLEAERDAKKRG 1857
Cdd:pfam05622 177 K--ANALRGQLET--YKRQVQELHGKLSEESKKADKLEFEYK-----KLEEKLEALQK-------EKERLIIERDTLRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1858 KAE----EAALKQKENAEKELDKQRKFAEQIAQQKLSAE--QECIRLKADFEH-AEQQRGLLDNELQRLKNEVNSTEKQR 1930
Cdd:pfam05622 241 NEElrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRLQHENKMlRLGQEGSYRERLTELQQLLEDANRRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1931 KQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSkqllESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRS 2009
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEELQKALQEQGSKA----EDSSLLKQKLEEHLEKLHEAQSElQKKKEQIEELEPKQDSN 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1389908274 2010 EAEKIlkeklaaineatrlkTEAEMALKAKEAENerlkrQAEEEAYQR 2057
Cdd:pfam05622 397 LAQKI---------------DELQEALRKKDEDM-----KAMEERYKK 424
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1574-1863 |
7.89e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.33 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1574 KMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEA 1653
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1654 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMK 1733
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1734 QAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEI 1813
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1814 WRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAA 1863
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1640-1720 |
8.03e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 39.99 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1640 QLEKTTAHKAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQRKKNAedelkRKSDAEKEAAKQKQRALDDLQ 1719
Cdd:PRK07353 51 RLAEAEKLEAQYEQQLASAR---KQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLE 122
|
.
gi 1389908274 1720 K 1720
Cdd:PRK07353 123 Q 123
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
2010-2149 |
8.14e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 42.35 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2010 EAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKrqaeeeayqrkllEDQAAQHKQDIEEKITQLQTSSDSELGRQ 2089
Cdd:TIGR00422 721 EAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYT-------------EAETAERLKLNAVDIKGAINFSEVEVVIE 787
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2090 KNIVEETLkQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGiadETQKSKLKAEEEA 2149
Cdd:TIGR00422 788 KPEVTEAV-VELVPGFEIIIPVKGLINKAKELARLQKQLDKEKK---EVIRIEGKLENEG 843
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1794-2073 |
8.31e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1794 KKQQKEANTAREEAEQELEIwrqkanealrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQ---KENA 1870
Cdd:pfam15905 63 KKSQKNLKESKDQKELEKEI----------RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAsleKQLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1871 E----KELDKQrKFAEQIAQQKLSAeqecirlkadfehaeqqrglLDNELQRLKNEVNSTEK----QRKQLEDELNKVRS 1942
Cdd:pfam15905 133 EltrvNELLKA-KFSEDGTQKKMSS--------------------LSMELMKLRNKLEAKMKevmaKQEGMEGKLQVTQK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1943 EMDSlLQMKINAEKASMVNTEKSKQlleSEALKMKQLADEAARMRSVAEEAKKQR---QIAEEEAARQRSEAEKILKEKL 2019
Cdd:pfam15905 192 NLEH-SKGKVAQLEEKLVSTEKEKI---EEKSETEKLLEYITELSCVSEQVEKYKldiAQLEELLKEKNDEIESLKQSLE 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908274 2020 AAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRK----LLEDQAAQHKQDIEE 2073
Cdd:pfam15905 268 EKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNaeleELKEKLTLEEQEHQK 325
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4596-4633 |
8.46e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 8.46e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908274 4596 QKLRDVSAYSKYLTCPKTKLKISYKDAMERSMTEEGTG 4633
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1499-1833 |
9.33e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1499 LRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmKMK 1578
Cdd:pfam07888 78 LESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-RMK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1579 EEASK----RQDVAADAEKQKQNIQQELQHLKSLSD--QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSE 1652
Cdd:pfam07888 157 ERAKKagaqRKEEEAERKQLQAKLQQTEEELRSLSKefQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1653 AELQELRDRAAEAEK--------------LRKAAQDEAERLRKQVAEETQRKKNAEDELKR-KSDAEKEAAKQKQRALDD 1717
Cdd:pfam07888 237 EELRSLQERLNASERkveglgeelssmaaQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEAD 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1718 LQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQtkamsfseqttkLEESLKKeqgnvlkLQEEADKLKKQQ 1797
Cdd:pfam07888 317 KDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQ------------LSESRRE-------LQELKASLRVAQ 377
|
330 340 350
....*....|....*....|....*....|....*.
gi 1389908274 1798 KEANTAREEAEQELEIWRQkaneaLRLRLQAEEEAQ 1833
Cdd:pfam07888 378 KEKEQLQAEKQELLEYIRQ-----LEQRLETVADAK 408
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1846-2081 |
9.33e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1846 KLEAERDAKKRGKAEEAALKQkenaekeLDKQRKFAEQIAQQKLSAEQEcirlkadfEHAEQQRGLLDNELQRLKNEVns 1925
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRR-------LEVERKRREQEEQRRLQQEQL--------ERAEKMREELELEQQRRFEEI-- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1926 teKQRKQ-LEDElnkvrsemdsllqmkinaekasmvntekskQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEA 2004
Cdd:pfam15709 390 --RLRKQrLEEE------------------------------RQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQR 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 2005 ARQRSEAEKILKEKLAAINEATRLKTE----AEMAlKAKEAENERLKRQAEE----EAYQRKLLEDQAAQHKQDIEEKIT 2076
Cdd:pfam15709 438 KKQQEEAERAEAEKQRQKELEMQLAEEqkrlMEMA-EEERLEYQRQKQEAEEkarlEAEERRQKEEEAARLALEEAMKQA 516
|
....*
gi 1389908274 2077 QLQTS 2081
Cdd:pfam15709 517 QEQAR 521
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1823-2017 |
9.85e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1823 RLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKEldKQRKFAEQIAQQKLSAEQECIRLKAdf 1902
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRERE--ELQREEERLVQKEEQLDARAEKLDN-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908274 1903 ehaeqqrglldnelqrLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmkinaEKASMVNTEKSKQLLesealkmKQLADE 1982
Cdd:PRK12705 103 ----------------LENQLEEREKALSARELELEELEKQLDNELY-----RVAGLTPEQARKLLL-------KLLDAE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908274 1983 aarmrsvAEEAKKQR--QIAEEEAARQRSEAEKILKE 2017
Cdd:PRK12705 155 -------LEEEKAQRvkKIEEEADLEAERKAQNILAQ 184
|
|
| |
