|
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 ... |
199-303 |
3.85e-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: 245.39 E-value: 3.85e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 199 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 278
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1655220517 279 RNDDIADGNPKLTLGLIWTIILHFQ 303
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
196-314 |
5.12e-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: 239.93 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 196 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 275
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220517 276 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 314
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
188-312 |
2.63e-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: 232.57 E-value: 2.63e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 188 ERAVIRIADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDF 267
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1655220517 268 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 312
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
316-421 |
7.14e-66 |
|
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: 219.12 E-value: 7.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1655220517 396 PEDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
317-421 |
4.42e-64 |
|
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: 213.79 E-value: 4.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
196-313 |
3.51e-62 |
|
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: 209.12 E-value: 3.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 196 DERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 275
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220517 276 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 313
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
317-421 |
2.25e-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: 2.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLLDP 396
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
315-421 |
4.12e-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: 176.77 E-value: 4.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 315 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAEReLGVTRLL 394
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1655220517 395 DPEDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
201-304 |
5.34e-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: 173.72 E-value: 5.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 279
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1655220517 280 NDDIADGNPKLTLGLIWTIILHFQI 304
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 ... |
188-300 |
1.15e-49 |
|
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: 173.32 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 265
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 266 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
317-417 |
5.75e-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: 162.20 E-value: 5.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
188-300 |
2.21e-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: 160.92 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 265
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 266 DFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21193 82 AFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
197-304 |
1.18e-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: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 272
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 273 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 304
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 ... |
317-417 |
5.83e-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: 156.40 E-value: 5.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
194-300 |
1.42e-42 |
|
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: 153.64 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 194 IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQ 272
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1655220517 273 VKLVNIRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
195-417 |
2.42e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 167.43 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 195 ADERDRVQKKTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 271
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 272 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGKL 350
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 351 FNAIIHKHRPALLDMSQVYRQSNQE--NLEQAFSVAERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 417
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
188-300 |
1.22e-41 |
|
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: 150.97 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 265
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 266 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
197-304 |
3.07e-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: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 272
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 273 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1925-2794 |
8.09e-40 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 164.93 E-value: 8.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 EMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSV--------AEEAKKQRQLAEDEAARQRAEAEKI 1996
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedarkAEEARKAEDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1997 ---LKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2073
Cdd:PTZ00121 1167 eeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2074 IVEETLRQKKVVEEEI-HIIRINFERASKEKSDLEvELKKlkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKV 2152
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMaHFARRQAAIKAEEARKAD-ELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2153 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2232
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2233 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEE---AEKLKKAAEdEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAA 2309
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEA-KKKAEEkkkADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdEELQRVKAqvndavKQKAQvENELSKVKMQ 2389
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAEEAKKKADEAKKA---------AEAKKKA---DEAKKAEE------AKKAD-EAKKAEEAKK 1535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2390 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKmkslAEEAARLSVEAEETARQrkTAEAELAEQRALAEKMLKEKM 2469
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKA 1609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2470 QAIQEATKLKAEAEELQKQknqaqEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2549
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKA-----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2550 AKAEEEATRFKKQADEAKvRLQETEKQTTEtvvqklETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETA 2628
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAK-KAEELKKKEAE------EKKKAEELKKAEEENKIKAEeAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2629 SAQQEQMEQQKAmlQQTFLTEKELLLKRERDVEDEKKKLQ--KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2706
Cdd:PTZ00121 1758 KIAHLKKEEEKK--AEEIRKEKEAVIEEELDEEDEKRRMEvdKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2707 V-------------------KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREklESLEVTSKQAASKTKEIE 2767
Cdd:PTZ00121 1836 AdsknmqleeadafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK--DDIEREIPNNNMAGKNND 1913
|
890 900
....*....|....*....|....*..
gi 1655220517 2768 VQTDKVPEEQLVSMTTVETTKKVFNGS 2794
Cdd:PTZ00121 1914 IIDDKLDKDEYIKRDAEETREEIIKIS 1940
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
317-417 |
3.16e-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: 143.22 E-value: 3.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
316-421 |
3.96e-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: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1655220517 396 PEDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1058-1135 |
8.15e-39 |
|
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: 140.43 E-value: 8.15e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1058 LSWQYLMRDIHMIKTWNITMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNRANQHYNTMVSS 1135
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
304-417 |
8.65e-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: 142.12 E-value: 8.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 304 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 383
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 384 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
199-300 |
1.92e-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: 140.60 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 199 DRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 277
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1655220517 278 IRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
201-302 |
2.28e-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: 2.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 278
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1655220517 279 RNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
197-304 |
4.88e-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: 139.58 E-value: 4.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKHLMKAQ--RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 274
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1655220517 275 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
316-417 |
4.65e-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: 136.92 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1655220517 396 PEDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
313-417 |
6.77e-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: 136.73 E-value: 6.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 313 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 392
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1655220517 393 LLDPEDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
320-421 |
1.04e-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: 135.63 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220517 399 VDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
196-304 |
9.52e-36 |
|
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: 9.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 196 DERDRVQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 274
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1655220517 275 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1937-2740 |
3.31e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 149.52 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1937 EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2013
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2014 AEVALKAKEAENERLKRQAED--EAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihi 2091
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--- 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2092 irinfERASKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2171
Cdd:PTZ00121 1243 -----KKAEEERNNEEIRKFEEARMAHFARR---------------QAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2172 EVERLKQKAAEANKLKDKAEKelekqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKE 2251
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKK--------AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2252 KAEKEAALLRQKAEE---AEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAE 2328
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAA--------------------KKKADEAKKKAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2329 QAlKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAqvnDAVKQKAQVenelskvKMQMDELlklKVRIEEENLRLM 2408
Cdd:PTZ00121 1435 EA-KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEE-------AKKADEA---KKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2409 QKNKDNTQKLLAEEAEKmkslAEEAaRLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQ 2488
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2489 KNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE----AEKLKLRVKELSSAQAKAEEEATRFKKQ 2562
Cdd:PTZ00121 1576 KNMALRKAEEAkkAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2563 ADEAKVRLQETEKQTTEtvvqkletqrlqSTREADDLKKAIAELEKEREKLKRDAQElqnKSKETASAQQEQMEQQKAml 2642
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE------------DKKKAEEAKKAEEDEKKAAEALKKEAEE---AKKAEELKKKEAEEKKKA-- 1718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2643 qqtfltekELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQqrqqklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2722
Cdd:PTZ00121 1719 --------EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
810 820
....*....|....*....|
gi 1655220517 2723 E--MEALEKKRLEQEKLLAD 2740
Cdd:PTZ00121 1783 EelDEEDEKRRMEVDKKIKD 1802
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
188-300 |
1.51e-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: 131.32 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 188 ERAVIR-IADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 265
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 266 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 300
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
301-417 |
1.67e-34 |
|
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: 130.17 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 301 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQA 380
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220517 381 FSVAERELGVTRLLDPEDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
316-414 |
3.34e-34 |
|
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: 128.70 E-value: 3.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1655220517 396 PEDVDVAHPDEKSIITYVS 414
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
317-417 |
6.72e-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: 127.91 E-value: 6.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLY 417
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
200-305 |
7.25e-33 |
|
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: 125.26 E-value: 7.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 276
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
320-422 |
9.88e-33 |
|
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: 124.66 E-value: 9.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVAERELGVTRLLDPE 397
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1655220517 398 DVDVAHPDEKSIITYVSSLYDVMPR 422
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1658-2701 |
1.31e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.05 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1658 EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1737
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1738 aatqlqamsfseKTTKLEESLKKEQGtvlqlQEEAEKLRKQeEEANKAREQaeKELETWRlKANEALRLRL-RAEEEAQR 1816
Cdd:PTZ00121 1107 ------------ETGKAEEARKAEEA-----KKKAEDARKA-EEARKAEDA--RKAEEAR-KAEDAKRVEIaRKAEDARK 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1817 KSLAQEEAEKQKTEAERdaKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfEHAEQQRGLldN 1896
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAAR--KAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA--------KKAEAVKKA--E 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1897 ELQRLKNEVNAAEKQRRQLE-DELAKVRSEMDALLQMKIQAEKvsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 1975
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEE-----ARKADELKKAEEKKKADEAKKAEEKKKADEAK 1308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1976 KKQRQLAEDEAARQRAEAEKilkeklaaiNEATRLKTEAEVALKAKEAenerlkRQAEDEAYQRKLledQAAQHKHDIQE 2055
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAK---------KKADAAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAE 1370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2056 KITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinferasKEKSDlevELKKL---KGIADETQKskakaeeeae 2132
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEED------------KKKAD---ELKKAaaaKKKADEAKK---------- 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 klkklaaeeerkrreAEEKVKKIAAAEEEAARQRKAaqdevERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAE 2212
Cdd:PTZ00121 1426 ---------------KAEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKAEEAKKKAEEAK---KADEAKKKAEEA 1482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2213 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2292
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE----------AKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2293 KEAEAEAAKRAAAEAAalKQKQEADAEMAKHKKEaeqALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKA-QVND 2371
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEE--AKKAEEDKNMALRKAE---EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeELKK 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2372 AVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQ-KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTA 2450
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2451 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnqaqEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLE 2530
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA----EEAKKDEEEKKKIAHLKKEE----EKKAEEIRKEKEA 1779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2531 ISAEaeklklrvkELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKER 2610
Cdd:PTZ00121 1780 VIEE---------ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLEEADAF 1849
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2611 EKLKRDAQELQNKSKETASaqqeqmeqqkamlqqTFLTEKELLLKRERDVE--DEKKKLQKH-LEDEV-NKAKALKDEQQ 2686
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEA---------------DFNKEKDLKEDDEEEIEeaDEIEKIDKDdIEREIpNNNMAGKNNDI 1914
|
1050
....*....|....*
gi 1655220517 2687 RQQKLMDEEKKKLQA 2701
Cdd:PTZ00121 1915 IDDKLDKDEYIKRDA 1929
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1648-2623 |
1.44e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 141.05 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1648 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEE-EKVRQ 1726
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEaRKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1727 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRLKANEAL 1804
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1805 RLRLRAEEEAQRKSlaqEEAEKQKTEAERDAKkkakaeeaalkqkenaEKELEKQRTFAEqiaqqklsaeqeyirlkADF 1884
Cdd:PTZ00121 1219 KAEDAKKAEAVKKA---EEAKKDAEEAKKAEE----------------ERNNEEIRKFEE-----------------ARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1885 EHAEQQRGLLDNELQRLKNEVNAAEKQRRQleDELAKvrsemdallqmkiqAEKVSQSNTEKSKQLLETEALKMKQLAEE 1964
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKK--------------AEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1965 AAR----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAEDEAYQ 2038
Cdd:PTZ00121 1327 AKKkadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKK 1406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2039 RKLLEDQAAQHKhdiqekitqlqssSVSELDRQKNIVEETLRQKKVVEEeihiirinferasKEKSDlevELKKLkgiAD 2118
Cdd:PTZ00121 1407 ADELKKAAAAKK-------------KADEAKKKAEEKKKADEAKKKAEE-------------AKKAD---EAKKK---AE 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2119 ETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEverlKQKAAEANKLKDKAEKELEKQV 2198
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA----KKKADEAKKAEEAKKADEAKKA 1530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2199 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRdeFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEA 2278
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK--AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2279 AKQAKaqKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKAlm 2358
Cdd:PTZ00121 1609 AEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA-------KKAEEDKKKA-- 1677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2359 dEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellKLKVRIEEENLRLMQKNKDNTQKLLaeEAEKMKSLAEEAARLSV 2438
Cdd:PTZ00121 1678 -EEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAE 1747
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2439 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKlkaeaEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ 2518
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2519 KSLEAE----------RKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETeKQTTETVVQKLETQ 2588
Cdd:PTZ00121 1823 DSKEMEdsaikevadsKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-DEIEKIDKDDIERE 1901
|
970 980 990
....*....|....*....|....*....|....*
gi 1655220517 2589 RLQSTREADDLKKAIAELEKErEKLKRDAQELQNK 2623
Cdd:PTZ00121 1902 IPNNNMAGKNNDIIDDKLDKD-EYIKRDAEETREE 1935
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
316-414 |
1.79e-32 |
|
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: 123.79 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1655220517 396 PEDVDVAHPDEKSIITYVS 414
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
304-417 |
7.70e-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: 122.25 E-value: 7.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 304 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 383
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 384 AERELGVTRLLDPEDV-DVAHPDEKSIITYVSSLY 417
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1566-2114 |
9.51e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 137.38 E-value: 9.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1566 SQRQGLAVDAEKQK--QNIQLELTQLknlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLR 1643
Cdd:COG1196 200 RQLEPLERQAEKAEryRELKEELKEL------EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1723
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1724 VRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR--LKAN 1801
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeaLAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1802 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1881
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1882 ADFEHAEQQRGLLDNELQ---------------RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQM-KIQAEKVSQSNTE 1945
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGveaayeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1946 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA----EAEKILKEKLAAINEATRLKTEAEVALKAK 2021
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlaGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2022 EAENERLKRQAEDEAYQ------RKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRIN 2095
Cdd:COG1196 674 LLEAEAELEELAERLAEeeleleEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEAL 753
|
570 580
....*....|....*....|
gi 1655220517 2096 FERASKEK-SDLEVELKKLK 2114
Cdd:COG1196 754 EELPEPPDlEELERELERLE 773
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1515-2728 |
1.26e-31 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 137.26 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1515 SEKLKEDEKKRMAEIQAQleTQKQLAEgHAKSVAK--AELEAqelklkmkEDASQRQGLAVDAEKQKQNIQLELT----- 1587
Cdd:NF041483 85 ADQLRADAERELRDARAQ--TQRILQE-HAEHQARlqAELHT--------EAVQRRQQLDQELAERRQTVESHVNenvaw 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1588 --QLKNLSEQEIRsknQQLEEaqvSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQKlrdqaAEAEKVRKAAQEEAER 1662
Cdd:NF041483 154 aeQLRARTESQAR---RLLDE---SRAEAEQALAAARAEaerLAEEARQRLGSEAESAR-----AEAEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1663 LRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQ-AE--------EAERRLKQAEEEKVRQIKVVEEV 1733
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQeAEealrearaEAEKVVAEAKEAAAKQLASAESA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 -AQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQ-LQEEAEKLRKqeEEANKAREQAEKELETWRLK-ANEALRLRLRA 1810
Cdd:NF041483 303 nEQRTRTAKEEIARLVGEATKEAEALKAEAEQALAdARAEAEKLVA--EAAEKARTVAAEDTAAQLAKaARTAEEVLTKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 EEEAQRKS-LAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ---RTFAEQIAQQKLSAEQEYIRLKADFEh 1886
Cdd:NF041483 381 SEDAKATTrAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTKEyraKTVELQEEARRLRGEAEQLRAEAVAE- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1887 AEQQRGlldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ-MKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1965
Cdd:NF041483 460 GERIRG------EARREAVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTLRRQAEETLERTRAEA 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1966 ARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLA-AINEATRLKTEAEVALKAKE-------AENERLKRQAEDEA 2036
Cdd:NF041483 534 ERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealadarAEAERIRREAAEET 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2037 YQrklLEDQAAqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIhiirinferASKEKSDLEVELKKLKGI 2116
Cdd:NF041483 614 ER---LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENV---------AVRLRSEAAAEAERLKSE 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2117 ADETqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA----AEANKLKDKAEK 2192
Cdd:NF041483 675 AQES-ADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSeellASARKRVEEAQA 753
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2193 ELEKqviLAKEAAQKST----AAEQKAQDVlsknkedllsqeklRDEFENAKKLAQAAETAkekaekeaalLRQKAEE-A 2267
Cdd:NF041483 754 EAQR---LVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAEEEIAG----------LRSAAEHaA 806
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2268 EKLKKAAEDEA--------AKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKqkqEADAEMAKHKKEAEQaLKQKSQVEK 2339
Cdd:NF041483 807 ERTRTEAQEEAdrvrsdayAERERASEDANRLRREAQEETEAAKALAERTVS---EAIAEAERLRSDASE-YAQRVRTEA 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2340 ELGLVKLQLDETdKQKALMDEELQRVK----AQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLR--------- 2406
Cdd:NF041483 883 SDTLASAEQDAA-RTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRadaaaqaeq 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2407 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEET-ARQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEE 2484
Cdd:NF041483 962 LIAEATGEAERLRAEAAETVGSAQQHAERIRTEAERVkAEAAAEAERLRTEAREEADRTLDE---ARKDANKRRSEaAEQ 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2485 LQKQKNQAQEKAKKLLEDKQEIQQR--LDKETQGfQKSLEAERKRQLEISAEA--------EKLKLRVKELSSAqakAEE 2554
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEALRttTEAEAQA-DTMVGAARKEAERIVAEAtvegnslvEKARTDADELLVG---ARR 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAElekEREKLKRDAQELQNKSKETASAqqeq 2634
Cdd:NF041483 1115 DATAIRERAEELRDRITGEIEELHERARRESAEQMKSAGERCDALVKAAEE---QLAEAEAKAKELVSDANSEASK---- 1187
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2635 meqqkamLQQTFLTEKELLLKrerdvEDEKKKlqkhlEDEVNKAKALKDEQQRQQKLMDEEKKKLqaiMDEAVKKQKEAE 2714
Cdd:NF041483 1188 -------VRIAAVKKAEGLLK-----EAEQKK-----AELVREAEKIKAEAEAEAKRTVEEGKRE---LDVLVRRREDIN 1247
|
1290
....*....|....
gi 1655220517 2715 AEMKNKQKEMEALE 2728
Cdd:NF041483 1248 AEISRVQDVLEALE 1261
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
201-304 |
1.97e-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: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 279
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1655220517 280 NDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
201-304 |
2.80e-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: 120.08 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 278
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1655220517 279 RNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1478-2089 |
3.53e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.45 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1478 QEYVTLRTRYSELS-TLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQE 1556
Cdd:COG1196 213 ERYRELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1557 LKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTAD 1636
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1637 DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRL 1716
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1717 KQAEEEKVRQIKVVEEVAQKTAATQLQamsfsekttkleeslkkeqgtVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1796
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAA---------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1797 RLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTF----------AEQI 1866
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpldkiraraALAA 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1867 AQQKLSAEQEYIRLKADFEHAEQQRGLLDNEL---QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqaekvSQSN 1943
Cdd:COG1196 591 ALARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA--------GGSL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1944 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2023
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2024 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS---SSVSELDRQKNIVEETLRQKKVVEEEI 2089
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlLAIEEYEELEERYDFLSEQREDLEEAR 811
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1591-2425 |
3.94e-31 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 136.42 E-value: 3.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1591 NLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvRKAAQEEAERLRKQvnEE 1670
Cdd:PTZ00121 1056 HEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARK-AEEAKKKAEDARKA--EE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1671 TQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAER--RLKQAEE-EKVRQIKVVEEVAQKTAATQLQAMSF 1747
Cdd:PTZ00121 1133 ARKAEDA-----RKAEEARKAEDAKRVEIARKAEDARKAEEARKaeDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1748 SEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQE-EAEK 1826
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVN 1906
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1907 AAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTE-KSKQLLETEALKMKQLAEE---AARLRSVAEEAKKQR 1979
Cdd:PTZ00121 1368 AAEKKKEEAKkkaDAAKKKAEEKKKADEAKKKAEEDKKKADElKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEAKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1980 QLAEDEAARQRAEAekiLKEKLAAINEATRLKTEAEVALKAKEAEN--ERLKRQAED----EAYQRKLLEDQAAQHKHDI 2053
Cdd:PTZ00121 1448 EAKKKAEEAKKAEE---AKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEakkaAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2054 QEKITQLQSSSVSELDRQKNIVE-ETLRQKKVVEEEIHIIRInfERASKEKSDLEVELKKlkgiADETQKSKAKAEEEAE 2132
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRK----AEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKaaqdEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2212
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK----KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2213 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALlrQKAEE-----AEKLKKAAEDEAAKQAKAQKD 2287
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL--KKAEEenkikAEEAKKEAEEDKKKAEEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2288 AErlrkeaeaeaakrAAAEAAALKQKQEADAEMAKHKKEA--EQALKQKSqvEKELGLVKLQLDETDKQKALMDEELQRV 2365
Cdd:PTZ00121 1753 EE-------------EKKKIAHLKKEEEKKAEEIRKEKEAviEEELDEED--EKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2366 KAQVNDA----VKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKD-NTQKLLAEEAEK 2425
Cdd:PTZ00121 1818 NLVINDSkemeDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfNKEKDLKEDDEE 1882
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1704-2291 |
1.12e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.91 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1704 KHKMQAEEAERRLKQAEE----------EKVRQIKVVEEvaQKTAATQLQAMSFSEKTTKLEESLKKEQgtvlQLQEEAE 1773
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlerledilgELERQLEPLER--QAEKAERYRELKEELKELEAELLLLKLR----ELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1774 KLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1853
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1854 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMK 1933
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1934 IQAEKVSQSNTEKSKQLLETEAlkmkQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2013
Cdd:COG1196 403 EELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2014 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQ-----------------------LQSSSVSELDR 2070
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavligveaayeaaleaalaaaLQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2071 QKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEE 2150
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2151 KVKKIAAAEEEAARQRKAAQD-EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2229
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2230 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEaAKQAKAQKDAERL 2291
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE-RELERLEREIEAL 779
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
197-306 |
2.15e-30 |
|
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: 118.07 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 272
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1655220517 273 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 306
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1639-2241 |
5.21e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 5.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1639 LQKLRDQAAEAEKVRKAAQEEAERlrkQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1718
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKEL---EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1719 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1798
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1799 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1878
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1879 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQLLETEALKM 1958
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-----AARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1959 KQLAEEAARLRSVAEEAkkQRQLAEDEAARQRAEAekilkekLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 2038
Cdd:COG1196 514 LLLAGLRGLAGAVAVLI--GVEAAYEAALEAALAA-------ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2039 RKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLrqkkvveeEIHIIRINFERASKEKSDLEVELKKLKGIAD 2118
Cdd:COG1196 585 RAALAAALARGA--IGAAVDLVASDLREADARYYVLGDTLL--------GRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2119 EtqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQV 2198
Cdd:COG1196 655 G---GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1655220517 2199 ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK 2241
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
200-302 |
6.69e-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: 116.43 E-value: 6.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1502-2097 |
6.96e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 132.19 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1581
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1582 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1661
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA----KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1662 RLRKQVNEETQK---KKNAEdELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKVVEEVAQKT 1737
Cdd:PTZ00121 1382 AAKKKAEEKKKAdeaKKKAE-EDKKKADELKKAAAAKKKA-DEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKA 1459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1738 AATQLQAmsfsEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRL-RLRAEEEA 1814
Cdd:PTZ00121 1460 EEAKKKA----EEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA--KKAEEAKKAdEAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1815 QRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL 1894
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1895 DNELQRLKNE-VNAAEKQRRQLEDELAKVRSEMDALLQMKiQAEKVSQSNTEKSKQLLETEalkmKQLAEEAARlrsvAE 1973
Cdd:PTZ00121 1614 KAEEAKIKAEeLKKAEEEKKKVEQLKKKEAEEKKKAEELK-KAEEENKIKAAEEAKKAEED----KKKAEEAKK----AE 1684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1974 EAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEValkaKEAENERLKRQAEDEAYQRKLLEDQAAQhKHDI 2053
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEE-KKKI 1759
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1655220517 2054 QEKITQLQSSSVSELDRQKNIVEETLRQK-----KVVEEEIHIIRINFE 2097
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEdekrrMEVDKKIKDIFDNFA 1808
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
320-421 |
7.31e-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: 116.21 E-value: 7.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655220517 399 VDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
322-417 |
9.78e-30 |
|
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: 115.91 E-value: 9.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 322 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 400
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1655220517 401 VAHPDEKSIITYVSSLY 417
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
320-419 |
2.91e-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: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED- 398
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1655220517 399 VDVAHPDEKSIITYVSSLYDV 419
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1602-2477 |
2.13e-28 |
|
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: 126.71 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1602 QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADdELQKLRDQAAEAEK-----VRKAAQEEAERLRKQVNEETQKKKN 1676
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1677 AEDELK-----------RKSEAEKEAARQkQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAm 1745
Cdd:TIGR02168 258 LTAELQeleekleelrlEVSELEEEIEEL-QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1746 sfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR--LRLRAEEEAQRKSLAQEE 1823
Cdd:TIGR02168 336 --AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiASLNNEIERLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1824 AEKQKTEAERdakkKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKN 1903
Cdd:TIGR02168 414 DRRERLQQEI----EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1904 EVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALkmkqLAEEAARLRSVAEEAKKQRQ--L 1981
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAA----LGGRLQAVVVENLNAAKKAIafL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1982 AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAEnerlkrQAEDEAyqRKLLE------------DQAA-- 2047
Cdd:TIGR02168 566 KQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALSyllggvlvvddlDNALel 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2048 QHKHDIQEKITQLQSSSV---------------SELDRQKNIvEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKK 2112
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLVrpggvitggsaktnsSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2113 LKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEK 2192
Cdd:TIGR02168 717 LRKELEELSR---------------------QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2193 ELekqvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKK 2272
Cdd:TIGR02168 776 EL-------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2273 AAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaalkqkqeadAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETD 2352
Cdd:TIGR02168 849 ELSEDIESLAAEIEELE----------------------------ELIEELESELEALLNERASLEEALALLRSELEELS 900
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2353 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvRIEEE---NLRLMQKNKDNTQKLLAEEAEKMKSL 2429
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEyslTLEEAEALENKIEDDEEEARRRLKRL 977
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2430 AEEAARL---SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK 2477
Cdd:TIGR02168 978 ENKIKELgpvNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1502-2225 |
3.20e-28 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 126.79 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAEleaqelKLKMKEDASQrqglaVDAEKQKQN 1581
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAE------ELRKAEDARK-----AEAARKAEE 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1582 IQleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQ-EEA 1660
Cdd:PTZ00121 1211 ER----KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1740
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1741 QLQAMSFSEKTTKLEESLKK--EQGTVLQLQEEAEKLRKQEEEANKArEQAEKELETWRLKANE---ALRLRLRAEEEAQ 1815
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKaeEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEkkkADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1816 RKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK--ELEKQRTFAEQIAQQKLSAEQEyiRLKAD----FEHAEQ 1889
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEA--KKKADeakkAEEAKK 1523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1890 QRGLLDNELQRLKNEVNAAEKQRRQleDELAKVRSEMDAllQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1969
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKA--DELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1970 SVAEEAK-KQRQLAEDEAARQRAE----AEKILKEKLAAINEATRLKTEAEVALKAKEAEN---ERLKRQAEDEayQRKL 2041
Cdd:PTZ00121 1600 LYEEEKKmKAEEAKKAEEAKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEED--KKKA 1677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2042 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKgiADETQ 2121
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEE 1755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2122 KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA----NKLKDKAEKELEKQ 2197
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGnlviNDSKEMEDSAIKEV 1835
|
730 740
....*....|....*....|....*...
gi 1655220517 2198 VILAKEAAQKSTAAEQKAQDVLSKNKED 2225
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGED 1863
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1761-2624 |
5.40e-28 |
|
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: 125.55 E-value: 5.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1761 EQGTVLQLQE-EAEKLRKQEEEA------NKAREQAEKELEtwrlKANEAL-RLR-LRAEEEAQRKSLaqeeaEKQKTEA 1831
Cdd:TIGR02168 142 EQGKISEIIEaKPEERRAIFEEAagiskyKERRKETERKLE----RTRENLdRLEdILNELERQLKSL-----ERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1832 ERdakkkakaeeaaLKQKENAEKELEKqrtfaEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1911
Cdd:TIGR02168 213 ER------------YKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1912 RRQLEDELAKVRSEMDAL------LQMKIQAEKVSQSNTEKSKQLLETEALKMKQ----LAEEAARLRSVAEEAKKQRQL 1981
Cdd:TIGR02168 276 VSELEEEIEELQKELYALaneisrLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELKEELES 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1982 AE---DEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKIT 2058
Cdd:TIGR02168 356 LEaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2059 QLQSSSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLA 2138
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELER---LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2139 AEEERKRREAEEKVKKIAAAEEEAA---------------RQRKAAQDEVERLKQKAA------EANKLKDKAEKELEKQ 2197
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAaieaalggrlqavvvENLNAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2198 VILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALL----------------- 2260
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssi 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2261 ---RQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2337
Cdd:TIGR02168 673 lerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2338 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQK 2417
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLER 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2418 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2497
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRLDKETQGFQKsLEAERKRQLEISAEAEKLKL-----RVKELSSAQAKAEEEATRFKKQADE-AKVRLQ 2571
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLeeaeaLENKIEDDEEEARRRLKRLENKIKElGPVNLA 990
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2572 -ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2624
Cdd:TIGR02168 991 aIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNEN 1044
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1849-2737 |
1.40e-27 |
|
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: 123.93 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1849 KENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK----ADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1924
Cdd:pfam02463 179 IEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 EMDAlLQMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAI 2004
Cdd:pfam02463 259 EIEK-EEEKLAQVLKENKEEEKEKKLQEEEL---KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2005 NEATRLKTEAEVALKAKEAENErlkrqAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRqkkv 2084
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEE-----EEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK---- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2085 veeeihIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAeekvkkiaaaeeeaar 2164
Cdd:pfam02463 406 ------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD---------------- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2165 qrkaaQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQ 2244
Cdd:pfam02463 464 -----ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2245 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-RLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2323
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLiPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2324 KKEAEQALKQKSQVE--KELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2401
Cdd:pfam02463 619 DKRAKVVEGILKDTEltKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2402 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSveAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2481
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLEDKQEiqqrldketqgfqkslEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2561
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQE----------------EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAL 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2562 QADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2641
Cdd:pfam02463 841 ELKEEQKLEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2642 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNK 2720
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890
....*....|....*..
gi 1655220517 2721 QKEMEALEKKRLEQEKL 2737
Cdd:pfam02463 999 RLEEEKKKLIRAIIEET 1015
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
200-302 |
2.49e-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: 109.11 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1259-2013 |
3.25e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1259 IRNTKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEaEADQATFDRLQDELKAATSV--SDKMTRLHSERDA 1336
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELrkAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1337 ElehyrqlagsllerwqavfaqiDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAAPVwdskalkeQLTQEK 1416
Cdd:PTZ00121 1209 E----------------------EERKAE-----------------------EARKAEDAKKAEAV--------KKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1417 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQeyvtlrtryselstltSQ 1496
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK----------------AE 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1497 YIKFILETQRRLEDDEKASE--KLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA--ELEAQELKLKMKEDASQRQGLA 1572
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEakKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAadEAEAAEEKAEAAEKKKEEAKKK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1573 VDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEeihliriqLQTTIKQKSTAdDELQKLRDQAAEAEKV 1652
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAE-EDKKKADELKKAAAAKKKADE--------AKKKAEEKKKA-DEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1653 RKAAQE--EAERLRKQVNEetqkkKNAEDELKRKSEAEKEAARQKQKAlDELQKHKMQAEEAERRLKQAEE-EKVRQIKV 1729
Cdd:PTZ00121 1450 KKKAEEakKAEEAKKKAEE-----AKKADEAKKKAEEAKKADEAKKKA-EEAKKKADEAKKAAEAKKKADEaKKAEEAKK 1523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1730 VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlr 1809
Cdd:PTZ00121 1524 ADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL--- 1600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1810 AEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ 1889
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1890 QRGllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR 1969
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1655220517 1970 SVAEEAKKQRQLAEDeaarQRAEAEKILKEKLAAINEATRLKTE 2013
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1949-2773 |
6.48e-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: 121.70 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1949 QLLETEALKMKQLAEEAA---RLRSVAEEAkkQRQLAEDEAARQRAEAekILKEKLAAINeatRLKTEAEVALKAKEAEN 2025
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2026 ErlKRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSsVSELDRQKNIVEETLRQKKV----VEEEIHIIRINFERASK 2101
Cdd:TIGR02168 221 E--LRELELALLVLRL--EELREELEELQEELKEAEEE-LEELTAELQELEEKLEELRLevseLEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2102 EKSDLEVELKKLKGIADETQKSKakaeeeaeklkklaaeeerkrreaeekvKKIAAAEEEAARQRKAAQDEVERLKQKAA 2181
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQL----------------------------EELEAQLEELESKLDELAEELAELEEKLE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2182 EANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLR 2261
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2262 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQK----SQV 2337
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfSEG 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2338 EKELGLVKLQLD----------ETDKQ-----KALMDEELQRVKAQVNDAVKQ--KAQVENELSKVKMQmdELLKLKVRI 2400
Cdd:TIGR02168 508 VKALLKNQSGLSgilgvlseliSVDEGyeaaiEAALGGRLQAVVVENLNAAKKaiAFLKQNELGRVTFL--PLDSIKGTE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2401 EEENLRLMQKNKDNTQKLLAEEAEKMKSLA----------------EEAARLSVEAEETAR------QRKTAEAELAEQR 2458
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRivtldgDLVRPGGVITGGS 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2459 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2538
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2539 KLRVKELSSAQAKAEEEATRFKKQADEAkvrlqETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2618
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEA-----EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2619 ELQNKsKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKK 2698
Cdd:TIGR02168 821 NLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2699 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEkKRLEQEKLLADENK-KLREKLE-SLEVTSKQAASKTKEIEVQTDKV 2773
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLE-LRLEGLEVRIDNLQeRLSEEYSlTLEEAEALENKIEDDEEEARRRL 974
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
193-304 |
8.56e-27 |
|
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: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 193 RIADERDRVQKKTFTKWVNKHLMKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 269
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655220517 270 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
200-305 |
1.50e-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: 107.42 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1973-2801 |
2.86e-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: 119.69 E-value: 2.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1973 EEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQhKHD 2052
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD-EQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2053 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAE 2132
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2212
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2213 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2292
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2293 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQ--VN 2370
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVraLT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2371 DAVKQKAQVENELSKVKMQMDELLKLKV-------RIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARL------- 2436
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIdpilnlaQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKesglrkg 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2437 -SVEAEETARQRKTAEAELAEQRALAEKMLKEKM--------QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQ 2507
Cdd:pfam02463 652 vSLEEGLAEKSEVKASLSELTKELLEIQELQEKAeselakeeILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQ 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2508 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLET 2587
Cdd:pfam02463 732 DKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELK 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2588 QRLQSTREADDLKKaiAELEKEREKLKRDAQELQNKSKETASAQQEQmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKL 2667
Cdd:pfam02463 812 EEAELLEEEQLLIE--QEEKIKEEELEELALELKEEQKLEKLAEEEL-ERLEEEITKEELLQELLLKEEELEEQKLKDEL 888
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2668 QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK-----------EAEAEMKNKQKEMEALEKKRLEQEK 2736
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeepeellleEADEKEKEENNKEEEEERNKRLLLA 968
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2737 LLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKD 2801
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
302-417 |
3.69e-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: 106.32 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 302 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAF 381
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655220517 382 SVAERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1786-2515 |
1.54e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.96 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1786 REQAEKELEtwRLKANEAlRLRLRAEE-EAQRKSLaQEEAEK-------QKTEAERDAKKKAKAEEAALKQKENAEKELE 1857
Cdd:COG1196 174 KEEAERKLE--ATEENLE-RLEDILGElERQLEPL-ERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1858 KqrtfaeqiaqqklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1937
Cdd:COG1196 250 E--------------LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1938 KVSQSNTEKSKQLLETEALKMKQLAEEAARLRSvAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 2017
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2018 LKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEihiirinfE 2097
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL--------A 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2098 RASKEKSDLEVELKKLKGIADEtqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaARQRKAAQDEVERLK 2177
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAE-------------------------------------------AAARLLLLLEAEADY 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2178 QKAAEANKLKDKAEKELEKQVILAkEAAQKSTAAEQKAQDVLSknkedLLSQEKLRDEFENAKKLAQaaetakekAEKEA 2257
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALA-----AALQNIVVEDDEVAAAAIE--------YLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2258 ALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2337
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2338 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKvRIEEENLRLMQKNKDNTQK 2417
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL-AEAEEERLEEELEEEALEE 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2418 LLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK----MQAIQEATKLKAEAEELQKQKNQAq 2493
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQREDL- 807
|
730 740
....*....|....*....|..
gi 1655220517 2494 EKAKKLLEdkqEIQQRLDKETQ 2515
Cdd:COG1196 808 EEARETLE---EAIEEIDRETR 826
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
322-417 |
2.53e-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: 103.00 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 322 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED-VD 400
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1655220517 401 VAHPDEKSIITYVSSLY 417
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1854-2705 |
2.62e-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: 116.69 E-value: 2.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1854 KELEKQrtfAEQIAQQKLSAEQeYIRLKADFEHAeqQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlQMK 1933
Cdd:TIGR02168 196 NELERQ---LKSLERQAEKAER-YKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQEL-EEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1934 IQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTE 2013
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKE---LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2014 AEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHK------HDIQEKITQLQSSsVSELDRQKNIVEETLRQKKVVEE 2087
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLEtlrskvAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2088 EIhiiriNFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRK 2167
Cdd:TIGR02168 425 EL-----LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2168 AAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKED-------LLSQEKLRDEF---- 2236
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVVVENLNAakkaiafLKQNELGRVTFlpld 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2237 -ENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAE------------DEAAKQAKAQKDAERLRKEAEAEAAKRA 2303
Cdd:TIGR02168 580 sIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2304 AAEAAALKQKQ---EADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVE 2380
Cdd:TIGR02168 660 VITGGSAKTNSsilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2381 NELSKVKMQMDELlklkvrieeenlrlmqknkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAeqral 2460
Cdd:TIGR02168 740 AEVEQLEERIAQL----------------------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE----- 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2461 aekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKL 2540
Cdd:TIGR02168 793 ---------QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAA 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2541 RVKELSSAQAKAEEEATRFKKQADEAKVRLQ--ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQ 2618
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2619 ELQnkskETASAQQEqmeqqkaMLQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKA--KALKDEQQRQQKL--- 2691
Cdd:TIGR02168 940 NLQ----ERLSEEYS-------LTLEEAEALENKIEDDEEEARRRLKRLENKIKElgPVNLAaiEEYEELKERYDFLtaq 1008
|
890
....*....|....*..
gi 1655220517 2692 ---MDEEKKKLQAIMDE 2705
Cdd:TIGR02168 1009 kedLTEAKETLEEAIEE 1025
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1595-2517 |
4.78e-25 |
|
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: 115.84 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1595 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKK 1674
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1675 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamsfSEKTTKL 1754
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD---------EEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1755 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERD 1834
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEE-------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1835 AKkkakaeeaalkqkENAEKELEKQRTFAEQIaqqklsaeqeyirlkadfEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1914
Cdd:pfam02463 393 KE-------------EELELKSEEEKEAQLLL------------------ELARQLEDLLKEEKKEELEILEEEEESIEL 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1915 LEDELAKVRSEMDALLQMKIQAEKVSqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAE 1994
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELEL----KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIK 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1995 KILKEKL-AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2073
Cdd:pfam02463 518 DGVGGRIiSAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2074 IVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL----KGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAE 2149
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesaKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2150 EKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEanKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQ 2229
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIKKKEQREKE--ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2230 EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaaKRAAAEAAA 2309
Cdd:pfam02463 756 RLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL---------EEEQLLIEQ 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELskvkmQ 2389
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK-----E 901
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2390 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEaelAEQRALAEKMLKEKM 2469
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK---RLLLAKEELGKVNLM 978
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2470 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGF 2517
Cdd:pfam02463 979 AIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
304-417 |
5.36e-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: 102.86 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 304 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 383
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 384 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
317-417 |
6.25e-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: 102.12 E-value: 6.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 396
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1655220517 397 ED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21198 80 ADmVLLSVPDKLSVMTYLHQIR 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
317-421 |
7.23e-25 |
|
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: 101.79 E-value: 7.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1655220517 397 EDVDVAHPDEKSIITYVSSLYDVMP 421
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
318-417 |
7.63e-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: 101.87 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 318 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 397
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1655220517 398 D-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
204-301 |
1.36e-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: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 204 KTFTKWVNKHLMKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 279
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1655220517 280 NDDIADGnPKLTLGLIWTIILH 301
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
316-422 |
2.15e-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: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 316 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ--ENLEQAFSVAERELGVTR 392
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1655220517 393 -LLDPEdvDVAHPDEKSIITYVSSLYDVMPR 422
Cdd:pfam00307 81 vLIEPE--DLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2179-2753 |
2.69e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2179 KAAEAN--KLKDKAEkELEKQV-ILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEK 2255
Cdd:COG1196 182 EATEENleRLEDILG-ELERQLePLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2256 EaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKS 2335
Cdd:COG1196 261 E---LAELEAELEELRLELEELELELEEAQAEEYEL------------------LAELARLEQDIARLEERRRELEERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2336 QVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKnKDNT 2415
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2495
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2496 AKKLLEDKQEIQQRLD------KETQGFQKSLEAERK---------------------RQLEISAEAEKLKLRVKELSSA 2548
Cdd:COG1196 479 LAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2549 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-----------LEKEREKLKRDA 2617
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2618 QELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKK 2697
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2698 KLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN------KKLREKLESLE 2753
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEelerelERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2420-2779 |
2.85e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.11 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2420 AEEAEKMKSLAEEAARLsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2499
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2500 LEDKQEIQQRLDKETQgfQKSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQtte 2579
Cdd:COG1196 287 QAEEYELLAELARLEQ--DIARLEERRRELE--ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2580 tvvqkletqRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltEKELLLKRERD 2659
Cdd:COG1196 360 ---------LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA--------LLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2660 VEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLA 2739
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220517 2740 DENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLV 2779
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
320-420 |
1.77e-23 |
|
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: 97.92 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDV 399
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1655220517 400 DVAHPDEKSIITYVSSLYDVM 420
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
201-304 |
3.05e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 97.36 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 276
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
957-1023 |
5.13e-23 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 95.02 E-value: 5.13e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 957 QLKPRNpaTPIKSKLPIQAVCDFKQMEITVHRGDECALLNNSQPYKWRVLNDKGSEASVPSICFLVP 1023
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
304-417 |
6.18e-23 |
|
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: 97.10 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 304 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 383
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 384 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1501-2424 |
8.26e-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: 108.52 E-value: 8.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1501 ILETQRRLEDDEKASEKLKEDEKKrmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1580
Cdd:pfam02463 185 LAELIIDLEELKLQELKLKEQAKK--ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1660
Cdd:pfam02463 263 EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQktaat 1740
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE----- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1741 qlqamsfsekttkleeslkkeqgtvlqlqeeaekLRKQEEEANKAREQAEKEletwrlKANEALRLRLRAEEEAQRKSLA 1820
Cdd:pfam02463 413 ----------------------------------LARQLEDLLKEEKKEELE------ILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1821 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQR 1900
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1901 LKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ 1980
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1981 LAEDEAARQRAEAEKILKEKlaainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQL 2060
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDT-----ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2061 QSSSVSELDRQKNIVEETLRQKKVVE---EEIHIIRINFERASKEKSDLEVELKKLKgIADETQKSKAKAEEEAEKLKKL 2137
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQK-IDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2138 AAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERlkqkaAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQD 2217
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR-----ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2218 VLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEA 2297
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2298 EAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2377
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE---EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1655220517 2378 QVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2424
Cdd:pfam02463 999 RLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGS 1045
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1263-2069 |
3.90e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.38 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1263 KDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELkaatsvsdkmtRLHSERDAELEHYR 1342
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI-----------RKFEEARMAHFARR 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1343 QLAGSLLERWQAVfaqiDLRQRELSllgRHMNSYKQSYEwlIQWLREARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1422
Cdd:PTZ00121 1269 QAAIKAEEARKAD----ELKKAEEK---KKADEAKKAEE--KKKADEAKKKAEEAKKA-----DEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1423 EKNKDQIENCQKDAKAYIDSLKDYefqilAYRALQDPIASPLKKPKMESASDNIIQEyvtlrtryselstltSQYIKFIL 1502
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADE-----AEAAEEKAEAAEKKKEEAKKKADAAKKK---------------AEEKKKAD 1394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEghAKSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQ 1580
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADE--AKKKAEEAKKADEAK-KKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 NIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihliriqlqttiKQKStadDELQKlRDQAAEAEKVRKAAQ-EE 1659
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA------------KKKA---DEAKK-AEEAKKADEAKKAEEaKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1660 AERLRKQvnEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAerrlKQAEEEKVRQIKVVEEVAQKTAA 1739
Cdd:PTZ00121 1536 ADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKMKA 1609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1740 TQL----QAMSFSEKTTKLEESLKKEQGTVLQLQEE---AEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlRAEE 1812
Cdd:PTZ00121 1610 EEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-----KKAE 1684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1813 EAQRKSlaqEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIaqqKLSAEQEyirlKADFEHAEQQRG 1892
Cdd:PTZ00121 1685 EDEKKA---AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA---KKEAEED----KKKAEEAKKDEE 1754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1893 LLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQ---------AEKVSQSNTEKSKQLLETEALKMKQLAE 1963
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1964 EAARLRSVAEEAK--------KQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDE 2035
Cdd:PTZ00121 1835 VADSKNMQLEEADafekhkfnKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDI 1914
|
810 820 830
....*....|....*....|....*....|....
gi 1655220517 2036 AYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELD 2069
Cdd:PTZ00121 1915 IDDKLDKDEYIKRDAEETREEIIKISKKDMCIND 1948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1350-1929 |
4.20e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 4.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1350 ERWQAVfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEknkDQI 1429
Cdd:COG1196 213 ERYREL--KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE----LAELEAELEELRLELEELE---LEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1430 ENCQKDAKAYIDSLKDYEFQILAYRALQdpiasplkkpkmESASDNIIQEYVTLRTRYSELSTLTSQyIKFILETQRRLE 1509
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERR------------RELEERLEELEEELAELEEELEELEEE-LEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1510 DDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1589
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1590 KNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1667
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELlaELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1668 NEETQKKKNAE-----------DELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQK 1736
Cdd:COG1196 511 KAALLLAGLRGlagavavligvEAAYEAALEAALAAALQNIVVEDDE----VAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1737 TAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQR 1816
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1817 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1896
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
570 580 590
....*....|....*....|....*....|...
gi 1655220517 1897 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1929
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
200-305 |
4.37e-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: 4.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQIS 305
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 ... |
200-305 |
6.79e-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: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 200 RVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1503-2395 |
8.14e-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: 105.14 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLkEDEKKRMAEIQAQLETQKQLAEG-HAKSVAKAELEAQELKLKMKEdasqrqglAVDAEKQKQN 1581
Cdd:TIGR02168 176 ETERKLERTRENLDRL-EDILNELERQLKSLERQAEKAERyKELKAELRELELALLVLRLEE--------LREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1582 IQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1661
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1662 RLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQ 1741
Cdd:TIGR02168 327 ELE-------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1742 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ 1821
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1822 EEAEKQKTEAErdakkkakaEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---------EYIRLKADFEHAeqqrg 1892
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAA----- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1893 lLDNELQ-RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLR-- 1969
Cdd:TIGR02168 539 -IEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1970 ------------SVAEEAKKQRQLAEDEA---------------ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 2022
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALELAKKLRPGYRivtldgdlvrpggviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2023 AENERLK---RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNI---VEETLRQKKVVEEEIHIIRINF 2096
Cdd:TIGR02168 698 KALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskeLTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2097 ERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERL 2176
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2177 KQKAAEANKLKDKAEKELekqvilakEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKlaqaaetakekaeke 2256
Cdd:TIGR02168 858 AAEIEELEELIEELESEL--------EALLNERASLEEALALLRSELEEL--SEELRELESKRSE--------------- 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2257 aalLRQKAEEA-EKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAeqalkqks 2335
Cdd:TIGR02168 913 ---LRRELEELrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI-------- 981
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2336 qveKELGLVKLQ-LDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLK 2395
Cdd:TIGR02168 982 ---KELGPVNLAaIEEYEELK----ERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2164-2705 |
9.56e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLA 2243
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2244 QAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2323
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2324 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2403
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2404 NLRLMQ--------KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEA 2475
Cdd:COG1196 500 EADYEGflegvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2476 TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ--KSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAE 2553
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2554 EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE 2633
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2634 QMEQQKAMLQQTFLTEKELLLKRErDVEDEKKKLQKHLE----------DEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2703
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLE-ELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAI 818
|
..
gi 1655220517 2704 DE 2705
Cdd:COG1196 819 EE 820
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
304-417 |
2.13e-21 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 92.83 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 304 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSV 383
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 384 AERELGVTRLLDPED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
317-417 |
5.10e-21 |
|
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: 90.87 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDP 396
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1655220517 397 EDVDV--AHPDEKSIITYVSSLY 417
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1409-2115 |
7.24e-21 |
|
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: 102.06 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1409 KEQLTQEKKLLEEIEKNKDQIENCQKDAKAYID------------SLKDYEFQILAYRALQDPIASP------------- 1463
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERYKElkaelrelelalLVLRLEELREELEELQEELKEAeeeleeltaelqe 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1464 ---------LKKPKMESASDNIIQEYVTLrtrYSELSTLTSQyIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLE 1534
Cdd:TIGR02168 265 leekleelrLEVSELEEEIEELQKELYAL---ANEISRLEQQ-KQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1535 TQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKL 1614
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1615 EEEIHLIRIQLQTtiKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaekeaARQ 1694
Cdd:TIGR02168 420 QQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ--------LQA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1695 KQKALDELQKHKMQAEEAERRLKQAEEEK-------VRQIKVVEE---------------VAQKTAATQLQAMSF----- 1747
Cdd:TIGR02168 490 RLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlSELISVDEGyeaaieaalggrlqaVVVENLNAAKKAIAFlkqne 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1748 SEKTTKLEESLKKE---QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW--------RLKANEALRLRLRAEE---- 1812
Cdd:TIGR02168 570 LGRVTFLPLDSIKGteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvdDLDNALELAKKLRPGYrivt 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1813 ---------------EAQRKSLAQ------EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKL 1871
Cdd:TIGR02168 650 ldgdlvrpggvitggSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1872 SAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL----LQMKIQAEKVSQSNTEKS 1947
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqiEQLKEELKALREALDELR 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1948 KQLLETE------ALKMKQLAEEAARLRSVAEEAKKQ-RQLAED--EAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 2018
Cdd:TIGR02168 810 AELTLLNeeaanlRERLESLERRIAATERRLEDLEEQiEELSEDieSLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2019 KAKEAENERLKRQAEDEAYQRKLLEDQ---AAQHKHDIQEKITQLQsssvSELDRQKniveETLRQKKVVEEEIHIIRIN 2095
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRREleeLREKLAQLELRLEGLE----VRIDNLQ----ERLSEEYSLTLEEAEALEN 961
|
810 820
....*....|....*....|
gi 1655220517 2096 FERASKEKsdLEVELKKLKG 2115
Cdd:TIGR02168 962 KIEDDEEE--ARRRLKRLEN 979
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1502-2580 |
1.10e-20 |
|
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: 101.41 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQRRLEDDEKASEKLKEdEKKRMAE-IQAQLETQKQLAEGHAKSVA-KAELEA--QELKLKMKEDASQRQGLAVDAEK 1577
Cdd:pfam01576 22 QKAESELKELEKKHQQLCE-EKNALQEqLQAETELCAEAEEMRARLAArKQELEEilHELESRLEEEEERSQQLQNEKKK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1578 QKQNIQLELTQLKnlsEQEIRSKNQQLEE--AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEkvrka 1655
Cdd:pfam01576 101 MQQHIQDLEEQLD---EEEAARQKLQLEKvtTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEE----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 aqEEAERLRKQVNEETQKKKNAEDELKR--KSEAEKEAARQKQKA-LDELQKH----KMQAEEAERRLKQAEEE-KVRQI 1727
Cdd:pfam01576 173 --EKAKSLSKLKNKHEAMISDLEERLKKeeKGRQELEKAKRKLEGeSTDLQEQiaelQAQIAELRAQLAKKEEElQAALA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQKTAAtqlqamsfsekttklEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrLKANEALRLR 1807
Cdd:pfam01576 251 RLEEETAQKNNA---------------LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA--LKTELEDTLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1808 LRAEEEAQRKSLAQEEAEKQKT---EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADF 1884
Cdd:pfam01576 314 TTAAQQELRSKREQEVTELKKAleeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1885 E-------HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE----KVSQSNTEKSKQLLET 1953
Cdd:pfam01576 394 RtlqqakqDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEgkniKLSKDVSSLESQLQDT 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1954 EAL---KMKQLAEEAARLRSVAEEAKK-QRQLAEDEAARQRAEAEkilkeklaaineatrlkteaevaLKAKEAENERLK 2029
Cdd:pfam01576 474 QELlqeETRQKLNLSTRLRQLEDERNSlQEQLEEEEEAKRNVERQ-----------------------LSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2030 RQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNiveetlrqkkvveeeihiirinfeRASKEKSDLE 2107
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEekAAAYDKLEKTKN------------------------RLQQELDDLL 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2108 VELKKLKGIADETQKskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERlKQKAAEANKLK 2187
Cdd:pfam01576 587 VDLDHQRQLVSNLEK-----------------------------------------KQKKFDQMLAEE-KAISARYAEER 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2188 DKAEKELE----KQVILAKEAAQKSTAAEQ--KAQDVLSKNKEDLLSQE----KLRDEFENAKKLAQAAETAkekaekea 2257
Cdd:pfam01576 625 DRAEAEAReketRALSLARALEEALEAKEEleRTNKQLRAEMEDLVSSKddvgKNVHELERSKRALEQQVEE-------- 696
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2258 alLRQKAEEAEKLKKAAED-----EAAKQA-KAQKDAErlrkeAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQAL 2331
Cdd:pfam01576 697 --MKTQLEELEDELQATEDaklrlEVNMQAlKAQFERD-----LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAV 769
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2332 KQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKqkaqvenELSKVKMQMDELL--------KLKvRIEEE 2403
Cdd:pfam01576 770 AAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR-------ELEEARASRDEILaqskesekKLK-NLEAE 841
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2404 NLRL-------------MQKNKDNTQKLLAEEAEKMKSLAEEAARLSV-------EAEETA--------RQRKTAE---- 2451
Cdd:pfam01576 842 LLQLqedlaaserarrqAQQERDELADEIASGASGKSALQDEKRRLEAriaqleeELEEEQsntellndRLRKSTLqveq 921
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2452 --AELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK-QEIQQRLDKETQGFQKS-------- 2520
Cdd:pfam01576 922 ltTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKiAQLEEQLEQESRERQAAnklvrrte 1001
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2521 ---------LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfkkqADEAKVRLQETEKQTTET 2580
Cdd:pfam01576 1002 kklkevllqVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR----ANAARRKLQRELDDATES 1066
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
321-419 |
1.41e-20 |
|
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: 89.72 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 321 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLD-PEDV 399
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1655220517 400 DVAHPDEKSIITYVSSLYDV 419
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1264-1929 |
1.45e-20 |
|
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: 100.90 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1264 DAEDTVKSYESRLRDVSKvpaEEKEVEAHRSQLKAMRAEAEAD-----------QATFDRLQDELKAATSVSDKMTRLHS 1332
Cdd:TIGR02168 299 RLEQQKQILRERLANLER---QLEELEAQLEELESKLDELAEElaeleekleelKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1333 ERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQ--------EKIEAAPVWD 1404
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaeleelEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1405 SKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqiLAYRALQDPIASPLKKPKMESASDNIIQEYVTLR 1484
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ---ENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1485 TRYS-ELSTLTSQYIKFILetQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKE 1563
Cdd:TIGR02168 533 EGYEaAIEAALGGRLQAVV--VENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1564 DASQRQGLA--------VDAEKQKQNIQLELTQLKNL--------------------SEQEIRSKNQQLEEAQVSRRKLE 1615
Cdd:TIGR02168 611 DPKLRKALSyllggvlvVDDLDNALELAKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEELE 690
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1616 EEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQK 1695
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1696 QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKL 1775
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1776 RKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKkakaeeaalkqkenAEKE 1855
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE--------------LRRE 916
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1856 LEKQRTFAEQIAQQKLSAEQEYIRLKadfehaEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1929
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQ------ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1287-2044 |
3.01e-20 |
|
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: 100.13 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1287 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1366
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1367 sllgRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY 1446
Cdd:TIGR02168 312 ----ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1447 EFQILAYRALQDPIASPLKKPKMESAS--DNIIQEYVTLRTRYS-----ELSTLTSQYIKFILETQRRLEDDEKASEKLK 1519
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDrrERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1520 E----------DEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELEAQEL---------KLKMKE-------------- 1563
Cdd:TIGR02168 468 EeleeaeqaldAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEgyeaaieaalggrl 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1564 -----DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN----QQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1634
Cdd:TIGR02168 548 qavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDreilKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 ADDELQKLRDQAAEAEKVRkAAQEEAERLRK---------QVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKH 1705
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYR-IVTLDGDLVRPggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1706 KMQAEEAERRLKQAEEEKVRQIkvveevaqktAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1785
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQI----------SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1786 REQAEKELETwrlkaNEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAkaeeaalkqKENAEKELEKQRTFAEQ 1865
Cdd:TIGR02168 777 LAEAEAEIEE-----LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER---------LESLERRIAATERRLED 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1866 IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTE 1945
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1946 KSKQL-LETEALKMkQLAEEAARLRS----VAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAA---INEAtrlkteaevA 2017
Cdd:TIGR02168 923 KLAQLeLRLEGLEV-RIDNLQERLSEeyslTLEEAEALENKIEDDEEEARRRLKR-LENKIKElgpVNLA---------A 991
|
810 820 830
....*....|....*....|....*....|
gi 1655220517 2018 LKAKEAENER---LKRQAEDEAYQRKLLED 2044
Cdd:TIGR02168 992 IEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
317-416 |
3.89e-20 |
|
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: 88.31 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 396
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|..
gi 1655220517 397 EDVdVAH--PDEKSIITYVSSL 416
Cdd:cd21255 80 ADM-VLLpiPDKLIVMTYLCQL 100
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
313-420 |
1.08e-19 |
|
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: 87.31 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 313 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTR 392
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1655220517 393 LLDPEDV-DVAHPDEKSIITYVSSLYDVM 420
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
202-302 |
2.67e-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: 86.10 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 277
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1655220517 278 IRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
317-416 |
6.55e-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: 84.90 E-value: 6.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 396
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1655220517 397 ED-VDVAHPDEKSIITYVSSL 416
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1265-1953 |
8.95e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 8.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1265 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrlHSERDAELEHYRQL 1344
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLE----------LEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1345 AGSLLERWQAVFAQIDLRQRELSLLGRhmnsykqsyewliqwlREARLRQEKIEAApvWDSKALKEQLTQEKKLLEEIEK 1424
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEE----------------RLEELEEELAELE--EELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1425 NKDQIENCQKDAKAyidslkdyefqilayralqdpiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILET 1504
Cdd:COG1196 352 ELEEAEAELAEAEE--------------------------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1505 QRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL 1584
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1585 ELTQLKNLSE-QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQkLRDQAAEAEKVRKAAQEEAERL 1663
Cdd:COG1196 485 ELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-AALAAALQNIVVEDDEVAAAAI 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1664 rkqvneETQKKKNAEdelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQ 1743
Cdd:COG1196 564 ------EYLKAAKAG----RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1744 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEE 1823
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1824 AEKQKTEAERDakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLkN 1903
Cdd:COG1196 714 EERLEEELEEE------------ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-G 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1904 EVN-------AAEKQRRQ-LEDELAKVRSEMDALLQMkiqaekVSQSNTEKSKQLLET 1953
Cdd:COG1196 781 PVNllaieeyEELEERYDfLSEQREDLEEARETLEEA------IEEIDRETRERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2483-2780 |
1.38e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2483 EELQKQKNQAqEKAKKLLEDKQEIQQRLD-KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2561
Cdd:COG1196 203 EPLERQAEKA-ERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2562 QADEAKVRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASAQQEQMEQQKAM 2641
Cdd:COG1196 282 ELEEAQAEEYELLAE-----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-LEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2642 LQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAImdEAVKKQKEAEAEmKNKQ 2721
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEE-ALAE 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2722 KEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2780
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
317-415 |
1.96e-18 |
|
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: 83.44 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGKLFNAIIHKHRPALLDMS-QVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1655220517 396 PEDVDVAHPDEKSIITYVSS 415
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1512-2512 |
2.37e-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: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1512 EKASEKLKEDEKkRMAEIQAQLETQKQLAEGHAKSVAKAElEAQELKLKMKE-DASQRQGLAVDAEKQKQNIqleltqlk 1590
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyEGYELLKEKEALERQKEAI-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1591 nlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLqttikqkstaddelqklrdqAAEAEKVRKAAQEEAERLRKQVNEE 1670
Cdd:TIGR02169 243 ---ERQLASLEEELEKLTEEISELEKRLEEIEQLL--------------------EELNKKIKDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1671 TQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLkqaEEEKVRQIKVVEEVAqktaatqlqamsfsEK 1750
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREI---EEERKRRDKLTEEYA--------------EL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1751 TTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREqaekELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTE 1830
Cdd:TIGR02169 363 KEELEDLRA-------ELEEVDKEFAETRDELKDYRE----KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1831 AERDAKKKAKAeeaalkqKENAEKELEKQrtfaeqiaqqklsaEQEYIRLKADFEHAEQqrglldnELQRLKNEVNAAEK 1910
Cdd:TIGR02169 432 IEAKINELEEE-------KEDKALEIKKQ--------------EWKLEQLAADLSKYEQ-------ELYDLKEEYDRVEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1911 QRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQLAEDEAArqR 1990
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVA-QLGSVGERYATAIEVAAGNRLNNVVVEDDAV--A 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1991 AEAEKILKEKlaAINEATRLKteaevalkakeaenerLKRQAEDEAYQRKLLEDQAAQHKHDiqekitqlqsssVSELDR 2070
Cdd:TIGR02169 561 KEAIELLKRR--KAGRATFLP----------------LNKMRDERRDLSILSEDGVIGFAVD------------LVEFDP 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2071 Q-KNIVEETLRQKKVVE--EEIHIIRINFERASkeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2147
Cdd:TIGR02169 611 KyEPAFKYVFGDTLVVEdiEAARRLMGKYRMVT-----LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2148 AEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA-------QKSTAAEQKAQDVLS 2220
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlssleQEIENVKSELKELEA 765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2221 KNKEDLLSQEKLRDEFENAKklaqaaetakekaekeAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaa 2300
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLE----------------ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ---------- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2301 kraaAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDEtdkqkalMDEELQRVKAQVNDAVKQKAQVE 2380
Cdd:TIGR02169 820 ----KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLK 888
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2381 NELSKVKMQMDEllkLKVRIEEENLRLMQKNK-DNTQKLLAEEA-EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2458
Cdd:TIGR02169 889 KERDELEAQLRE---LERKIEELEAQIEKKRKrLSELKAKLEALeEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2459 ALaEKMLKEKMQAIQeatklkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK 2512
Cdd:TIGR02169 966 EI-RALEPVNMLAIQ-------EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1683-2789 |
2.41e-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: 93.70 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLkkeq 1762
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEIL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1763 gtvlqlqEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrlrlrAEEEAQRKSLaqeEAEKQKTEAERDAKKKAKAE 1842
Cdd:pfam01576 78 -------HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL-----DEEEAARQKL---QLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1843 EAALKQKENAEKELEKQRtfaeqIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNA---AEKQRRQLEDEL 1919
Cdd:pfam01576 143 LEDQNSKLSKERKLLEER-----ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1920 AKVRSEMdalLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE----AKKQRQLAEDEAARQRAEAEK 1995
Cdd:pfam01576 218 TDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiSELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1996 I-LKEKLAAineatrLKTEAEVALKAKEAENE-RLKRQAEDEAYQrKLLEDQAAQHKHDIQEkITQLQSSSVSELDRQkn 2073
Cdd:pfam01576 295 RdLGEELEA------LKTELEDTLDTTAAQQElRSKREQEVTELK-KALEEETRSHEAQLQE-MRQKHTQALEELTEQ-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2074 iVEETLRQKKVVEEEIHIIRinferasKEKSDLEVELKKLKGIADETQKskakaeeeaeklkklaaeeerKRREAEEKVK 2153
Cdd:pfam01576 365 -LEQAKRNKANLEKAKQALE-------SENAELQAELRTLQQAKQDSEH---------------------KRKKLEGQLQ 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2154 KIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKqviLAKEAAQkstaAEQKAQDVLSknkedlLSQEKLR 2233
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK---LSKDVSS----LESQLQDTQE------LLQEETR 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2234 DEFENAKKlaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraAAEAAALKQK 2313
Cdd:pfam01576 483 QKLNLSTR------------------LRQLEDERNSLQEQLEEEEEAKRNVERQLSTL------------QAQLSDMKKK 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2314 QEADAEMakhkkeAEQALKQKSQVEKELGLVKLQLDEtdkqKALMDEELQrvkaqvndavKQKAQVENELSKVKMQMDEL 2393
Cdd:pfam01576 533 LEEDAGT------LEALEEGKKRLQRELEALTQQLEE----KAAAYDKLE----------KTKNRLQQELDDLLVDLDHQ 592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2394 LKLKvrieeENLRLMQKNKDntqKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEAELAeqRALAEkmLKEKMQAIQ 2473
Cdd:pfam01576 593 RQLV-----SNLEKKQKKFD---QMLAEEKAISARYAEERDR----AEAEAREKETRALSLA--RALEE--ALEAKEELE 656
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2474 EATK-LKAEAEELQKQKNQAQ------EKAKKLLEDK-QEIQQRLDKETQGFQKSLEAerKRQLEISAEAEKLKLRvKEL 2545
Cdd:pfam01576 657 RTNKqLRAEMEDLVSSKDDVGknvhelERSKRALEQQvEEMKTQLEELEDELQATEDA--KLRLEVNMQALKAQFE-RDL 733
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2546 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVV--QKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNK 2623
Cdd:pfam01576 734 QARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAakKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRE 813
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2624 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRE---------RDVEDEKKKLQKHLEDEVNKAKALKDEQQR---QQKL 2691
Cdd:pfam01576 814 LEEARASRDEILAQSKESEKKLKNLEAELLQLQEdlaaserarRQAQQERDELADEIASGASGKSALQDEKRRleaRIAQ 893
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2692 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEA---LEKKRLEQEKLLADENKKLREKLESLE--VTSKQAAS----- 2761
Cdd:pfam01576 894 LEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAersTSQKSESARQQLERQNKELKAKLQEMEgtVKSKFKSSiaale 973
|
1130 1140
....*....|....*....|....*....
gi 1655220517 2762 -KTKEIEVQTDKVPEEQLVSMTTVETTKK 2789
Cdd:pfam01576 974 aKIAQLEEQLEQESRERQAANKLVRRTEK 1002
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2319-2767 |
2.93e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.20 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2319 EMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVE---NELSKVKMQMDELLK 2395
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2396 lKVRIEEENLRLMQKNKDNTQKLLAE------EAEKMKSLAEEAARLSVEAEETARQRKTAEAELA---EQRALAEKMLK 2466
Cdd:PRK03918 253 -SKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSrleEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2467 EKMQAIQEATKLKAEAEELQKQKN------QAQEKAKKLLEDKQEIQQRL-DKETQGFQKSLEAERKRQLEISAEAEKLK 2539
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2540 LRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLetqrlqsTREADDLKKAIAELEKEREKLKRDAQE 2619
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEY-------TAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2620 LQN--KSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKL------QKHLEDEVNKAKALKDEQQRQQKL 2691
Cdd:PRK03918 485 LEKvlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2692 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE----------QEKLLADENKKLREKLESLEVTSKQAAS 2761
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLElkdaekelerEEKELKKLEEELDKAFEELAETEKRLEE 644
|
....*.
gi 1655220517 2762 KTKEIE 2767
Cdd:PRK03918 645 LRKELE 650
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
320-416 |
3.14e-18 |
|
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: 82.75 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 320 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ----ENLEQAFSVAERELGVTRLLD 395
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1655220517 396 PEDVDVAHPDEKSIITYVSSL 416
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
319-417 |
3.20e-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: 83.12 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1655220517 399 -VDVAHPDEKSIITYVSSLY 417
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1770-2624 |
9.05e-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: 91.67 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1770 EEAEKLRKQEEEANKAREQAEKELETWRLKANEALR---LRLRAEE-EAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAA 1845
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1846 LKQKENAEKELEKQRTFAEQIAQQ-KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1924
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 EMDALlQMKIQAEKVSQ-SNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED----------------EAA 1987
Cdd:TIGR02169 337 EIEEL-EREIEEERKRRdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkreldrlqEEL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1988 RQRAEAEKILKEKLAAINEA-TRLKTEAEVALKAKEAENERLKRQAED-EAYQRKLLEDQAAQHKhdIQEKITQLQSSsV 2065
Cdd:TIGR02169 416 QRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEYDR--VEKELSKLQRE-L 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2066 SELDRQKNIVEETLRQKKVVEEEI------------HIIRInferasKEKSDLEVEL---KKLKGIADETQ--------- 2121
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaQLGSV------GERYATAIEVaagNRLNNVVVEDDavakeaiel 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2122 -KSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVER---LKQKAAEANKLKDKAekeleKQ 2197
Cdd:TIGR02169 567 lKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKY-----RM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2198 VILAKEAAQKS---TAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAA 2274
Cdd:TIGR02169 642 VTLEGELFEKSgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2275 EDEAAK-QAKAQKDAERLRKEAEAEAAkraaaeaaaLKQKQEA-DAEMAKHKKEAEqalkqksqvEKELGLVKLQLDETD 2352
Cdd:TIGR02169 722 EKEIEQlEQEEEKLKERLEELEEDLSS---------LEQEIENvKSELKELEARIE---------ELEEDLHKLEEALND 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2353 KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlmqknKDNTQKLLAEEAEKMKSLAEE 2432
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE--------IQELQEQRIDLKEQIKSIEKE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2433 AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdk 2512
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-- 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2513 etqgfqKSLEAERKRQLEISAE---AEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekqttetvvqkLETQR 2589
Cdd:TIGR02169 934 ------SEIEDPKGEDEEIPEEelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE------------LKEKR 995
|
890 900 910
....*....|....*....|....*....|....*
gi 1655220517 2590 LQSTREADDLKKAIAELEKEREKLKRDAQELQNKS 2624
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREVFMEAFEAINEN 1030
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
319-422 |
1.21e-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: 81.63 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1655220517 399 VDV--AHPDEKSIITYVSSLYDVMPR 422
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1755-2633 |
1.35e-17 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 91.43 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1755 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqRKSLAQEEAEKQKTEAERD 1834
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEA------------RRSLASRPAYDGADIGYQA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1835 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqklsaeqeyirlkadfEHAEQQrglldnelQRLKNEVNAAEKQRRQ 1914
Cdd:NF041483 75 EQLLRNAQIQADQLRADAERELRDARAQTQRILQ----------------EHAEHQ--------ARLQAELHTEAVQRRQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1915 -LEDELAKVRSEMDALLQMKIQ-AEKVSQSNTEKSKQLL-ETEALKMKQLAEEAARLRSVAEEAkKQRQLAEDEAArqRA 1991
Cdd:NF041483 131 qLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEA-RQRLGSEAESA--RA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1992 EAEKILKeklaaineatRLKTEAEVALKAKEAENERLKRQAEdeayqrklledqaaqhkhdiqekitQLQSSSVSELDRQ 2071
Cdd:NF041483 208 EAEAILR----------RARKDAERLLNAASTQAQEATDHAE-------------------------QLRSSTAAESDQA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2072 KNIVEETLRQkkvveeeihiirinferASKEKSDLEVELKKLKGIADETqkskakaeeeaeklkklaaeeerKRREAEEK 2151
Cdd:NF041483 253 RRQAAELSRA-----------------AEQRMQEAEEALREARAEAEKV-----------------------VAEAKEAA 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2152 VKKIAAAEEEAARQRKAAQDEVERLKQKA--------AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQ------- 2216
Cdd:NF041483 293 AKQLASAESANEQRTRTAKEEIARLVGEAtkeaealkAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQlakaart 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2217 --DVLSKNKEDllSQEKLRDEFENAKKLAQaaetakEKAEKEAALLRQKAEEAEKLKKAAEDEA----AKQAKAQKDAER 2290
Cdd:NF041483 373 aeEVLTKASED--AKATTRAAAEEAERIRR------EAEAEADRLRGEAADQAEQLKGAAKDDTkeyrAKTVELQEEARR 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2291 LrkeaeaeaakraAAEAAALKQKQEADAEM--AKHKKEAEQALKQKSQVEKELgLVKLQLDETD-KQKALMDEELQRVKA 2367
Cdd:NF041483 445 L------------RGEAEQLRAEAVAEGERirGEARREAVQQIEEAARTAEEL-LTKAKADADElRSTATAESERVRTEA 511
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2368 qVNDAVKQKAQVENELSKVKMQMDELlklkvRIE-EENLRLMQKNKDNTQKLLAEEAE-----KMKSLAEEAARLSVEAE 2441
Cdd:NF041483 512 -IERATTLRRQAEETLERTRAEAERL-----RAEaEEQAEEVRAAAERAARELREETEraiaaRQAEAAEELTRLHTEAE 585
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2442 EtarQRKTAEAELAEQRALAEKMLKEkmqAIQEATKLKAE-AEELQKQKNQAQEKAKKLledkqeiqqRLDKETQGFQKS 2520
Cdd:NF041483 586 E---RLTAAEEALADARAEAERIRRE---AAEETERLRTEaAERIRTLQAQAEQEAERL---------RTEAAADASAAR 650
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2521 LEAE----RKRQlEISAEAEKLKlrvkelssaqAKAEEEATRFKKQADEAKVRLqETEKQTTETVVQKLETQRlqsTREA 2596
Cdd:NF041483 651 AEGEnvavRLRS-EAAAEAERLK----------SEAQESADRVRAEAAAAAERV-GTEAAEALAAAQEEAARR---RREA 715
|
890 900 910
....*....|....*....|....*....|....*....
gi 1655220517 2597 DD-LKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQE 2633
Cdd:NF041483 716 EEtLGSARAEADQERERAREQSEElLASARKRVEEAQAE 754
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
319-418 |
1.97e-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: 80.78 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1655220517 399 VDVA--HPDEKSIITYVSSLYD 418
Cdd:cd21261 83 MMVMgrKPDPMCVFTYVQSLYN 104
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
203-300 |
2.98e-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: 80.08 E-value: 2.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 203 KKTFTKWVNKHL-MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 278
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1655220517 279 RNDDI-ADGNPKLTLGLIWTIIL 300
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
319-417 |
4.46e-17 |
|
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: 80.13 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1655220517 399 -VDVAHPDEKSIITYVSSLY 417
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
321-419 |
1.05e-16 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 78.77 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 321 KLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPEDVD 400
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMA 87
|
90 100
....*....|....*....|
gi 1655220517 401 VAH-PDEKSIITYVSSLYDV 419
Cdd:cd21250 88 SAEePDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2173-2782 |
1.28e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 88.19 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2173 VERLKQKAAEANKLKDK--AEKELEKQVILA--------KEAAQKSTAAEQKAQDVLSKNKEDLLSQ-EKLRDEFENAKK 2241
Cdd:TIGR02168 202 LKSLERQAEKAERYKELkaELRELELALLVLrleelreeLEELQEELKEAEEELEELTAELQELEEKlEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2242 LAQAAETAkekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMA 2321
Cdd:TIGR02168 282 EIEELQKE----------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----------SKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2322 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSkvkmqmdELLKLKVRIE 2401
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-------RLEARLERLE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2402 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2481
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLEDKQEIQQRLD------KETQGFQKSLEA---------------ERKRQLEISAEAEKLKL 2540
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqavvvenlnAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2541 RVKELSSAQAKAEEEATRFKKQADEAKVRLQeTEKQTTETVVQKLETQRLQSTREADDL--------------------- 2599
Cdd:TIGR02168 574 TFLPLDSIKGTEIQGNDREILKNIEGFLGVA-KDLVKFDPKLRKALSYLLGGVLVVDDLdnalelakklrpgyrivtldg 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2600 -----------------------KKAIAELEKEREKLKRDAQELQNKSKEtASAQQEQMEQQKAMLQQTFLTEKELLLKR 2656
Cdd:TIGR02168 653 dlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2657 ERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2736
Cdd:TIGR02168 732 RKDLARLEAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2737 LLADENKKLREKLESLEVTSKQAASKTKEIEV--QTDKVPEEQLVSMT 2782
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDleEQIEELSEDIESLA 858
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1848-2733 |
1.69e-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: 87.82 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1848 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLL----DNELQRLKNEVNAAEKQRRQLEDELAKVR 1923
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1924 SEMDallQMKIQAEKVSQSNTEKsKQLLETEALKMKQLAEEaarlrsvaEEAKKQRQLAEDEAarQRAEAEKILKEKLAA 2003
Cdd:TIGR02169 251 EELE---KLTEEISELEKRLEEI-EQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2004 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVS------ELDRQKNIVEE 2077
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetrdELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2078 TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQkskakaeeeaeklkklaaeeeRKRREAEEKVKKIAA 2157
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---------------------EEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2158 AEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQeklrdefe 2237
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHGT-------- 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2238 nakkLAQaaetakekaekeaaLLRQKAEEAEKLKKAA----------EDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEA 2307
Cdd:TIGR02169 527 ----VAQ--------------LGSVGERYATAIEVAAgnrlnnvvveDDAVAKEAIELLKRRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2308 AALKQKQEADAEMA----KHKKEAEQALKQksqVEKELGLVklqlDETDKQKALMD---------EELQRVKAQVNDAVK 2374
Cdd:TIGR02169 589 DLSILSEDGVIGFAvdlvEFDPKYEPAFKY---VFGDTLVV----EDIEAARRLMGkyrmvtlegELFEKSGAMTGGSRA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2375 QKAQVENELSkvkmQMDELLKLKVRIEEenlrlMQKNKDNtqklLAEEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAE 2453
Cdd:TIGR02169 662 PRGGILFSRS----EPAELQRLRERLEG-----LKRELSS----LQSELRRIENRLDELsQELSDASRKIGEIEKEIEQL 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2454 LAEQRALAEKM--LKEKMQAIQEA-TKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERK 2526
Cdd:TIGR02169 729 EQEEEKLKERLeeLEEDLSSLEQEiENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2527 RQLEISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRlqstrEADDLKKAIAEL 2606
Cdd:TIGR02169 809 RIEARLREIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAALRDL 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2607 EKEREKLKRDAQELQNKSKETASAQQEQMEQ--QKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDE 2684
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2685 QQRQQKLMD---------EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLE 2733
Cdd:TIGR02169 961 QRVEEEIRAlepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2405-2770 |
2.61e-16 |
|
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: 86.72 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2405 LRLMQKNKDNTQKLLAEEAEKMkslaeEAARLSVEAEETARQ----RKTAEAELAEQRALaekmlkEKMQAIQeatklkA 2480
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKM-----EQERLRQEKEEKAREverrRKLEEAEKARQAEM------DRQAAIY------A 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2481 EAEELqkqknqAQEKAKKLLEDKQEIQQRldketqgfqkslEAERKRQLEISAEAEklklRVKELSSAQAKAEEEATRFK 2560
Cdd:pfam17380 338 EQERM------AMERERELERIRQEERKR------------ELERIRQEEIAMEIS----RMRELERLQMERQQKNERVR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2561 KQADEA-KVRLQETEKQtTETVVQKLETQRLQSTREaDDLKKAIAELEKEREK-LKRDAQELQNKSKETASAQQEQMEQQ 2638
Cdd:pfam17380 396 QELEAArKVKILEEERQ-RKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAReMERVRLEEQERQQQVERLRQQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2639 KAMLQQtfltEKElllKRERDVEDEKKKlqKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQ-AIMDEavKKQKEAEAEm 2717
Cdd:pfam17380 474 RKKLEL----EKE---KRDRKRAEEQRR--KILEKELEERKQAMIEEERKRKLLEKEMEERQkAIYEE--ERRREAEEE- 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2718 KNKQKEMEalEKKRLEQEKLLADENkklREKLESLEVTS------KQAASKTKEIEVQT 2770
Cdd:pfam17380 542 RRKQQEME--ERRRIQEQMRKATEE---RSRLEAMERERemmrqiVESEKARAEYEATT 595
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1387-1929 |
3.97e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.27 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1387 LREARLRQEKIEAApVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqilayRALQDPIASPLKK 1466
Cdd:PRK03918 216 LPELREELEKLEKE-VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI------EELEEKVKELKEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1467 PKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmAEIQAQLETQKQLAEGHAKS 1546
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-KELEKRLEELEERHELYEEA 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1547 VAKAElEAQELKLKMKEDASQR-QGLAVDAEKQKQNIQLE---LTQLKNLSEQEIRSKNQQLEEAQVSRRKLeeeihlir 1622
Cdd:PRK03918 368 KAKKE-ELERLKKRLTGLTPEKlEKELEELEKAKEEIEEEiskITARIGELKKEIKELKKAIEELKKAKGKC-------- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1623 iqlqTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkKKNAEDELKRKSE--AEKEAARQKQKALD 1700
Cdd:PRK03918 439 ----PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE----LRELEKVLKKESEliKLKELAEQLKELEE 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1701 ELQKHkmQAEEAERRLKQAEEEKVRQIKVVEEVaqktaatqlqamsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEE 1780
Cdd:PRK03918 511 KLKKY--NLEELEKKAEEYEKLKEKLIKLKGEI------------------KSLKKELEKLEELKKKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1781 EankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK-- 1858
Cdd:PRK03918 571 E----LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEElr 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1859 ------QRTFAEQ----IAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDeLAKVRSEMDA 1928
Cdd:PRK03918 647 keleelEKKYSEEeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEE 725
|
.
gi 1655220517 1929 L 1929
Cdd:PRK03918 726 L 726
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2328-2745 |
5.64e-16 |
|
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: 85.54 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2328 EQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDEL---LKLKVRIEEEN 2404
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVvteFEATTCSLEEL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2405 LRLMQKNKDNTQkllaeeaEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaeKMLKEKMQAIQEATKLKAEAEE 2484
Cdd:pfam05483 365 LRTEQQRLEKNE-------DQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEKLLDEKKQFEKIAEE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2485 LQKQKN------QAQEKAKKLLEDKQEI----QQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSA------ 2548
Cdd:pfam05483 434 LKGKEQelifllQAREKEIHDLEIQLTAiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtl 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2549 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK-----EREKLKRDAQ----- 2618
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEnarsiEYEVLKKEKQmkile 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2619 --------ELQNKSKETASAQQEQME-QQKAMLQQTFLTEKELLL-KRERDVEDEKKKLQKHLEdevNKAKALKDEQQRQ 2688
Cdd:pfam05483 594 nkcnnlkkQIENKNKNIEELHQENKAlKKKGSAENKQLNAYEIKVnKLELELASAKQKFEEIID---NYQKEIEDKKISE 670
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2689 QKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEAL-EKKRLEQEKLLADENKKL 2745
Cdd:pfam05483 671 EKLL-EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmEKHKHQYDKIIEERDSEL 727
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
322-417 |
6.63e-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: 76.63 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 322 LLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDPED-VD 400
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1655220517 401 VAHPDEKSIITYVSSLY 417
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
199-298 |
6.82e-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: 76.42 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 199 DRVQKKTFTKWVNKHLMKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 273
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1655220517 274 KLVNIRNDDIADGNPKLTLGLIWTI 298
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1895-2747 |
7.15e-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: 85.50 E-value: 7.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1895 DNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiqaekvsqsNTEKSKQLLETEALKMKQLAEEAARLRSVaEE 1974
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERL-------------RREREKAERYQALLKEKREYEGYELLKEK-EA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1975 AKKQRQLAEDEAARQRAEAEKIlKEKLAAINEatrlktEAEVALKAKEAENERLKRQAEDE--AYQRKLledqaaqhkHD 2052
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKL-TEEISELEK------RLEEIEQLLEELNKKIKDLGEEEqlRVKEKI---------GE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2053 IQEKITQLQSSsVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAE 2132
Cdd:TIGR02169 299 LEAEIASLERS-IAEKERELEDAEERLAK---LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 KLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA-NKLKDKAEKELEKQVILaKEAAQKSTAA 2211
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEK-EDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2212 EQKaqdvLSKNKEDLlsqEKLRDEFENAKKLAQAAETAKEKaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAE-- 2289
Cdd:TIGR02169 454 EWK----LEQLAADL---SKYEQELYDLKEEYDRVEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKas 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2290 ---------RLRKEAEAEAAKRAAAEAAALKQKQEADAEMAkhkKEAEQALKQ-KSQVEKELGLVKLQLDETDKQKALMD 2359
Cdd:TIGR02169 520 iqgvhgtvaQLGSVGERYATAIEVAAGNRLNNVVVEDDAVA---KEAIELLKRrKAGRATFLPLNKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2360 E------ELQRVKAQVNDAVKQKAQ---VENELSKVKMQMDEL-------------------------LKLKVRIEEENL 2405
Cdd:TIGR02169 597 GvigfavDLVEFDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYrmvtlegelfeksgamtggsraprgGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2406 RLMQKNKDNTQKLLA---EEAEKMKSLAEEA-ARLSVEAEETARQRKTAEAELAEQRALAEKM--LKEKMQAIQEA-TKL 2478
Cdd:TIGR02169 677 QRLRERLEGLKRELSslqSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQEEEKLKERLeeLEEDLSSLEQEiENV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2479 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD----KETQGFQKSLEAERKRQLEISAEAEKlklRVKELSSAQAKAEE 2554
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQ---KLNRLTLEKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQELQNKSKEtasaQQEQ 2634
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-----EELEELEAALRDLESRLGDLKKERDELEAQLRE----LERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2635 MEQQKAMLQQTFLTEKELLLKRErDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQAIMDEAVKKQKE 2712
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELqrVEEEIRALEPVNMLAIQEYEE 983
|
890 900 910
....*....|....*....|....*....|....*
gi 1655220517 2713 AEAEMKNKQKEMEALEKKRLEQEKLLADENKKLRE 2747
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2315-2685 |
8.83e-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: 85.12 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2315 EADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLD--ETDKQKALMDEELQRVK---------AQVNDAVKQKAQVENEL 2383
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKreyegyellKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2384 SKVKmqmDELLKLKVRIEEENLRLMQKNKDntqkllaeeaekmksLAEEAARLSVEAEETARQRKTAEAELAEQRALAEK 2463
Cdd:TIGR02169 247 ASLE---EELEKLTEEISELEKRLEEIEQL---------------LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2464 MLKEKMQaiqeatklkaEAEELQKQKNQAQEKAKKLLEDKQEiqqrldketqgFQKSLEAERKRQLEISAEAEKLKlrvK 2543
Cdd:TIGR02169 309 SIAEKER----------ELEDAEERLAKLEAEIDKLLAEIEE-----------LEREIEEERKRRDKLTEEYAELK---E 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2544 ELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTR-----EADDLKKAIAELEKEREKLKRDAQ 2618
Cdd:TIGR02169 365 ELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELqrlseELADLNAAIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2619 ELQNKSKEtasaQQEQMEQQKAMLQQtflTEKELLLKRE--RDVEDEKKKLQKHLEDEVNKAKALKDEQ 2685
Cdd:TIGR02169 445 DKALEIKK----QEWKLEQLAADLSK---YEQELYDLKEeyDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1587-2119 |
8.96e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.09 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1587 TQLKNLSEqEIRSKNQQLEEAQVSRRKLEE--EIHLIRIQLQTTIKQkstaddELQKLRDQAAEAEKVRKAAQEEAERLR 1664
Cdd:PRK02224 213 SELAELDE-EIERYEEQREQARETRDEADEvlEEHEERREELETLEA------EIEDLRETIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1665 KQVNEETQKKKNAEDELKRkSEAEKEAARQKQKALDElqkhkmQAEEAERRLkqaeeekvrqikvvEEVAQKTAATQLQA 1744
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGL-DDADAEAVEARREELED------RDEELRDRL--------------EECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1745 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEaqRKSLAQEEA 1824
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--LEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1825 EKQKTEAERDAKKkakaeeaalkqkENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNE 1904
Cdd:PRK02224 423 ELREREAELEATL------------RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1905 VNAAEKQRRQLEDeLAKVRSEMDALLQmkiQAEKVSQSNTEKsKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED 1984
Cdd:PRK02224 491 VEEVEERLERAED-LVEAEDRIERLEE---RREDLEELIAER-RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1985 EAARQRAEAeKILKEKLAAINEA-TRLKTEAEVALKAKEAE------NERLKRQAEdeayqrklLEDQAAQHKHDIQEKI 2057
Cdd:PRK02224 566 EAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEdeierlREKREALAE--------LNDERRERLAEKRERK 636
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2058 TQLQS----SSVSELDRQKNIVEETLRQkkvVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2119
Cdd:PRK02224 637 RELEAefdeARIEEAREDKERAEEYLEQ---VEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1287-2122 |
1.52e-15 |
|
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: 84.64 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1287 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhyrqlagSLLERWQAVFAQIDLRQREL 1366
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-------LQEEELKLLAKEEEELKSEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1367 SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQiencqkdakayidslkdy 1446
Cdd:pfam02463 303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL------------------ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1447 efQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRyselstlTSQYIKFILETQRRLEDDEKaseklkeDEKKRM 1526
Cdd:pfam02463 365 --QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE-------EEKEAQLLLELARQLEDLLK-------EEKKEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1527 AEIQAQLETQKQLAEGHAKSVaKAELEAQELKLKMKEdasqrqglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEE 1606
Cdd:pfam02463 429 LEILEEEEESIELKQGKLTEE-KEELEKQELKLLKDE----------LELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1607 AQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE 1686
Cdd:pfam02463 498 RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGA 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1687 AEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvl 1766
Cdd:pfam02463 578 RKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSL--- 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1767 qLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAL 1846
Cdd:pfam02463 655 -EEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1847 KQKENAEKELEKQRTFAEQ--IAQQKLSAEQEYIRLKADFEHAEQQRglldNELQRLKNEVNAAEKQRRQLEDELAKVRS 1924
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEekSRLKKEEKEEEKSELSLKEKELAEER----EKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 EMDALLQMKIQAEKVSQSN---TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKL 2001
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEkikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2002 AAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSsvseldrQKNIVEETLRQ 2081
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE-------ENNKEEEEERN 962
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1655220517 2082 KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQK 2122
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2324-2766 |
1.57e-15 |
|
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: 83.92 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2324 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV----R 2399
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2400 IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLK 2479
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2480 AEAEELQKQknqaqekakklLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELssaqakaEEEATRF 2559
Cdd:TIGR04523 391 SQINDLESK-----------IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL-------TNQDSVK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2560 KKQADEAKVRLQETEKQTTETvvqKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK 2639
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVL---SRSINKIKQNLE--QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2640 AMlqQTFLTEKELLLKrerDVEDEKKKLqkhleDEVNKAKALKDEQQRQQKLMDE---EKKKLQAIMDEAVKKQKEAEAE 2716
Cdd:TIGR04523 528 KL--ESEKKEKESKIS---DLEDELNKD-----DFELKKENLEKEIDEKNKEIEElkqTQKSLKKKQEEKQELIDQKEKE 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2717 MKNKQKEMEALEKKRLEQEKLLADENKKlREKLESLEVTSKQAASKTKEI 2766
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQE 646
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1490-2390 |
1.87e-15 |
|
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: 84.07 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1490 LSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKK----------RMAEIQAQLETQK-QLA---------------EGH 1543
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKlegestdlqeQIAELQAQIAELRaQLAkkeeelqaalarleeETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1544 AKSVA-KAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSE---------QEIRSKNQQleEAQVSRRK 1613
Cdd:pfam01576 258 QKNNAlKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdtldttaaqQELRSKREQ--EVTELKKA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1614 LEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA----AEAEKVRKAAQEEAERLRKQVN-------EETQKKKNAEDELK 1682
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAkrnkANLEKAKQALESENAELQAELRtlqqakqDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsEKTTKLEESLKkeq 1762
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE--ETRQKLNLSTR--- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1763 gtVLQLQEEAEKLRKQEEEANKAREQAEKELETWR----------------LKANEALRLRLRAEEEAQRKSLAQEEAEK 1826
Cdd:pfam01576 491 --LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlsdmkkkleedagtLEALEEGKKRLQRELEALTQQLEEKAAAY 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 QKTEA--ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQ---EYIRLKADFEHAEQQRGLLDNELQRL 1901
Cdd:pfam01576 569 DKLEKtkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARyaeERDRAEAEAREKETRALSLARALEEA 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1902 KNEVNAAEKQRRQLedelakvRSEMDALLQMKIQAEKvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKkqrql 1981
Cdd:pfam01576 649 LEAKEELERTNKQL-------RAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAK----- 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1982 aedeaarqraeaekilkeklaaineaTRLkteaEVALKAKEAENERlKRQAEDEayqrklledQAAQHKHDIQEKITQLQ 2061
Cdd:pfam01576 716 --------------------------LRL----EVNMQALKAQFER-DLQARDE---------QGEEKRRQLVKQVRELE 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2062 SssvsELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEE 2141
Cdd:pfam01576 756 A----ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKES 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2142 ERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKlkDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSK 2221
Cdd:pfam01576 832 EKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGAS--GKSALQDEKRRLEARIAQLEEELEEEQSNTELLN 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2222 NKEDLLSQ--EKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE--AAKQAKAQKDAERLRKEAEA 2297
Cdd:pfam01576 910 DRLRKSTLqvEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSsiAALEAKIAQLEEQLEQESRE 989
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2298 EAAKRAAAEAAALKQKqEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKA 2377
Cdd:pfam01576 990 RQAANKLVRRTEKKLK-EVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNE 1068
|
970
....*....|...
gi 1655220517 2378 QVENELSKVKMQM 2390
Cdd:pfam01576 1069 SMNREVSTLKSKL 1081
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1483-2411 |
2.85e-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: 83.56 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1483 LRTRYSELSTLTsQYIKfILETQRRLEDDEK-------ASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1555
Cdd:TIGR00606 171 LKQKFDEIFSAT-RYIK-ALETLRQVRQTQGqkvqehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1556 ELKLKMKEDASQRQGLavdaekqkQNIQLELTQLKNlSEQEIRSKNQQLEEAQVS-RRKLEEEIHLIRIQLQTTIKQKSt 1634
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKI--------MKLDNEIKALKS-RKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKE- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 addelQKLRDQAAEAEKVRKAA----QEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1710
Cdd:TIGR00606 319 -----RELVDCQRELEKLNKERrllnQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1711 EAERRLKQAEEEKVRQI-KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1789
Cdd:TIGR00606 394 NFHTLVIERQEDEAKTAaQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1790 EKELETWRlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqKENAEKELEKQ-RTFAEQIAQ 1868
Cdd:TIGR00606 474 LELDQELR----KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLD-------QEMEQLNHHTTtRTQMEMLTK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1869 QKLSAEQEYIRLKAdfEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1946
Cdd:TIGR00606 543 DKMDKDEQIRKIKS--RHSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1947 SKQLLET--EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR-LKTEAEVALKAKEA 2023
Cdd:TIGR00606 621 LSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2024 ENERLKRQAEDEAYQRKLLEDQAAQH----KHDIQEKITQLQSSSVSEL-DRQKNIVEETLRQKKVVEE-EIHIIRINFE 2097
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDemlgLAPGRQSIIDLKEKEIPELrNKLQKVNRDIQRLKNDIEEqETLLGTIMPE 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2098 RASKEksDLEVELKKLKGIADETQKSKAKAEEEAEKL-----KKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2172
Cdd:TIGR00606 781 EESAK--VCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2173 VERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2252
Cdd:TIGR00606 859 IQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2253 AEKEAALLRQKAEEAEKLKKAAEDeaakqaKAQKDAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALK 2332
Cdd:TIGR00606 939 AQDKVNDIKEKVKNIHGYMKDIEN------KIQDGKDD---------------------YLKQKETELNTVNAQLEECEK 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2333 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKaqVNDAVKqkaQVENELSKVKMQMDELLKLKVRIE----EENLRLM 2408
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELK---EVEEELKQHLKEMGQMQVLQMKQEhqklEENIDLI 1066
|
...
gi 1655220517 2409 QKN 2411
Cdd:TIGR00606 1067 KRN 1069
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2312-2767 |
3.42e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2312 QKQEADAEMAKHkkeaEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQV-------NDAVKQKAQVENELS 2384
Cdd:PRK02224 235 TRDEADEVLEEH----EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLeeleeerDDLLAEAGLDDADAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2385 KVKMQMDELLKLKVRIEE--ENLRLMQKNKDNTQKLLAEEAEKMKSLA----EEAARLSVEAEETARQRKTAEAELAEQR 2458
Cdd:PRK02224 311 AVEARREELEDRDEELRDrlEECRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESELEEAREAVEDRREEIEELE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2459 ALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2538
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2539 ---KLRVKELSSAQAKAEEEATRFKKQADEAKvRLQETEKQttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKR 2615
Cdd:PRK02224 471 eedRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDR-----IERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2616 DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL-LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2694
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAeLKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2695 EKKKLQAimdeavKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:PRK02224 625 RRERLAE------KRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE 691
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1935-2671 |
3.58e-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: 83.09 E-value: 3.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1935 QAEKVSQSNTEKSKQLLEtEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEA 2014
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2015 EVALKAKEAENERLKRQAEdEAYQRKLLEDQAAQHKHDIQEKITQLQ--SSSVSELDRQKNIVEETLRQKKVVEEEIHII 2092
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARIEELRAQEAvlEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2093 RINFERASKEKSdLEVELKKLKGIAdeTQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDE 2172
Cdd:TIGR00618 311 RIHTELQSKMRS-RAKLLMKRAAHV--KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2173 VERLKQKAAEANKLKDKAEKELEKQvilakEAAQKSTAAEQkaQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEK 2252
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQATI-----DTRTSAFRDLQ--GQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2253 AEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAaeaaaLKQKQEADAEMAKHKKEAEQALK 2332
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-----PNPARQDIDNPGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2333 QKSQVEKELGLVKLQLDETDKQKALMDEELQRVK------AQVNDAVKQKAQ-VENELSKVKMQMDELLKLKVRIEEENL 2405
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQqsfsilTQCDNRSKEDIPnLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2406 RLMQK--NKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR--------KTAEAELAEQRALAEKMLKEKMQAI--- 2472
Cdd:TIGR00618 616 ALLRKlqPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehalsiRVLPKELLASRQLALQKMQSEKEQLtyw 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2473 -----QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgFQKSLEAERKRQLEISAEAEK---LKLRVKE 2544
Cdd:TIGR00618 696 kemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 LSSAQ-AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnK 2623
Cdd:TIGR00618 775 QTGAElSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL-K 853
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2624 SKETASAQQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHL 2671
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL----SDKLNGINQIKIQFDGDALIKFL 897
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4200-4238 |
3.74e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.74e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 4200 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNQIL 4238
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1785-2586 |
4.44e-15 |
|
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: 82.86 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1785 AREQAEKELETWRLKANEaLRLRLRAEEEAQ-------RKSLAQEEAEKQKTEAERDA-----KKKAKAEEAALKQKENA 1852
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKD-LQRRLNESNELHekqkfylRQSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1853 EKELEKQRTFAE-----------QIAQQKLSAE---QEYIRLKADFEHAEQQRGLLDNELQRL--KNEVNAAEKQRRQLE 1916
Cdd:pfam15921 151 VHELEAAKCLKEdmledsntqieQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1917 DELAKVRSEM----DALLQMKIQA----EKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAAR 1988
Cdd:pfam15921 231 TEISYLKGRIfpveDQLEALKSESqnkiELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1989 QRAEAEKILKEKLAAINEatrLKTEAEVALKAKEAENERLKRQ---AEDEAYQRKLLEDQAAQHKHDIQEkitQLQSSSV 2065
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDD---QLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2066 SELDRQKNIVEETLRQKKVVEEEIHiIRINFERASKEKSDLEVELKKLKGIAdETQKSkakaeeeaeklkklaaeeerkr 2145
Cdd:pfam15921 385 DLHKREKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKS---------------------- 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2146 reaeekvkkiaAAEEEAARQRKAAQDEVERLKQKAAEANKLkdKAEKELEKQVIlAKEAAQKST--AAEQKAQDVLSKNK 2223
Cdd:pfam15921 441 -----------ECQGQMERQMAAIQGKNESLEKVSSLTAQL--ESTKEMLRKVV-EELTAKKMTleSSERTVSDLTASLQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2224 EDLLSQEKLRDEFENAKKLAQAaetakekaekeaallrqKAEEAEKLKKaaEDEAAKQAKAQKDAERLrkeaeaeAAKRA 2303
Cdd:pfam15921 507 EKERAIEATNAEITKLRSRVDL-----------------KLQELQHLKN--EGDHLRNVQTECEALKL-------QMAEK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2304 AAEAAALKQKQEADAEM-AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvenE 2382
Cdd:pfam15921 561 DKVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL---------E 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2383 LSKVKM--QMDELLKLKVRIEEENLRLMQKNKDNTQKL--LAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQ 2457
Cdd:pfam15921 632 LEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2458 RALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKETQgFQKSLEAERKRQLE-ISAEAE 2536
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL----EEAMTNANKEKH-FLKEEKNKLSQELStVATEKN 786
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2537 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQE----TEKQTTETVVQKLE 2586
Cdd:pfam15921 787 KMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKLQ 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1967-2753 |
5.01e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.81 E-value: 5.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1967 RLRSVAE-EAKKQRQLAEDEAARQR-AEAEKILKEKlaaINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLED 2044
Cdd:TIGR02169 161 EIAGVAEfDRKKEKALEELEEVEENiERLDLIIDEK---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2045 QAAQHKHDIQEKITQLQSSSVSELDRQKNIV-------EETLRQKKVVEEEIHIIRinferasKEKSDLEVELKKLKGIA 2117
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEeieqlleELNKKIKDLGEEEQLRVK-------EKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2118 DETQkskakaeeeaeklkklaaeeerkrreaeEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELekq 2197
Cdd:TIGR02169 311 AEKE----------------------------RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY--- 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2198 vilaKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2277
Cdd:TIGR02169 360 ----AELKEELEDLRAELEEVDKEFAE---TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2278 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE---ADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQ 2354
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2355 KALMDEELQRVKAQVNDAVKQKAQ-----------------VENELskVKMQMDELLKL------------KVRIEEENL 2405
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLGSVGERyataievaagnrlnnvvVEDDA--VAKEAIELLKRrkagratflplnKMRDERRDL 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2406 RLMQKNK---------DNTQK------------LLAEEAEKMKSLAEEAARLSVEAE------------ETARQR----K 2448
Cdd:TIGR02169 591 SILSEDGvigfavdlvEFDPKyepafkyvfgdtLVVEDIEAARRLMGKYRMVTLEGElfeksgamtggsRAPRGGilfsR 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2449 TAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQkqknQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2528
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2529 LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEK 2608
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2609 EREKLKRDAQELQNKSKETASaqQEQMEQQKAMLQQTFLTEKELLLKR----ERDVEDEKKKLQKHLEDEVNKAKALKDE 2684
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKE--QIKSIEKEIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLRELERK 904
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2685 QQrQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAdENKKLREKLESLE 2753
Cdd:TIGR02169 905 IE-ELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIRALE 971
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1574-1985 |
5.18e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.12 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1574 DAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIR--IQLQTTIKQKSTADDELQKLRDQAAEAEK 1651
Cdd:COG4717 75 ELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1652 VRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ------AEEEKVR 1725
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEeleeleEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1726 QIKVVEEVAQKTAATQLQAMSFS---------------------------EKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1778
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlflvlGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1779 EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEK 1858
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1859 QRTFAEqiAQQKLSAEQEYIRLKADFEHAEQQRGLLDN---ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLqmkiq 1935
Cdd:COG4717 394 AEEYQE--LKEELEELEEQLEELLGELEELLEALDEEEleeELEELEEELEELEEELEELREELAELEAELEQLE----- 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1936 aekvSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDE 1985
Cdd:COG4717 467 ----EDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
317-417 |
5.81e-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: 73.95 E-value: 5.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 396
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1655220517 397 ED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1575-1905 |
7.44e-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: 81.71 E-value: 7.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1575 AEKQKQNiqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRDQAAEAEKVRK 1654
Cdd:pfam17380 285 SERQQQE------KFEKMEQERLRQEKEEKAREVERRRKLEE--------------AEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1655 AAQEEAERLRkqvneetQKKKNAEDELKRKSEAEKEAARQKQkaLDELQKHKMQAE-------EAERRLKQAEEEKVRQI 1727
Cdd:pfam17380 345 ERERELERIR-------QEERKRELERIRQEEIAMEISRMRE--LERLQMERQQKNervrqelEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQGTV----LQLQEEAEKLRKQEEEANKAREQAEKELETwRLKANEA 1803
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEAR--QREVRRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1804 LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkKAKAEEAALKQKENAEKELEKQRTFAE--QIAQQKLSAEQEYIRLK 1881
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEKEME---ERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLE 569
|
330 340
....*....|....*....|....
gi 1655220517 1882 ADFEHAEQQRGLLDNELQRLKNEV 1905
Cdd:pfam17380 570 AMEREREMMRQIVESEKARAEYEA 593
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
202-302 |
9.31e-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: 73.10 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNKHLMK--AQRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 273
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1655220517 274 KLVNIRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1502-1782 |
1.35e-14 |
|
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: 80.94 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQR-RLEDDEKASE-----KLKEDEKKRmaeiQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR---QGLA 1572
Cdd:pfam17380 296 MEQERlRQEKEEKAREverrrKLEEAEKAR----QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERirqEEIA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1573 VDAEKQKQ--NIQLELTQLKNLSEQEIRS-KNQQLEEAQVSRRKLEEEIHLIRIQLQttikQKSTADDELQKLRDQAA-E 1648
Cdd:pfam17380 372 MEISRMREleRLQMERQQKNERVRQELEAaRKVKILEEERQRKIQQQKVEMEQIRAE----QEEARQREVRRLEEERArE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1649 AEKVRKAAQE-----------EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK 1717
Cdd:pfam17380 448 MERVRLEEQErqqqverlrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQK 527
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1718 QAEEEKVRQIKVVEEVAQKTAA----TQLQAMSFSEKTTKLeESLKKEQGTVLQLQeEAEKLRKQEEEA 1782
Cdd:pfam17380 528 AIYEEERRREAEEERRKQQEMEerrrIQEQMRKATEERSRL-EAMEREREMMRQIV-ESEKARAEYEAT 594
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2153-2760 |
1.77e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2153 KKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKL 2232
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2233 RDEFENAKKLAQAAETAKEKAEKEAALlRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEaeaeaakraaaeaaaLKQ 2312
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE---------------ING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2313 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDE-----------ELQRVKAQVNDAVKQKAQVEN 2381
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkrltglTPEKLEKELEELEKAKEEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2382 ELSKVKmqmDELLKLKVRIEEENLRLMQKNK--------------DNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQR 2447
Cdd:PRK03918 406 EISKIT---ARIGELKKEIKELKKAIEELKKakgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2448 KTAEAELAEQRAL-AEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKLLEDKQEIqqrldketqgfqKSLEAERK 2526
Cdd:PRK03918 483 RELEKVLKKESELiKLKELAEQLKELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEI------------KSLKKELE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2527 RQLEISAEAEKLKLRVKELSSAQAKAEEEATRFK-KQADEAKVRLQETEKqttetvvqkletqrlqSTREADDLKKAIAE 2605
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEP----------------FYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2606 LEKEREKLKRDAQELQNKSKETASAQQEqMEQQKAMLQQtfltekellLKRERDVEDEKKKLQKHLEDEvNKAKALKDEQ 2685
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKR-LEELRKELEE---------LEKKYSEEEYEELREEYLELS-RELAGLRAEL 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2686 QRQQKLMDEEKKKLqaimdeavKKQKEAEAEMKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAA 2760
Cdd:PRK03918 683 EELEKRREEIKKTL--------EKLKEELEEREKAKKELEKLEKAL--------ERVEELREKVKKYKALLKERA 741
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3217-3255 |
1.87e-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: 1.87e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 3217 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPELHEQL 3255
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
317-417 |
2.57e-14 |
|
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: 71.98 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAErELGVTRLLDP 396
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1655220517 397 ED-VDVAHPDEKSIITYVSSLY 417
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2350-2767 |
3.92e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2350 ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEENLRLMQKNKDNTQKLLAEEAEK---M 2426
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2427 KSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQaqekakkLLEDKQEI 2506
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREE-------LEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2507 QQRLDKE---TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQ 2583
Cdd:PRK02224 327 RDRLEECrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2584 --KLETQRLQSTREADDLKKAIAELEKEREKLK---RDAQELQNKSK--------------ETASAQQEQMEQQKAMLQQ 2644
Cdd:PRK02224 407 lgNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELED 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2645 TFLTEKELLLKRER-----DVEDEKKKLQ---KHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE 2716
Cdd:PRK02224 487 LEEEVEEVEERLERaedlvEAEDRIERLEerrEDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2717 MKNKQKEMEALEKKRleqekllaDENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:PRK02224 567 AEEAREEVAELNSKL--------AELKERIESLERIRTLLAAIADAEDEIE 609
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2449-2785 |
4.09e-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: 79.73 E-value: 4.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2449 TAEAELAEQRALAE-KMLKEKMQAIQEATK-LKAEAEELQKQKNQAqEKAKKLLEDKQEIQQR-LDKETQGFQKSLEAER 2525
Cdd:TIGR02169 165 VAEFDRKKEKALEElEEVEENIERLDLIIDeKRQQLERLRREREKA-ERYQALLKEKREYEGYeLLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2526 KRQLEISAEAEKLKL----RVKELSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKK 2601
Cdd:TIGR02169 244 RQLASLEEELEKLTEeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE-KIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2602 AIAELEKEREKLKRDAQELqnksketaSAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEV 2675
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEEL--------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdelKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2676 NKAKALKDEQQRQQKLMDEEKKKL---QAIMDEAVK----KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK---L 2745
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLseeLADLNAAIAgieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydL 474
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655220517 2746 REKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTTVE 2785
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1648-2342 |
4.70e-14 |
|
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: 79.63 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1648 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEA-ARQKQKALDELQKHKMQAEEAERrlKQAEEEKVRQ 1726
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAeLLTLRSQLLTLCTPCMPDTYHER--KQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1727 IKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL 1806
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1807 RLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENA-EKELEKQRTFAEQIAQQKlSAEQEYIRLKADFE 1885
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHiRDAHEVATSIREISCQQH-TLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1886 HAEQQRGLLDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ---LLETEALKMK 1959
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQREQATIDTRtsaFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQESAQSLK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1960 QLAEEAARLRSVAEEAKKQRQLAEDEAARQrAEAEKILKEKLAAINEA----------TRLKTEAEVALKAKEAENERLK 2029
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLEL-QEEPCPLCGSCIHPNPArqdidnpgplTRRMQRGEQTYAQLETSEEDVY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2030 RQAEDEAYQRKLLEDQAAQHKHDIQeKITQLQSSSVSELDRQKNIVEETLrqkKVVEEEIHIIRINFERASKEKSDLEVE 2109
Cdd:TIGR00618 549 HQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQ---DLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2110 LKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAE-EEAARQRKAAQDEVERLKQKAAEANKLKD 2188
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2189 KAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKK-------------------------LA 2243
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKarteahfnnneevtaalqtgaelshLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2244 QAAETAKEKAEKEAALLRQKaeEAEKLKKAAEDEAAKQAKAQKDAERLrkEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2323
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
730
....*....|....*....
gi 1655220517 2324 KKEAEQALKQKSQVEKELG 2342
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKLN 879
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
317-414 |
5.48e-14 |
|
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: 70.87 E-value: 5.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1655220517 396 PEDVDVAHPDEKSIITYVS 414
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1503-2060 |
5.88e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLK--EDEKKRMAEIQAQLETQKQLAEGHAksVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1580
Cdd:COG4913 239 RAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 NIQLELTQLKNLSEQEIRSKNQQLEEaqvsrrkLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1660
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM----QAEEAERRLKQA---EEEKVR------QI 1727
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRDALAEAlglDEAELPfvgeliEV 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQK-------TAATQL--------QAMSFSEKTT--------KLEESLKKEQGTVLQLQEEAEKLrkqEEEANK 1784
Cdd:COG4913 470 RPEEERWRGaiervlgGFALTLlvppehyaAALRWVNRLHlrgrlvyeRVRTGLPDPERPRLDPDSLAGKL---DFKPHP 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1785 AREQAEKEL--------------------------------------------ETWRL-KANEALRLRLRAEEEAQRKSL 1819
Cdd:COG4913 547 FRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirSRYVLgFDNRAKLAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1820 AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQqklsAEQEYIRLKA---DFEHAEQQrglldn 1896
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAE----LEAELERLDAssdDLAALEEQ------ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1897 eLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK 1976
Cdd:COG4913 694 -LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1977 KQRQLAEDEAARQRAEAEKILKE--------------KLAAINE-ATRLKTEAEVALKAKEAENERLKRQAEDEayQRKL 2041
Cdd:COG4913 773 ERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEyLALLDRLEEDGLPEYEERFKELLNENSIE--FVAD 850
|
650
....*....|....*....
gi 1655220517 2042 LEDQAAQHKHDIQEKITQL 2060
Cdd:COG4913 851 LLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1394-1975 |
9.78e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.54 E-value: 9.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1394 QEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAkayidslkdyefqilayralqdpiasplkkpkmesas 1473
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA------------------------------------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1474 DNIIQEYvtlRTRYSELSTLTsqyikfilETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE 1553
Cdd:PRK02224 240 DEVLEEH---EERREELETLE--------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1554 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1633
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1634 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELK--RKSEAEKEAARQKQKA------------L 1699
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRtaRERVEEAEALLEAGKCpecgqpvegsphV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1700 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1779
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1780 EEankareqAEKELETWRLKANEAlrlRLRAEEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALkqkENAEKELEKQ 1859
Cdd:PRK02224 547 AE-------LEAEAEEKREAAAEA---EEEAEEAREE--VAELNSKLAELKERIESLERIRTLLAAI---ADAEDEIERL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1860 RTFAEQIAQQKlsaEQEYIRLKADFEHAEQQRGLLDNE-LQRLKNEVNAAEKQRRQLEDELAKVRSEMDAlLQMKIQAek 1938
Cdd:PRK02224 612 REKREALAELN---DERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDD-LQAEIGA-- 685
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220517 1939 vsqsnTEKSKQLLETEALKMKQLAEEAARLRSVAEEA 1975
Cdd:PRK02224 686 -----VENELEELEELRERREALENRVEALEALYDEA 717
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1503-2012 |
1.09e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKED----EKKRMA---EIQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlavDA 1575
Cdd:PRK02224 248 ERREELETLEAEIEDLRETiaetEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDAD-----AEAVEARRE---EL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLELTQlknlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRiqlqttiKQKSTADDELQKLRDQAAEAEKVRKA 1655
Cdd:PRK02224 320 EDRDEELRDRLEE----CRVAAQAHNEEAESLREDADDLEERAEELR-------EEAAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaEKEAARQKQKALD-ELQKHKMQAEEAERRLKQAE----EEKVRQIKVV 1730
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELRE-ERDELREREAELEaTLRTARERVEEAEALLEAGKcpecGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKtaatqlqamsfSEKTTKLE---ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1807
Cdd:PRK02224 468 ETIEED-----------RERVEELEaelEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKR 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1808 LRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQ-EYIR-LKADFE 1885
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAA--------------EAEEEAEEAREEVAELNSKLAELKERIESlERIRtLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1886 HAEQQRGLLDNELQRLkNEVNaaeKQRRQLEDELAKVRSEMDAllqmKIQAEKVS--QSNTEKSKQLLETEALKMKQLAE 1963
Cdd:PRK02224 603 DAEDEIERLREKREAL-AELN---DERRERLAEKRERKRELEA----EFDEARIEeaREDKERAEEYLEQVEEKLDELRE 674
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1964 EAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAAI-NEATRLKT 2012
Cdd:PRK02224 675 ERDDLQAEIGAVE--NELEELEELRERREALENRVEALEALyDEAEELES 722
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
204-305 |
1.97e-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: 69.57 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 204 KTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
319-417 |
2.66e-13 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 68.92 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSVAERELGVTRLLDPED 398
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1655220517 399 VdVAHPDEKSIITYVSSLY 417
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3881-3919 |
2.82e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.58 E-value: 2.82e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 3881 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3919
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
220-299 |
4.86e-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: 68.39 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 220 HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 291
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1655220517 292 LGLIWTII 299
Cdd:cd21223 105 LALLWRII 112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2172-2819 |
5.53e-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: 75.93 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2172 EVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDEFENAkklaqaAETAKE 2251
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQ---SQEDLRNQLQNT------VHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2252 KAEKEAALLRQKAEEAEKLKKA--AEDEAAKQAKA------QKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH 2323
Cdd:pfam15921 157 AKCLKEDMLEDSNTQIEQLRKMmlSHEGVLQEIRSilvdfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2324 K------KEAEQALKQKSQVEKELGLVKLQldetDKQKALMDEElqrvKAQVNDAVKQKAQVENELSKVKMQMdELLKLK 2397
Cdd:pfam15921 237 KgrifpvEDQLEALKSESQNKIELLLQQHQ----DRIEQLISEH----EVEITGLTEKASSARSQANSIQSQL-EIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2398 VRieEENLRLMQKNKDntqklLAEEAEKMKSLAEEAARLSVEA-EETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2476
Cdd:pfam15921 308 AR--NQNSMYMRQLSD-----LESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2477 KLKAEAEELQKQKNQAQEKAKKL-----------------LEDKQEIQQRLDKETQGFQKSLEAERKRQLE-ISAEAEKL 2538
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlrreLDDRNMEVQRLEALLKAMKSECQGQMERQMAaIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2539 KlrvkELSSAQAKAEEEATRFKKQADE---AKVRLQETEKQTTETVVQKLETQR-LQSTR-EADDLKKAIAELEKEREKL 2613
Cdd:pfam15921 461 E----KVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQEKERaIEATNaEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2614 KRDAQELQNKSKETASAQQEQMEQQKAM--LQQTFLTEKELLLKRERD---VEDEKKKLQKHLED---EVNKAKALKDEQ 2685
Cdd:pfam15921 537 KNEGDHLRNVQTECEALKLQMAEKDKVIeiLRQQIENMTQLVGQHGRTagaMQVEKAQLEKEINDrrlELQEFKILKDKK 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2686 qrqqklmDEEKKKLQA-IMDEAVKKQKEAEAemknKQKEMEALEKKRLEQEKLLaDENKKLREKLESL----EVTSKQAA 2760
Cdd:pfam15921 617 -------DAKIRELEArVSDLELEKVKLVNA----GSERLRAVKDIKQERDQLL-NEVKTSRNELNSLsedyEVLKRNFR 684
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2761 SKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNgSVEAvkKDGASPLAFEGIRESVPAER 2819
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLK-SMEG--SDGHAMKVAMGMQKQITAKR 740
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
195-301 |
6.61e-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: 68.08 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 195 ADERDrvqKKTFTKWVNKHLMKAQrhITDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 266
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1655220517 267 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 301
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2966-3004 |
7.34e-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: 7.34e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 2966 FLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDMNKKL 3004
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2311-2541 |
8.22e-13 |
|
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: 73.64 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKvkmQM 2390
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2391 DELLKLKvRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALaekmLKEKMQ 2470
Cdd:COG4942 111 RALYRLG-RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL----LAELEE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2471 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLR 2541
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
781-971 |
8.28e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.55 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 781 QLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAF 860
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 861 TAALQTQWSWILQLCCCIETHLKENTAHFQFFSDVKEAEERIKKMQDTMKRKYTCDrsiTVTRLEDLVQDAADEREQLNE 940
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1655220517 941 IKTHLEGLKRRAKTIVQLKPRNPATPIKSKL 971
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1419-2121 |
9.33e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.49 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1419 LEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPI------ASPLKKPKMESASDNIIQEYVTLRTRYSELST 1492
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKreyegyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1493 LTSQYIKFILETQRRLEDDEKASEKLKEDE----KKRMAEIQAQLETQKqlaeghaKSVAKAELEAQELKLKMKEDASQR 1568
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIASLE-------RSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1569 QGLAVDAEKQKQNI---QLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1642
Cdd:TIGR02169 332 DKLLAEIEELEREIeeeRKRRDKLTEEyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1643 RDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1722
Cdd:TIGR02169 412 QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1723 kvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA---EKELETWR-- 1797
Cdd:TIGR02169 492 -------LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvEDDAVAKEai 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1798 --LKANEALRL------RLRAEEEAQRKSLA-------------QEEAEK------------QKTEAERDAKKKAKA--- 1841
Cdd:TIGR02169 565 elLKRRKAGRAtflplnKMRDERRDLSILSEdgvigfavdlvefDPKYEPafkyvfgdtlvvEDIEAARRLMGKYRMvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1842 --------------EEAALKQKENAEKELEKQRTFAEQIaqQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNA 1907
Cdd:TIGR02169 645 egelfeksgamtggSRAPRGGILFSRSEPAELQRLRERL--EGLKRELS--SLQSELRRIENRLDELSQELSDASRKIGE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1908 AEKQRRQLEDELAKVRSEMDAlLQMKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAARLRsvAEEAKKQRQLAEDEAA 1987
Cdd:TIGR02169 721 IEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQEIENVKSELKELEAR---IEELEEDLHKLE--EALNDLEARLSHSRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1988 RQRAEAEKIlKEKLAAINEATRlktEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSvSE 2067
Cdd:TIGR02169 795 EIQAELSKL-EEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-EE 869
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2068 LDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 2121
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1791-2777 |
9.41e-13 |
|
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: 75.47 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1791 KELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK------ELEKQRTFAE 1864
Cdd:TIGR00606 158 QEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEirdqitSKEAQLESSR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1865 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEvnaaEKQRRQLEDELAKVRsemdallqmkiqaEKVSQSNT 1944
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR----KKQMEKDNSELELKM-------------EKVFQGTD 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1945 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-------EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVA 2017
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLnqektelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELD 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2018 LKAKEAENERLKRQAEDEAYQRKLLEDQ-AAQHKHDIQEKITqLQSSSVSELDRQKNIVEETLRQKKVVeeeihiirinf 2096
Cdd:TIGR00606 381 GFERGPFSERQIKNFHTLVIERQEDEAKtAAQLCADLQSKER-LKQEQADEIRDEKKGLGRTIELKKEI----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2097 eraskeksdLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAaqdEVERL 2176
Cdd:TIGR00606 449 ---------LEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA---DLDRK 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2177 KQKAAEANKLKDKAEKELEKQVILAKeaaqKSTAAEQKAQDVLSKNKEDLLSQEKlrdEFENAKKLAQAAETAKEKaeke 2256
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQMEMLTK----DKMDKDEQIRKIKSRHSDELTSLLG---YFPNKKQLEDWLHSKSKE---- 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2257 aalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAalkqkQEADAEMAKHKKEAEQALKQKSQ 2336
Cdd:TIGR00606 586 ---INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-----QDEESDLERLKEEIEKSSKQRAM 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2337 VEKELGLVKLQLDETD--------------KQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLkvriee 2402
Cdd:TIGR00606 658 LAGATAVYSQFITQLTdenqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL------ 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2403 enLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAEL-AEQRALAEKMLKEKMQAIQEATKLKAE 2481
Cdd:TIGR00606 732 --APGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEeSAKVCLTDVTIMERFQMELKDVERKIA 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQgfqkSLEAERKRQLEISAEAEKLKLRVKELSSAqakaeeeatrfKK 2561
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVS----KIELNRKLIQDQQEQIQHLKSKTNELKSE-----------KL 874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2562 QADEAKVRLQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM 2641
Cdd:TIGR00606 875 QIGTNLQRRQQFEEQLVE-----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEK 949
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2642 LQQTFLTEKELllkrERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQ----------- 2710
Cdd:TIGR00606 950 VKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrk 1025
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2711 -----KEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQ 2777
Cdd:TIGR00606 1026 renelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFR 1097
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1653-2062 |
9.88e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1653 RKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE--KVRQIKVV 1730
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRlRLRA 1810
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLE-------ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 EEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA----------------------- 1867
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1868 ---QQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMDALLQMKIQAEKVSQS 1942
Cdd:COG4717 280 flvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeeLLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1943 NTEKSKQLLETE--ALKMKQLAEEAARLRSVAEEAKKQRQLAE--DEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL 2018
Cdd:COG4717 360 EEELQLEELEQEiaALLAEAGVEDEEELRAALEQAEEYQELKEelEELEEQLEELLGELEELLEALDEEELEEELEELEE 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2019 KAKEAENER---LKRQAEDEAYQRKLLEDQAAQH-KHDIQEKITQLQS 2062
Cdd:COG4717 440 ELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELRE 487
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3293-3331 |
1.13e-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: 1.13e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 3293 LLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMAKTL 3331
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4470-4508 |
1.23e-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: 1.23e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 4470 LLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMVDRI 4508
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2545-2764 |
1.74e-12 |
|
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: 72.49 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 LSSAQAKAEEEATRFKKQADEAKVRLQETEK--QTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQN 2622
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKelAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2623 KSKETAS---AQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ------KHLEDEVNKAKALKDEQQRQQKLMD 2693
Cdd:COG4942 91 EIAELRAeleAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2694 EEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD---ENKKLREKLESLEVTSKQAASKTK 2764
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAAAERTP 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2548-2767 |
1.86e-12 |
|
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: 72.49 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2548 AQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKEt 2627
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2628 asaQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAV 2707
Cdd:COG4942 102 ---QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2708 KKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
319-414 |
1.98e-12 |
|
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: 66.26 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLDPE 397
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1655220517 398 DVDVAHPDEKSIITYVS 414
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1503-2061 |
2.56e-12 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQ-------------LAEGHAKSV---AKAELEAQELKLKMKEDAS 1566
Cdd:NF041483 603 ERIRREAAEE--TERLRTEAAERIRTLQAQAEQEAErlrteaaadasaaRAEGENVAVrlrSEAAAEAERLKSEAQESAD 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1567 QRQGLAV-------------------DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQT 1627
Cdd:NF041483 681 RVRAEAAaaaervgteaaealaaaqeEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVE 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1628 TIKQKST-----ADDELQKLRD-----------------QAAE--AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKR 1683
Cdd:NF041483 761 EADRRATelvsaAEQTAQQVRDsvaglqeqaeeeiaglrSAAEhaAERTRTEAQEEADRVRSDAYAERERASEDANRLRR 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1684 KSEAEKEAA-----RQKQKALDELQKHKMQAEEAERRLK--------QAEEEKVRQIKVVEEVAQK------TAATQLQA 1744
Cdd:NF041483 841 EAQEETEAAkalaeRTVSEAIAEAERLRSDASEYAQRVRteasdtlaSAEQDAARTRADAREDANRirsdaaAQADRLIG 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1745 MSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQeeeankAREQAEKELETwrlKANEALRLRlraEEEAQRKSLAQEEA 1824
Cdd:NF041483 921 EATSEAERLTAEARAEAERLRDEARAEAERVRAD------AAAQAEQLIAE---ATGEAERLR---AEAAETVGSAQQHA 988
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1825 EKQKTEAERDAKKKAKAEEAALKQK--------ENAEKELEKQRT-FAEQIAQQKLSAEQEYIRLKADfEHAEQQRGLLD 1895
Cdd:NF041483 989 ERIRTEAERVKAEAAAEAERLRTEAreeadrtlDEARKDANKRRSeAAEQADTLITEAAAEADQLTAK-AQEEALRTTTE 1067
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1896 NELQRlKNEVNAAEKQRRQLEDE--------LAKVRSEMDALLqmkIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAAR 1967
Cdd:NF041483 1068 AEAQA-DTMVGAARKEAERIVAEatvegnslVEKARTDADELL---VGARRDATAIRERAEELRDRITGEIEELHERARR 1143
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1968 -----LRSVAEEAKKQRQLAEDEAARQRAEAEKILKE--------KLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2034
Cdd:NF041483 1144 esaeqMKSAGERCDALVKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEA 1223
|
650 660 670
....*....|....*....|....*....|...
gi 1655220517 2035 EAY------QRKLleDQAAQHKHDIQEKITQLQ 2061
Cdd:NF041483 1224 EAKrtveegKREL--DVLVRRREDINAEISRVQ 1254
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1629-2041 |
2.57e-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: 73.62 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1629 IKQKSTADDELQKLRDQAAEAEKV--RKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAEKEAARQKQKALDELQKHK 1706
Cdd:pfam17380 213 IQMSTVAPKEVQGMPHTLAPYEKMerRKESFNLAEDVTTMTPEYTVRY-NGQTMTENEFLNQLLHIVQHQKAVSERQQQE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1707 MQAEEAERRLKQAEEEKVRQIkvveevaqktaatqlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEAnkar 1786
Cdd:pfam17380 292 KFEKMEQERLRQEKEEKAREV---------------------ERRRKLEEAEKARQA---EMDRQAAIYAEQERMA---- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1787 EQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQeeaEKQKTEAERDAKKKAKAEEAALKQKENAEKElEKQRTFAEQI 1866
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISRMR---ELERLQMERQQKNERVRQELEAARKVKILEE-ERQRKIQQQK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1867 AQ-QKLSAEQEYIRlKADFEHAEQQRgllDNELQRLKNEVNAAEKQ---RRQLEDELAKVRSEMDALLQMKIQAEkvsqs 1942
Cdd:pfam17380 420 VEmEQIRAEQEEAR-QREVRRLEEER---AREMERVRLEEQERQQQverLRQQEEERKRKKLELEKEKRDRKRAE----- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1943 ntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLA-EDEAARQRAEAEK---ILKEKLAAINEATRLKTEAEVAL 2018
Cdd:pfam17380 491 --EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEMEERRRIQEQMRKATEERSRL 568
|
410 420
....*....|....*....|...
gi 1655220517 2019 KAKEAENERLKRQAEDEAYQRKL 2041
Cdd:pfam17380 569 EAMEREREMMRQIVESEKARAEY 591
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2063-2767 |
3.22e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2063 SSVSELDRQKnivEETLRQKKVVEEEIHIIRI-------NFERASKEKSDLEvELKKLKGIADETQKSKAKAEEEAEKLK 2135
Cdd:TIGR02169 163 AGVAEFDRKK---EKALEELEEVEENIERLDLiidekrqQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2136 KLAAEEErkrreaeekVKKIAAAEEEAARQRKAAQDEVERLKQKAAEAN-KLKDKAEKE-----------------LEKQ 2197
Cdd:TIGR02169 239 KEAIERQ---------LASLEEELEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEqlrvkekigeleaeiasLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2198 VILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDE 2277
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2278 aakqakaQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL 2357
Cdd:TIGR02169 387 -------LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2358 MDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE------NLRLMQKNKDNTQKLLAE--EAEKMKSL 2429
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrggraVEEVLKASIQGVHGTVAQlgSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2430 AEEAA---RLS---VEAEETA-------RQRKTAEA------ELAEQRALAEKMLKEK---------------------- 2468
Cdd:TIGR02169 540 AIEVAagnRLNnvvVEDDAVAkeaiellKRRKAGRAtflplnKMRDERRDLSILSEDGvigfavdlvefdpkyepafkyv 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2469 ------MQAIQEATKLKA-------EAEELQK--------------QKNQAQEKAKklLEDKQEIQQRLDKETQGFQKSL 2521
Cdd:TIGR02169 620 fgdtlvVEDIEAARRLMGkyrmvtlEGELFEKsgamtggsraprggILFSRSEPAE--LQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2522 EAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQStrEADDLKK 2601
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEA--RIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2602 AIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERdVEDEKkklqKHLEDEVNKAKA 2680
Cdd:TIGR02169 773 DLHKLEEALNDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEI----QELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2681 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADEN---KKLREKLESLEVTSK 2757
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLE 927
|
810
....*....|
gi 1655220517 2758 QAASKTKEIE 2767
Cdd:TIGR02169 928 ALEEELSEIE 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2072-2635 |
4.12e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2072 KNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKlkklaaeeerkrreaeek 2151
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS------------------ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2152 VKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEkqvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK 2231
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-----LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2232 LRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK-KAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL 2310
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEAdAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKAL---------MDEELQRVKAQVNDAVKQKAQVEN 2381
Cdd:PRK03918 409 KITARI-GELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeeytaelkrIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2382 ------ELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKL-------------LAEEAEKMKSLAEEAARLSVEAEE 2442
Cdd:PRK03918 488 vlkkesELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLkekliklkgeiksLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2443 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQaQEKAKKLLEDKQEIQQRLDKETQGFQ 2518
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNeyleLKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELR 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2519 KSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvqkletqRLQSTREADD 2598
Cdd:PRK03918 647 KELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE---------REKAKKELEK 715
|
570 580 590
....*....|....*....|....*....|....*..
gi 1655220517 2599 LKKAIAELEKEREKLKRdaqeLQNKSKETASAQQEQM 2635
Cdd:PRK03918 716 LEKALERVEELREKVKK----YKALLKERALSKVGEI 748
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1586-2009 |
4.26e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 4.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1586 LTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRK 1665
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1666 QVN--EETQKKKNAEDELKRKSEaEKEAARQKQKALDELQKhkmQAEEAERRLKQAEEEkvrqikVVEEVAQKTAATQLQ 1743
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPE-RLEELEERLEELRELEE---ELEELEAELAELQEE------LEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1744 AMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEE--EANKAREQAEKELETWRL----------------------- 1798
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARLllliaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1799 ----------------------KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKEL 1856
Cdd:COG4717 274 tiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1857 EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQ--QRGLLDNELQRLKNEVNAAEkqrRQLEDELAKVRSEMDALLQMKI 1934
Cdd:COG4717 354 REAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELE---EQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 1935 QAEKvsqsntEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATR 2009
Cdd:COG4717 431 EEEL------EELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2310-2613 |
7.42e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.30 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVK--QKAQVENELSKVk 2387
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQL--ADYQQAL--DVQQTRAIQYQQAVQalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2388 mqmdELLKLKVRIEEenlrLMQKNKDNTQKLLAEE-----AEKMKSLAEEAARL------SVEAEETARQRKTAEAELAE 2456
Cdd:PRK04863 436 ----TADNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLRE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2457 QRALAEKM--LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE 2534
Cdd:PRK04863 508 QRHLAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2535 AEKLKLRVKELSS-AQA--KAEEEATRFKKQADEAkvrlQETEKQTTETVVQKLETQRlQSTREADDLKKAIAELEKERE 2611
Cdd:PRK04863 588 LEQLQARIQRLAArAPAwlAAQDALARLREQSGEE----FEDSQDVTEYMQQLLERER-ELTVERDELAARKQALDEEIE 662
|
..
gi 1655220517 2612 KL 2613
Cdd:PRK04863 663 RL 664
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1445-2114 |
8.77e-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: 72.06 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1445 DYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKaseKLKEDEKK 1524
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKEN---KLQENRKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1525 rmaeIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQR-------QGLAVDAEK------QKQNIQLELTQLKN 1591
Cdd:pfam05483 115 ----IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnllkETCARSAEKtkkyeyEREETRQVYMDLNN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1592 LSEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1667
Cdd:pfam05483 191 NIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1668 NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLK-------QAEEEKVRQIkvvEEVAQKTAAT 1740
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQM---EELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1741 QLQAMSFSEKTTKLEESLKKEQGTVLQ-------LQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlrAEEE 1813
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKnedqlkiITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL---LDEK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1814 AQRKSLAQE-------------EAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ--KLSAEQEYI 1878
Cdd:pfam05483 425 KQFEKIAEElkgkeqelifllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdKLLLENKEL 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1879 RLKAD---FEHAEQQRGLLDNELQ--RLKNEVNAAEKQRRQLEDELAKVRSEM-DALLQMKIQAEKvSQSNTEKSKQLLE 1952
Cdd:pfam05483 505 TQEASdmtLELKKHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFiQKGDEVKCKLDK-SEENARSIEYEVL 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1953 TEALKMKQLAEEAARLRSVAEEAKK--QRQLAEDEAARQRAEAE-------KILKEKLAAINEATRLKTEAEVALKAKEA 2023
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2024 ENERLKRQA-EDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKE 2102
Cdd:pfam05483 664 EDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSA 740
|
730
....*....|..
gi 1655220517 2103 KSDLEVELKKLK 2114
Cdd:pfam05483 741 KAALEIELSNIK 752
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
319-418 |
9.91e-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: 64.28 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 319 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSN---QENLEQAFSVAERE-LGVTRLL 394
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1655220517 395 DPEDVdVAHPDEKSIITYVSSLYD 418
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2416-2737 |
1.05e-11 |
|
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: 69.95 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK 2495
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2496 AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEklkLRVKELSSAQAKAEEEATRFKKQADEAKvrlqetEK 2575
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2576 QTTETVVQKLETQRLQSTREADDLKKAIAELE-KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQtfltekelll 2654
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQELQQAREEQIELKERRLAE---------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2655 KRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDE---AVKKQKEAEAEMKNKQKEMEALEKKR 2731
Cdd:pfam13868 255 EAEREEEEFERMLRKQAEDE----EIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1655220517 2732 LEQEKL 2737
Cdd:pfam13868 331 IEEERQ 336
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
197-296 |
1.21e-11 |
|
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: 64.75 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRvQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 268
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1655220517 269 KHRQVKLVNIRNDDIADGNPKLTLGLIW 296
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
686-875 |
1.38e-11 |
|
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: 67.09 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 686 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 762
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 763 LQYDKLLHDSKAR---LRYLVQLHTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGV 839
Cdd:cd00176 86 QRWEELRELAEERrqrLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220517 840 QTTGDKLLRDGHP-GRKTIEAFTAALQTQWSWILQLC 875
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1644-1884 |
1.48e-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: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1723
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1724 VRQIKVVEEV---AQKTA-ATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlk 1799
Cdd:COG4942 100 EAQKEELAELlraLYRLGrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1800 anealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR 1879
Cdd:COG4942 178 -------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1655220517 1880 LKADF 1884
Cdd:COG4942 251 LKGKL 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1151-1832 |
1.56e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 71.30 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1151 TKIKDLRLKLDGCESrtvTRLRQPVDKEPLKACAQKTAEQMKVQSEL-EGLKKDLNSITEKTEEILASPQ---QSSSAPM 1226
Cdd:pfam15921 117 TKLQEMQMERDAMAD---IRRRESQSQEDLRNQLQNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1227 LRSElDVTLKKMDHVYGLSSVYLDKLKT-IDIVIRNTkdaeDTVKSY-ESRLrdvskVPAEEkeveahrsQLKAMRAEAE 1304
Cdd:pfam15921 194 VDFE-EASGKKIYEHDSMSTMHFRSLGSaISKILREL----DTEISYlKGRI-----FPVED--------QLEALKSESQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1305 ADQATFdrLQDElkaatsvSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL----SLLGRHMNSYKQSY 1380
Cdd:pfam15921 256 NKIELL--LQQH-------QDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQArnqnSMYMRQLSDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1381 EWLIQWLREA-RLRQEKIEA---------APVWDSKALKEQLTQE--------KKLLEEIEKNKDQIENCQKDAKAYID- 1441
Cdd:pfam15921 327 SQLRSELREAkRMYEDKIEElekqlvlanSELTEARTERDQFSQEsgnlddqlQKLLADLHKREKELSLEKEQNKRLWDr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1442 -------------SLKDYEFQILAYRALQDPIASPLKKpKMESASDNIIQEYVTLRtrysELSTLTSQyIKFILETQRRL 1508
Cdd:pfam15921 407 dtgnsitidhlrrELDDRNMEVQRLEALLKAMKSECQG-QMERQMAAIQGKNESLE----KVSSLTAQ-LESTKEMLRKV 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1509 EDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK----AELEAQELK-LKMKEDASQR-----QGLAVDAEKQ 1578
Cdd:pfam15921 481 VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrVDLKLQELQhLKNEGDHLRNvqtecEALKLQMAEK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1579 KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQ--TTIKQKSTA----------DDELQKLRDQA 1646
Cdd:pfam15921 561 DKVIEILRQQIENMT-QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAkirelearvsDLELEKVKLVN 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1647 AEAEKVRkaAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD-ELQKHKMQAEEAERRLKQA------ 1719
Cdd:pfam15921 640 AGSERLR--AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtTTNKLKMQLKSAQSELEQTrntlks 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1720 -EEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1798
Cdd:pfam15921 718 mEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
730 740 750
....*....|....*....|....*....|....
gi 1655220517 1799 KANealrlrlRAEEEAQRKSLAQEEAEKQKTEAE 1832
Cdd:pfam15921 798 QER-------RLKEKVANMEVALDKASLQFAECQ 824
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2451-2776 |
1.60e-11 |
|
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: 70.81 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2451 EAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEK---AKKLLEDKQEiQQRLDKETQGFqKSLEaerkr 2527
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKveeAEKKAKDQKE-EDRRNYPTNTY-KTLE----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2528 qLEIsAEAEkLKLRVKELSSAQAKAEEEATRFKKQADEAKVRlqetEKQTTETVVQKLETQRLQSTREADdlKKAIAELE 2607
Cdd:NF033838 176 -LEI-AESD-VEVKKAELELVKEEAKEPRDEEKIKQAKAKVE----SKKAEATRLEKIKTDREKAEEEAK--RRADAKLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2608 KEREKLKRDAQELQNKSKETASAQQEQM----EQQKAMLQQTFLTEKEL---LLKRERDVEDEKKKLqkhlEDEVNKAKA 2680
Cdd:NF033838 247 EAVEKNVATSEQDKPKRRAKRGVLGEPAtpdkKENDAKSSDSSVGEETLpspSLKPEKKVAEAEKKV----EEAKKKAKD 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2681 LKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEM-KNKQKEMEALEKKRLEQEKLladENKKLR-EKLESLEVTSKQ 2758
Cdd:NF033838 323 QKEEDRRNYP--TNTYKTLELEIAESDVKVKEAELELvKEEAKEPRNEEKIKQAKAKV---ESKKAEaTRLEKIKTDRKK 397
|
330
....*....|....*...
gi 1655220517 2759 AASKTKEIEVQTDKVPEE 2776
Cdd:NF033838 398 AEEEAKRKAAEEDKVKEK 415
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2890-2927 |
1.64e-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: 1.64e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 2890 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPELHTR 2927
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2351-2763 |
1.68e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2351 TDKQKALMDEELQRVKAQVNDAVKQK---AQVENELSKVKMQMDELLKLKVRIEEE--NLRLMQKNKDNTQKLLAEEAEk 2425
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAE- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2426 MKSLAEEAARLSVEAE---ETARQRKTAEAELAE-QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLE 2501
Cdd:COG4717 141 LAELPERLEELEERLEelrELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2502 DKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE------------ATRFKKQADEAKVR 2569
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2570 LQETEKQTTETVVQKLETQRLQSTREADDLKKAI--AELEKEREKLKRDAQELQNKSKETASAQQEQ-MEQQKAMLQQTF 2646
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLspEELLELLDRIEELQELLREAEELEEELQLEElEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2647 LTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL----MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQK 2722
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeLEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1655220517 2723 EMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKT 2763
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3624-3658 |
2.07e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.07e-11
10 20 30
....*....|....*....|....*....|....*
gi 1655220517 3624 LLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQM 3658
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPET 35
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2485-2782 |
2.43e-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: 70.54 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2485 LQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEisaEAEKLKlrvkelssaQAKAEEEATRFKKQAD 2564
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKE----EKAREVERRRKLE---EAEKAR---------QAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2565 EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE-KLKRDAQELqnkskETASAQQEQMEQQKAMLQ 2643
Cdd:pfam17380 342 MAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQqKNERVRQEL-----EAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2644 QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKL-----MDEEKKKLQAIMDEAVKKQKEAEAE-M 2717
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR--LEEQERQQQVerlrqQEEERKRKKLELEKEKRDRKRAEEQrR 494
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2718 KNKQKEMEALEKKRLEQE---KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMT 2782
Cdd:pfam17380 495 KILEKELEERKQAMIEEErkrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2518-2744 |
2.77e-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: 69.02 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2518 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREAD 2597
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-----LAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2598 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ--QTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2675
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2676 NKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKK 2744
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1574-2114 |
2.84e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1574 DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1653
Cdd:PRK03918 190 NIEELIKEKEKELEEVLR-EINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1654 KAAQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRqikvVEEV 1733
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER----LEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQKTAATQlqamsfsEKTTKLEESLKKEQgTVLQLQEEAEKLRKQE-----EEANKAREQAEKELETWRLKANEALRLRL 1808
Cdd:PRK03918 344 KKKLKELE-------KRLEELEERHELYE-EAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1809 RAEEEAQRKSLAQEEAEKQK----------TEAERDAKKKAKAEEAALKQKE--NAEKELEKQRTFAEQIaQQKLSAEQE 1876
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKgkcpvcgrelTEEHRKELLEEYTAELKRIEKElkEIEEKERKLRKELREL-EKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1877 YIRLKadfEHAEQQRGlLDNELQRL-KNEVNAAEKQRRQLEDELAKVRSEMdallqmkiqaekvsqsntekskQLLETEA 1955
Cdd:PRK03918 495 LIKLK---ELAEQLKE-LEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEI----------------------KSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1956 LKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDE 2035
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2036 AYQRKLLEDQAAQHKhDIQEKITQLQSSSVSEldRQKNIVEETLRqkkvVEEEIHIIRINFERASKEKSDLEVELKKLK 2114
Cdd:PRK03918 629 DKAFEELAETEKRLE-ELRKELEELEKKYSEE--EYEELREEYLE----LSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1604-2123 |
3.75e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1604 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVnEETQKKKNAEDELKR 1683
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1684 K---SEAEKEAARQKQKALDE-LQKHKMQAEEAERRLKQAeEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLK 1759
Cdd:PRK03918 239 EieeLEKELESLEGSKRKLEEkIRELEERIEELKKEIEEL-EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1760 KEQGTVLQLQEEAEKLRKQEEEANKAREQAEK------ELETWRLKANEALRLRLRAEE-EAQRKSLAQEEAEKQKTEAE 1832
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKElekrleELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1833 RdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA------------DFEHAEQQRGLLDNELQR 1900
Cdd:PRK03918 398 K--------------AKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1901 LKNEVNAAEKQRRQLEDELAKVRSEMDA---LLQMKIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLRSVAEEAKK 1977
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNLE----ELEKKAEEYEKLKEKLIKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1978 QRQLAEDEAARqraeaEKILKEKLAAINEATRlKTEAEVALKAKEAENERLKRQAEDE--------AYQRKLLEDQAAQH 2049
Cdd:PRK03918 540 EIKSLKKELEK-----LEELKKKLAELEKKLD-ELEEELAELLKELEELGFESVEELEerlkelepFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2050 KHDIQEKITQLQSS---SVSELDRQKNIVEETLRQ-----KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQ 2121
Cdd:PRK03918 614 LEREEKELKKLEEEldkAFEELAETEKRLEELRKEleeleKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
..
gi 1655220517 2122 KS 2123
Cdd:PRK03918 694 KT 695
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1262-1974 |
4.05e-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: 70.00 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1262 TKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRL---HSERDAEL 1338
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQeavLEETQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1339 EHYRQLAGSLLE---------RWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKAL 1408
Cdd:TIGR00618 287 NRARKAAPLAAHikavtqieqQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1409 -KEQLTQEKKLLEEIEKNKDQIENCQKDAKAyIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRY 1487
Cdd:TIGR00618 367 iREISCQQHTLTQHIHTLQQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1488 SELSTLTSQYIKFIL--ETQRRLeDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELE-AQELKLKMKED 1564
Cdd:TIGR00618 446 AITCTAQCEKLEKIHlqESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1565 ASQRQGLAVDAEKQKQniqleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstaDDELQKLRD 1644
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQL-------------ETSEEDVYHQLTSERKQRASLKEQMQEI--------------QQSFSILTQ 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1645 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE-------AERRLK 1717
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalhalQLTLTQ 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1718 QAEEEKVRQIKVVEEVAQKTAATQLQAM-SFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETW 1796
Cdd:TIGR00618 658 ERVREHALSIRVLPKELLASRQLALQKMqSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1797 RLKANEALRlrlRAEEEAQRKSLAQEEAEKQKTEAErdakkkaKAEEAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQ 1875
Cdd:TIGR00618 738 EDALNQSLK---ELMHQARTVLKARTEAHFNNNEEV-------TAALQTGAELSHLAAEIQfFNRLREEDTHLLKTLEAE 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1876 EYIRLKADFEHAEQQRGLLDNELQRLKNevnaaekQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1955
Cdd:TIGR00618 808 IGQEIPSDEDILNLQCETLVQEEEQFLS-------RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
730
....*....|....*....
gi 1655220517 1956 LKMKQLAEEAARLRSVAEE 1974
Cdd:TIGR00618 881 INQIKIQFDGDALIKFLHE 899
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2262-2613 |
4.21e-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: 69.38 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2262 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKqeadaemakhKKEAEQALKQK--SQVEK 2339
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEER----------KRELERIRQEEiaMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2340 ELGLVKLQLDETDKQkalmdeelQRVKAQVNDAVKQKAQVENELSKVKMQMDELlkLKVRIEEENLRlmqknkdntqkll 2419
Cdd:pfam17380 377 MRELERLQMERQQKN--------ERVRQELEAARKVKILEEERQRKIQQQKVEM--EQIRAEQEEAR------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2420 aeeAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKL 2499
Cdd:pfam17380 434 ---QREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE--------------ERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2500 LEdkQEIQQRLdketqgfQKSLEAERKRQLeISAEAEKlklRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2579
Cdd:pfam17380 497 LE--KELEERK-------QAMIEEERKRKL-LEKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|....
gi 1655220517 2580 tvvqklETQRLQSTREADDLKKAIAELEKEREKL 2613
Cdd:pfam17380 564 ------ERSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1656-2196 |
4.44e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEetqKKKNAEDELKRKSEAE---KEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqiKVVEE 1732
Cdd:PRK03918 163 AYKNLGEVIKEIKR---RIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1733 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEK--ELETWRLKANEALRlrlRA 1810
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELR---EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 EEEAQRKSLAQEEAEKQKTEAERDakkkAKAEEAALKQKENAEKELEKQRTFAEqiaqqklsaeqEYIRLKADFEHAEQQ 1890
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHE-----------LYEEAKAKKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1891 RGLL-DNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQS---------------NTEKSKQLLETE 1954
Cdd:PRK03918 378 KKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1955 ALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR--------AEAEKILKEKLAAINeATRLKTEAEVALKAKEAEN- 2025
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelAEQLKELEEKLKKYN-LEELEKKAEEYEKLKEKLIk 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2026 ---------ERLKRQAEDEAYQRKLLE--DQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQkkvveeeihiiri 2094
Cdd:PRK03918 537 lkgeikslkKELEKLEELKKKLAELEKklDELEEELAELLKELEELGFESVEELEERLKELEPFYNE------------- 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2095 nFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE-AEEKVKKIAAAEEEAARQRKAAQDEV 2173
Cdd:PRK03918 604 -YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAEL 682
|
570 580
....*....|....*....|...
gi 1655220517 2174 ERLKQKAAEANKLKDKAEKELEK 2196
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEE 705
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1670-2729 |
5.67e-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: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1670 ETQKKKNAEDELKRKSEAEKEAARQKQKALDelQKHKMQAEEAERRLKQAEEEKVRQI--KVVEEVAQKTAATQLqAMSF 1747
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKALETLRQVRQT--QGQKVQEHQMELKYLKQYKEKACEIrdQITSKEAQLESSREI-VKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1748 SEKTTKLEESLKK---EQGTVLQLQEEAEKLRKQEEEankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLaqEEA 1824
Cdd:TIGR00606 244 ENELDPLKNRLKEiehNLSKIMKLDNEIKALKSRKKQ----MEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTV--REK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1825 EKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRG-LLDNELQrlkn 1903
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGpFSERQIK---- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1904 evNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKK----QR 1979
Cdd:TIGR00606 394 --NFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSD 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1980 QLAEDEAARQRAEAEKILKEKlaaiNEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ-------RKLLEdQAAQHKHD 2052
Cdd:TIGR00606 472 RILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttRTQME-MLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2053 IQEKITQLQSSSVSELDRQKNiveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSkakaeeeae 2132
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLG----YFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL-----EQNKN--------- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 klkklaaeeerkrreaeekvkKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLkDKAEKELEKQvilAKEAAQKSTAAE 2212
Cdd:TIGR00606 609 ---------------------HINNELESKEEQLSSYEDKLFDVCGSQDEESDL-ERLKEEIEKS---SKQRAMLAGATA 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2213 QKAQDVlsknkedllsqEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2292
Cdd:TIGR00606 664 VYSQFI-----------TQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2293 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKqkalmdeeLQRVKAQVNDA 2372
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI--------MERFQMELKDV 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2373 VKQKAQVENELSKVKMqmdellklkvrieeeNLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEETARQRKTAEA 2452
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDL---------------DRTVQQVNQEKQEK--QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN 867
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2453 ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEIS 2532
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE---KEELISSKETSNKKAQDKVN 944
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2533 AEAEKLKLRVKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTE------TVVQKLETQRLQSTREADDLKka 2602
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGKDDYLKQKEtelnTVNAQLEECEKHQEKinedmrLMRQDIDTQKIQERWLQDNLT-- 1022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2603 iaeLEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLT---EKELLLKRERDVEDEKKKLQKHLedevnKAK 2679
Cdd:TIGR00606 1023 ---LRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLikrNHVLALGRQKGYEKEIKHFKKEL-----REP 1094
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2680 ALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEK 2729
Cdd:TIGR00606 1095 QFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHSMKMEEINK 1144
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1406-2056 |
5.91e-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: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1406 KALKE-QLTQEK---KLLEEIEKNKDQIEncQKDAKAYIDSLkdyefqilayraLQDPIA-SPLKKPKMESASDNIIQEY 1480
Cdd:pfam05483 120 KAIQElQFENEKvslKLEEEIQENKDLIK--ENNATRHLCNL------------LKETCArSAEKTKKYEYEREETRQVY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1481 VTLRTRYSELST----LTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQ---LETQKQLAEGHAKSVAKAELE 1553
Cdd:pfam05483 186 MDLNNNIEKMILafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1554 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKS 1633
Cdd:pfam05483 266 SRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1634 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ---VNEETQKKKNAEDE---LKRKSEAEKEAAR----QKQKALDELQ 1703
Cdd:pfam05483 346 AHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQlkiITMELQKKSSELEEmtkFKNNKEVELEELKkilaEDEKLLDEKK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1704 KHKMQAEEAERR------LKQAEEEKVRQIKVveEVAQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTV---------LQ 1767
Cdd:pfam05483 426 QFEKIAEELKGKeqelifLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEkEKLKNIELTAhcdklllenKE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1768 LQEEAE----KLRKQEEEANKAREQAEKELEtwRLKANEALRLRLRAEEEAQRKSLAQ---------EEAEKQKTEAERD 1834
Cdd:pfam05483 504 LTQEASdmtlELKKHQEDIINCKKQEERMLK--QIENLEEKEMNLRDELESVREEFIQkgdevkcklDKSEENARSIEYE 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1835 AKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLDNElqrlknEVNAAEKQRRQ 1914
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN---------------KALKKKGSAENK------QLNAYEIKVNK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1915 LEDELAKVRS---EMDALLQMKIQAEKVSQSNtekskqlLETEALKMKQLAEEAARLRSVAEEaKKQRQLAEDEA--ARQ 1989
Cdd:pfam05483 641 LELELASAKQkfeEIIDNYQKEIEDKKISEEK-------LLEEVEKAKAIADEAVKLQKEIDK-RCQHKIAEMVAlmEKH 712
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1990 RAEAEKILKEKLAAI-------NEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEK 2056
Cdd:pfam05483 713 KHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
195-302 |
6.15e-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: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLKH 270
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 271 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1545-2392 |
6.27e-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: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1545 KSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRS--KNQQLEEAQVSRR------KLEE 1616
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSRlysklyKEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1617 EIHLIRIQLQTTIKQKSTaddelqKLRDQAAEAEKVRKAAQE---EAERLRKQVNEETQKKKNAEDELKRKSEAEKEAAR 1693
Cdd:pfam05483 89 KIKKWKVSIEAELKQKEN------KLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1694 QKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQaMSFS-----EKTTKLEESLKKEQGT---- 1764
Cdd:pfam05483 163 TCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLE-MHFKlkedhEKIQHLEEEYKKEINDkekq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1765 ----VLQLQEEAEKLRKQ----EEEANKAREQAEK-ELETWRLKANEALRLRLRAEEEAQRKSLaQEEAEKQKTeAERDA 1835
Cdd:pfam05483 242 vsllLIQITEKENKMKDLtfllEESRDKANQLEEKtKLQDENLKELIEKKDHLTKELEDIKMSL-QRSMSTQKA-LEEDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1836 KKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQklsaeqeyirLKADFEHAEQqrgLLDNELQRLKNEvnaaEKQRRQL 1915
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE----------FEATTCSLEE---LLRTEQQRLEKN----EDQLKII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1916 EDELAKVRSEMDALLQMKiqaekvsqSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAK-KQRQLAEDEAARQRAEAE 1994
Cdd:pfam05483 383 TMELQKKSSELEEMTKFK--------NNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHD 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1995 KILKEKLAAINEATRLKteaEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaqhkhdiqeKITQLQSSSVSELDRQKni 2074
Cdd:pfam05483 455 LEIQLTAIKTSEEHYLK---EVEDLKTELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQ-- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2075 vEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK 2154
Cdd:pfam05483 520 -EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2155 IAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKedlLSQEKLRD 2234
Cdd:pfam05483 599 LKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2235 EFENAKKLaqaaetakekaekeaallrqkAEEAEKLKKAAEDEAAKQAKaqkdaerlrkeaeaeaakraaaeaaalkqkq 2314
Cdd:pfam05483 676 EVEKAKAI---------------------ADEAVKLQKEIDKRCQHKIA------------------------------- 703
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2315 EADAEMAKHKKEAEQALKQKsqvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE 2392
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1565-1973 |
8.72e-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: 68.83 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1565 ASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKnQQLEEAQVSRRKLEEEI-----HLIRiqLQTTIKQKSTAD--- 1636
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMA-RELEELSARESDLEQDYqaasdHLNL--VQTALRQQEKIEryq 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1637 DELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkKKNAEDELKrkseaekEAARQ---KQKALDELQKHKMQAEEAE 1713
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEAR-------LEAAEEEVD-------SLKSQladYQQALDVQQTRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1714 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK--QEEEANKAREQAEK 1791
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiaGEVERSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1792 ELETWRLKANEALRLR-LRAE-EEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE----KQRTFAEQ 1865
Cdd:COG3096 500 LLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEeleeQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1866 IAQ-----QKLSAEQEYIRLKADFEHAEQQRglldneLQRLKNEVNAAekqrrqLEDelakvRSEMDALLQMKIQAE--- 1937
Cdd:COG3096 580 RSElrqqlEQLRARIKELAARAPAWLAAQDA------LERLREQSGEA------LAD-----SQEVTAAMQQLLERErea 642
|
410 420 430
....*....|....*....|....*....|....*..
gi 1655220517 1938 KVSQSNTEKSKQLLETEALKMKQLA-EEAARLRSVAE 1973
Cdd:COG3096 643 TVERDELAARKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4124-4162 |
9.98e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 9.98e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 4124 LLEAQAATGYVIDPIKNLKLNVTEAVKMGVVGPEFKDKL 4162
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4546-4584 |
1.14e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.26 E-value: 1.14e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 4546 FLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTAQKL 4584
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1814-2068 |
1.39e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1814 AQRKSLAQEEAEKQKTEAerdakkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGL 1893
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ----------------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1894 LDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAE 1973
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1974 EAKKQRQlaedEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDI 2053
Cdd:COG4942 161 ELAALRA----ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*
gi 1655220517 2054 QEKITQLQSSSVSEL 2068
Cdd:COG4942 237 AAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2325-2566 |
1.99e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2325 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvrieEEN 2404
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--------EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2405 LRLMQKNKDNTQKLLAE---EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmQAIQEATKLKAE 2481
Cdd:COG4942 92 IAELRAELEAQKEELAEllrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR----------EQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKK 2561
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 1655220517 2562 QADEA 2566
Cdd:COG4942 242 RTPAA 246
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1079-1876 |
2.00e-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: 67.69 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1079 KTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQ----VESNYNRANQHYNTMVSSAEQGEQDESVCKTYLTKIK 1154
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1155 DLRLKLDGCESRTVTRLRQPV-DKEPLKACAQKTAEQMKVQSELEGLKKDLN-SITEKTEEILASPQQSSSAPMLRSELD 1232
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKeSEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEEELL 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1233 VTLKKMDHVYGLSSVYLDKLKTIDIVIRNTKDAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDR 1312
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQ 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1313 LQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARL 1392
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1393 RQEKIEAA-----PVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLK-- 1465
Cdd:pfam02463 537 AVENYKVAistavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEad 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1466 ---KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEG 1542
Cdd:pfam02463 617 eddKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1543 HAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIR 1622
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1623 IQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1702
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEEL 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1703 Q-KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK---- 1777
Cdd:pfam02463 857 ErLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeee 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1778 ------------QEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAA 1845
Cdd:pfam02463 937 peellleeadekEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
810 820 830
....*....|....*....|....*....|.
gi 1655220517 1846 LKQKENAEKELEKQRTFAEQIAQQKLSAEQE 1876
Cdd:pfam02463 1017 QRLKEFLELFVSINKGWNKVFFYLELGGSAE 1047
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2167-2753 |
2.28e-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: 67.30 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2167 KAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAqdVLSKNKEDLLSQEKLRDEFENAKKLAQAA 2246
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEA--VLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2247 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE 2326
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2327 AEQALKQKSQV-----EKELGLVKLQLDETDKQKALMDEELQ---RVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKV 2398
Cdd:TIGR00618 387 QKTTLTQKLQSlckelDILQREQATIDTRTSAFRDLQGQLAHakkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2399 RIEEENLRLMQKnkdntQKLLAEEAEKMKSLAEEAARLSVEAEETARQrkTAEAELAEQRALAEKMLKEKMQA-IQEATK 2477
Cdd:TIGR00618 467 SLKEREQQLQTK-----EQIHLQETRKKAVVLARLLELQEEPCPLCGS--CIHPNPARQDIDNPGPLTRRMQRgEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2478 LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLE-AERKRQLEISAEAEKLKLRVKELSSAQAKAEEEA 2556
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2557 trfKKQADEAKVRLQETEKQTTETVVQKLETQrlqsTREADDLKKaiaelEKEREKLKR-DAQELQNKSKETASAQQEQM 2635
Cdd:TIGR00618 620 ---KLQPEQDLQDVRLHLQQCSQELALKLTAL----HALQLTLTQ-----ERVREHALSiRVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2636 EQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKA-----LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQ 2710
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKARTEAHFNNN 767
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1655220517 2711 KEAEAEMKNKQKEMEaLEKKRLEQEKLLADENKKLREKLESLE 2753
Cdd:TIGR00618 768 EEVTAALQTGAELSH-LAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1264-1816 |
2.67e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1264 DAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYR 1342
Cdd:COG1196 278 ELELELEEAQAEEYELlAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1343 QLAGSLLERWQAVFAQIDLRQRElsllgrhmnsykqsyewliqwlrEARLRQEKIEAApvwdsKALKEQLTQEKKLLEEI 1422
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEE-----------------------LEELAEELLEAL-----RAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1423 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDpiasplkkpKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFIL 1502
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALE---------EAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAE-------------GHAKSVAKAELEAQELKLKMKEDASQRQ 1569
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligvEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1570 GLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1647
Cdd:COG1196 561 AAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1648 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1727
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQKTAATQLQamsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKA-Nealrl 1806
Cdd:COG1196 721 LEEEALEEQLEAEREE----------LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE--ALGPvN----- 783
|
570
....*....|
gi 1655220517 1807 rLRAEEEAQR 1816
Cdd:COG1196 784 -LLAIEEYEE 792
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4468-4505 |
2.84e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 57.88 E-value: 2.84e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 4468 QRLLEAQACTGGIIDPNTGEKFSVADAMNKGLVDKIMV 4505
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1968-2689 |
2.85e-10 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 67.16 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1968 LRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaINEATRLKTE--AEVALKAKEAENERLKRQAEDEAYQRKLLEdQ 2045
Cdd:NF041483 78 LRNAQIQADQLRADAERELRDARAQTQRILQEH---AEHQARLQAElhTEAVQRRQQLDQELAERRQTVESHVNENVA-W 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2046 AAQHKHDIQEKITQLQSSSVSELDrqKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKlkgiadETQKSKA 2125
Cdd:NF041483 154 AEQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK------DAERLLN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2126 KAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRkaAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAA 2205
Cdd:NF041483 226 AASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQR--MQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2206 QK--STAAEQKAQDVLSKNKEdllsQEKLRDEFENAKKLAQAAETakekaekeaallRQKAEEAEKLK-KAAEDEAAKQA 2282
Cdd:NF041483 304 EQrtRTAKEEIARLVGEATKE----AEALKAEAEQALADARAEAE------------KLVAEAAEKARtVAAEDTAAQLA 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2283 KAQKDAER-LRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKE------LGLVKLQLD------ 2349
Cdd:NF041483 368 KAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDdtkeyrAKTVELQEEarrlrg 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2350 ETDKQKALMDEELQRVKAQV-NDAVKQ----KAQVENELSKVKMQMDElLKLKVRIEEENLRLMQKNKDNTQKLLAEEAe 2424
Cdd:NF041483 448 EAEQLRAEAVAEGERIRGEArREAVQQieeaARTAEELLTKAKADADE-LRSTATAESERVRTEAIERATTLRRQAEET- 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2425 kMKSLAEEAARLSVEAEETAR-QRKTAEAELAEQRALAEK-MLKEKMQAIQEATKLKAEAEE----LQKQKNQAQEKAKK 2498
Cdd:NF041483 526 -LERTRAEAERLRAEAEEQAEeVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEErltaAEEALADARAEAER 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2499 LLEDKQEIQQRLDKETqgfqksleAERKRQLEISAEAEKLKLR---VKELSSAQAKAEEEATRFKKQADEAKVRLQETEK 2575
Cdd:NF041483 605 IRREAAEETERLRTEA--------AERIRTLQAQAEQEAERLRteaAADASAARAEGENVAVRLRSEAAAEAERLKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2576 QTTETVVQKLETqrlQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQkamlqqtfltEKELLLK 2655
Cdd:NF041483 677 ESADRVRAEAAA---AAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQ----------SEELLAS 743
|
730 740 750
....*....|....*....|....*....|....*.
gi 1655220517 2656 RERDVEDEKKKLQKHLEDEVNKAKAL--KDEQQRQQ 2689
Cdd:NF041483 744 ARKRVEEAQAEAQRLVEEADRRATELvsAAEQTAQQ 779
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1595-1925 |
2.97e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 66.43 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1595 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR-KAAQEEAERLRKQVNEETQK 1673
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRqKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1674 KKNAEDELKRKSEAEKEAARQKQKALDELQKHKMqaEEAERRLKQAEEEKVRQ-IKVVEEVAQKTAATQLQAMSFSEKTT 1752
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKEEKRDSRLGRYKE--EETEIREKEYQENKWSTeVRQAEEEGEEEEDKSEEAEEVPTENF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1753 KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1832
Cdd:pfam02029 175 AKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1833 RdakkkakaeeaalkqkENAEKELEKqrtfAEQIAQQKLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKNEVN----AA 1908
Cdd:pfam02029 255 R----------------RRQEKESEE----FEKLRQKQQEAELELEELK---KKREERRKLLEEEEQRRKQEEAerklRE 311
|
330
....*....|....*..
gi 1655220517 1909 EKQRRQLEDELAKVRSE 1925
Cdd:pfam02029 312 EEEKRRMKEEIERRRAE 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1391-1740 |
3.15e-10 |
|
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: 66.69 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1391 RLRQEKIEaapvwdsKALKEQLTQEKK-LLEEIEKNKdQIENCQKDAKAYIDSlkdyefqilayralQDPIASPLKKPKM 1469
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDR--------------QAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1470 ESASDniiQEYVTLRTRYSELSTLTSQYIKFILETQRRLE--------DDEKASEKLKEDEKKRMAEIQAQLETQKQLAE 1541
Cdd:pfam17380 345 ERERE---LERIRQEERKRELERIRQEEIAMEISRMRELErlqmerqqKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1542 ghAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEihli 1621
Cdd:pfam17380 422 --MEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ---EEERKRKKLELEKEKRDRKRAEEQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1622 riqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEEtQKKKNAEDElkRKSEAEKEAARQKQKALDE 1701
Cdd:pfam17380 493 ---------RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEE--RRKQQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|....*....
gi 1655220517 1702 LQKHKMQAEEAERrlkqaEEEKVRQIKVVEEVAQKTAAT 1740
Cdd:pfam17380 561 ATEERSRLEAMER-----EREMMRQIVESEKARAEYEAT 594
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1496-2119 |
3.19e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.07 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1496 QYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtQKQLAEGHAKSVAKAELEAQElklkmkedasqrqglavDA 1575
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQ-EMQMERDAMADIRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQ---VSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL--RDQAAEAE 1650
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRkmmLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1651 KVRKAAQEEAERLRKQVNEetqkkknAEDELkrksEAEKEAARQKQKALdeLQKHKmqaEEAERRLKQAEEEkvrqikvV 1730
Cdd:pfam15921 224 KILRELDTEISYLKGRIFP-------VEDQL----EALKSESQNKIELL--LQQHQ---DRIEQLISEHEVE-------I 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVL----QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALrl 1806
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSEL-- 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1807 rlrAEEEAQRKSLAQEEA----EKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKA 1882
Cdd:pfam15921 359 ---TEARTERDQFSQESGnlddQLQKLLAD--------------LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1883 DFEHAEQQRglLDNELQRLKNEVNAaekqrrQLEDELAKVRSEMDALlqmkiqaEKVSQ--SNTEKSKQLLE--TEALKM 1958
Cdd:pfam15921 422 DDRNMEVQR--LEALLKAMKSECQG------QMERQMAAIQGKNESL-------EKVSSltAQLESTKEMLRkvVEELTA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1959 KQLAEEAARlRSVAEEAKkqrQLAEDEAARQRAEAE--KILKEKLAAINEATRLKTEAEvALKAKEAENERLKRQAEDEA 2036
Cdd:pfam15921 487 KKMTLESSE-RTVSDLTA---SLQEKERAIEATNAEitKLRSRVDLKLQELQHLKNEGD-HLRNVQTECEALKLQMAEKD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2037 YQRKLLEDQAaqhkhdiqEKITQL---QSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKE----KSDLEVE 2109
Cdd:pfam15921 562 KVIEILRQQI--------ENMTQLvgqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRElearVSDLELE 633
|
650
....*....|
gi 1655220517 2110 LKKLKGIADE 2119
Cdd:pfam15921 634 KVKLVNAGSE 643
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1572-1973 |
3.29e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1572 AVDAEKQKQNIQLELtqlkNLSEQEIRSKNQQLEEAQVSRRKLEEEI-----HLIRIQ----LQTTIKQkstADDELQKL 1642
Cdd:PRK04863 288 ALELRRELYTSRRQL----AAEQYRLVEMARELAELNEAESDLEQDYqaasdHLNLVQtalrQQEKIER---YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1643 RDQAAEAEKVRKAAQEEAERLRkqvneetqkkknaedelKRKSEAEKEAARQK------QKALDELQKHKMQAEEAERRL 1716
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENE-----------------ARAEAAEEEVDELKsqladyQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1717 KQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK------QEEEANKAREqAE 1790
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagevsRSEAWDVARE-LL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1791 KELETWRLKAN--EALRLRLRaeeEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1868
Cdd:PRK04863 503 RRLREQRHLAEqlQQLRMRLS---ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1869 QKLSAEQEYIRLKADFEHAEQQRglldnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN--TEK 1946
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARA-------PAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERdeLAA 652
|
410 420
....*....|....*....|....*...
gi 1655220517 1947 SKQLLETEALKMKQL-AEEAARLRSVAE 1973
Cdd:PRK04863 653 RKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1565-1801 |
3.60e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1565 ASQRQGLAVDAEKQKQNIQLELTQLknlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1644
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1645 QAAEAEKVRKAAQEE-AERLRK-QVNEETQKKK---NAED--ELKRKSEAEKEAARQKQKALDELQKhkmQAEEAERRLK 1717
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRAlYRLGRQPPLAlllSPEDflDAVRRLQYLKYLAPARREQAEELRA---DLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1718 QAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWR 1797
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....
gi 1655220517 1798 LKAN 1801
Cdd:COG4942 248 FAAL 251
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3957-3995 |
3.81e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 57.72 E-value: 3.81e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 3957 LLEAQNATGGLMDPEYCFHLPTDVAMQRGYINKETLDRI 3995
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
203-299 |
4.24e-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: 59.89 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 203 KKTFTKWVNKHLMKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 267
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 268 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 299
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2546-2810 |
4.33e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 65.24 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2546 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK 2625
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2626 ETASAQQEQMEQQKAMLQ-------QTFLTEKELLlkrerdvedekKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKK 2698
Cdd:COG3883 90 ERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL-----------SKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2699 LQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2778
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1655220517 2779 VSMTTVETTKKVFNGSVEAVKKDGASPLAFEG 2810
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1270-2079 |
5.79e-10 |
|
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: 65.97 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1270 KSYESRLRDVSKVPAEEKEVEAHRSQLKamraeaEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLL 1349
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLK------NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1350 ERWQAVFAQIDLRQREL-SLLGRHMNSYKQSYEWLIQwLREARLR----QEKIEAAPVWDSKALKeqltQEKKLLEEIEK 1424
Cdd:pfam01576 229 AQIAELRAQLAKKEEELqAALARLEEETAQKNNALKK-IRELEAQiselQEDLESERAARNKAEK----QRRDLGEELEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1425 NKDQIENCQkDAKAYIDSLkdyefqilayRALQDPIASPLKKpKMESASDNIIQEYVTLRTRYSE-LSTLTSQyikfiLE 1503
Cdd:pfam01576 304 LKTELEDTL-DTTAAQQEL----------RSKREQEVTELKK-ALEEETRSHEAQLQEMRQKHTQaLEELTEQ-----LE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1504 TQRRledDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAEKQKQNIQ 1583
Cdd:pfam01576 367 QAKR---NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE-----------SERQRAELA 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1584 LELTQLKNlseqEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTikQKSTADDELQKLrdqaAEAEKVRkAAQEEAERL 1663
Cdd:pfam01576 433 EKLSKLQS----ELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT--QELLQEETRQKL----NLSTRLR-QLEDERNSL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1664 RKQVNEETQKKKNAEdelkrkseaekeaaRQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQ 1743
Cdd:pfam01576 502 QEQLEEEEEAKRNVE--------------RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1744 AmsfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlRLRAEEEAQRK------ 1817
Cdd:pfam01576 568 Y----DKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEE---RDRAEAEAREKetrals 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1818 -SLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK---ELEKQRTFAEQIAQQ------------------KLSAEQ 1875
Cdd:pfam01576 641 lARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvhELERSKRALEQQVEEmktqleeledelqatedaKLRLEV 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1876 EYIRLKADF--------EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDelAKVRSEMDaLLQMKIQAEKVSQSNTEKS 1947
Cdd:pfam01576 721 NMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA--AKKKLELD-LKELEAQIDAANKGREEAV 797
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1948 KQLLETEAlKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRAEAEKI-LKEKLAAINEATRlKTEAEVALKAKEAENE 2026
Cdd:pfam01576 798 KQLKKLQA-QMKDLQRELEEARASRDEILAQSK--ESEKKLKNLEAELLqLQEDLAASERARR-QAQQERDELADEIASG 873
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2027 RLKRQAEDEAYQRklLEDQAAQHKHDIQEKitQLQSSSVSELDRQKNIVEETL 2079
Cdd:pfam01576 874 ASGKSALQDEKRR--LEARIAQLEEELEEE--QSNTELLNDRLRKSTLQVEQL 922
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2402-2631 |
7.11e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2402 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRalaekmlkekmqaiQEATKLKAE 2481
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE--------------AELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLED--KQEIQQRLD-----KETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE 2554
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2555 EATRFKKQADEAKVRLQ--ETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2631
Cdd:COG4942 172 ERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2204-2761 |
7.19e-10 |
|
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: 66.02 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2204 AAQKSTAAEQKAQDVLSKNKEDLLSQekLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAeDEAAKQAK 2283
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRT--LDDQ------------------------WKEKRDELNGELSAA-DAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2284 AQKDAerlrkeaeaeaakraaaEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKELGLVKLQLD-------ETDKQKA 2356
Cdd:pfam12128 322 SELEA-----------------LEDQHGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2357 LMDEELQRVKAQVND--------AVKQKAQVENELSKVKMQM------------DELLKLKVRIEEENLRLMQknkdntq 2416
Cdd:pfam12128 383 KIKEQNNRDIAGIKDklakireaRDRQLAVAEDDLQALESELreqleagklefnEEEYRLKSRLGELKLRLNQ------- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2417 kLLAEEAEKMKslaeeaarLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKA 2496
Cdd:pfam12128 456 -ATATPELLLQ--------LENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2497 KKLLEDKQEIQQRLDKETQGFQKSLEAERKRQL--------EISAEAEK-------LKLRVKELSSAQAKAEEEATRfkk 2561
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELlhrtdldpEVWDGSVGgelnlygVKLDLKRIDVPEWAASEEELR--- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2562 qadeAKVRLQETEKQTTETVVQKLETQrlqstreaddLKKAIAELEKEREKLKRDAQELQNkSKETASAQQEQMEQQKAM 2641
Cdd:pfam12128 604 ----ERLDKAEEALQSAREKQAAAEEQ----------LVQANGELEKASREETFARTALKN-ARLDLRRLFDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2642 LQQTFLTEKELLLKRERDVEDEKKKLQKHLED--EVNKAKALKDEQQRQQK---LMDEEKKKLQAIMDEAVKKQKEAEAE 2716
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAwlEEQKEQKREARTEKQAYwqvVEGALDAQLALLKAAIAARRSGAKAE 748
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2717 MKNKQKEME-ALEKKRLEQEKL--LADENKKLREKLESLEVTSKQAAS 2761
Cdd:pfam12128 749 LKALETWYKrDLASLGVDPDVIakLKREIRTLERKIERIAVRRQEVLR 796
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1622-1834 |
8.63e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.44 E-value: 8.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1622 RIQLQttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE---ETQKKKNAEDELKRKSEAEKEAARQKQKA 1698
Cdd:PRK09510 66 RQQQQ----QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKErlaAQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1699 ldeLQKHKMQAEEAERRL----KQAEEEKVRQikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEK 1774
Cdd:PRK09510 142 ---AAAAKAKAEAEAKRAaaaaKKAAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1775 LRKQEEEANKAREQAEKELEtwrlkanealrlrlrAEEEAQRKSLAQEEAEKQKTEAERD 1834
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAK---------------AAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1637-2119 |
9.82e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 9.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1637 DELQKLRDQAAEAEKVRKAAQEEAERLRkQVNEETQKKKNAEDELkRKSEAEKEAAR--QKQKALDELQKhkmQAEEAER 1714
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERL-AELEYLRAALRlwFAQRRLELLEA---ELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1715 RLKQAEEEKVRQikvveEVAQKTAATQLQAmsfsekttkLEESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQAEKEL 1793
Cdd:COG4913 303 ELARLEAELERL-----EARLDALREELDE---------LEAQIRGNGGDRLeQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1794 ET--WRLKANEA--LRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkkakaeeaaLKQKENAEKELEKQRtfaEQIAQQ 1869
Cdd:COG4913 369 AAlgLPLPASAEefAALRAEAAALLEALEEELEALEEALAEAEAA-----------LRDLRRELRELEAEI---ASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1870 KLSAEQEYIRLKADFEHAeqqRGLLDNELQ--------RLKNEV--NAAEK----QRRQL---EDELAKVRSEMDAL-LQ 1931
Cdd:COG4913 435 KSNIPARLLALRDALAEA---LGLDEAELPfvgelievRPEEERwrGAIERvlggFALTLlvpPEHYAAALRWVNRLhLR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1932 MKIQAEKVSQSNTEKSKQLLETEALKMK--------------QLAEEAARLR--SVAE---------------------E 1974
Cdd:COG4913 512 GRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleaELGRRFDYVCvdSPEElrrhpraitragqvkgngtrhE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1975 AKKQRQLAED-----EAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLleDQAAQH 2049
Cdd:COG4913 592 KDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAERE 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2050 KHDIQEKITQLQSSS--VSELDRQkniVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2119
Cdd:COG4913 670 IAELEAELERLDASSddLAALEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1411-2119 |
1.25e-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: 64.66 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1411 QLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlayralqdpIASPLKKPKMESASDNIIQEyvtLRTRYSEL 1490
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKI---------NNSNNKIKILEQQIKDLNDK---LKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1491 STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqaqLETQKQLAEgHAKSVAKAELEAQELKLKMKedasqrqg 1570
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQK-------KENKKNIDK-FLTEIKKKEKELEKLNNKYN-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1571 lavDAEKQKQNIQLELTQLKNlseqEIRSKNQQLEEAQVSRRKLEeeihliriQLQTTIKQKSTADDELQKlrdQAAEAE 1650
Cdd:TIGR04523 163 ---DLKKQKEELENELNLLEK----EKLNIQKNIDKIKNKLLKLE--------LLLSNLKKKIQKNKSLES---QISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1651 KVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV 1730
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKTAATQLQamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLrlra 1810
Cdd:TIGR04523 305 EQDWNKELKSELK--NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE---KQNEIEKL---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 EEEAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQrtfAEQIAQQKLSAEQEYIRLKADFEHAEQQ 1890
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQ---IKKLQQEKELLEKEIERLKETIIKNNSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1891 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmKIQAEKVSQSNTEKSKQLLETEALKmKQLAEEAARLRS 1970
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1971 VAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQA-EDEAYQRKLLEDQAAQH 2049
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSlKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2050 KHDIQEKITqLQSSSVSELDRQKNIVEETLRQ-----------KKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIAD 2118
Cdd:TIGR04523 598 KKDLIKEIE-EKEKKISSLEKELEKAKKENEKlssiiknikskKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
.
gi 1655220517 2119 E 2119
Cdd:TIGR04523 677 D 677
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1654-1914 |
1.35e-09 |
|
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: 63.33 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1654 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1733
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQKTAAtqlqamsfsekttklEESLKKEQGTVLQLQEEAEKlrKQEEEAN-KAREQAEKELETWRLKANEAlrlrLRAEE 1812
Cdd:TIGR02794 125 KAKQAA---------------EAKAKAEAEAERKAKEEAAK--QAEEEAKaKAAAEAKKKAEEAKKKAEAE----AKAKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1813 EAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRG 1892
Cdd:TIGR02794 184 EAEAK--AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSN----------AEKQGG 251
|
250 260
....*....|....*....|..
gi 1655220517 1893 LLDNELQRLKNEVNAAEKQRRQ 1914
Cdd:TIGR02794 252 ARGAAAGSEVDKYAAIIQQAIQ 273
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1184-1722 |
1.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1184 AQKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQQsssapmLRSELDVTLKKMDHvyglssvylDKLKTIDIVIRNTK 1263
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYE------LLAELARLEQDIAR---------LEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1264 DAEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQ 1343
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1344 LAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIE 1423
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1424 KNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILE 1503
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLE---AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1504 tqRRLEDDEKASEKLKEDEKKR--------MAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA 1575
Cdd:COG1196 554 --EDDEVAAAAIEYLKAAKAGRatflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1655
Cdd:COG1196 632 LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhKMQAEEAERRLKQAEEE 1722
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE---PPDLEELERELERLERE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2262-2767 |
1.52e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.55 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2262 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEA-DAEMAKHKKEAEQALKQKSQVEKE 2340
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2341 LGLVKLQLDETDkqkalmDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlKLKVRIEEENLrlmQKNKDNTQKLLA 2420
Cdd:COG4913 325 LDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAEEF---AALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2421 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRA----LAEKMLkEKMQAIQEATKLKAE-----AEELQ-KQKN 2490
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnIPARLL-ALRDALAEALGLDEAelpfvGELIEvRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2491 QAQEKA-------------------KKLLE--DKQEIQQRLDkeTQGFQKSLEAERKRQLEISAEAEKLKLRVkelSSAQ 2549
Cdd:COG4913 474 ERWRGAiervlggfaltllvppehyAAALRwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKP---HPFR 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2550 AKAEEEATRfkkQADEAKVR----LQETEKQTTET---------------------------VVQKLETQRlqstREADD 2598
Cdd:COG4913 549 AWLEAELGR---RFDYVCVDspeeLRRHPRAITRAgqvkgngtrhekddrrrirsryvlgfdNRAKLAALE----AELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2599 LKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKA 2678
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2679 KALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQ 2758
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
....*....
gi 1655220517 2759 AASKTKEIE 2767
Cdd:COG4913 782 LNRAEEELE 790
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2212-2792 |
1.80e-09 |
|
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: 64.60 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2212 EQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERL 2291
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2292 RKEAEAEaakraaaeaaaLKQKQEADAEMAKHKkEAEQALKQKSQVEKELGLVKlQLDETDKQKALMDEELQ-------R 2364
Cdd:TIGR00618 259 QQLLKQL-----------RARIEELRAQEAVLE-ETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQskmrsraK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2365 VKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNT-QKLLAEEAEKMKSLAEEAARLSVEAEET 2443
Cdd:TIGR00618 326 LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTlTQHIHTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2444 ARQRKTAEAELAEQRALAEKMLKEKMQaiQEATKLKAEAEELQKQKNQAQEKAKKLLEdkQEIQQRLDKETQGFQkSLEA 2523
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEKIHL--QESAQSLKEREQQLQ-TKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2524 ERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqetekqtTETVVQKLETQRLQSTREADDLKKAI 2603
Cdd:TIGR00618 481 IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGP---------LTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2604 AELEKEREKLKRDAQELQnksketasaqqeQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHledevnkAKALKD 2683
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQ------------QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-------EDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2684 EQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMkNKQKEMEALEKKRLEQEKLLADENKKL----REKLESLEVTSKQA 2759
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT-ALHALQLTLTQERVREHALSIRVLPKEllasRQLALQKMQSEKEQ 691
|
570 580 590
....*....|....*....|....*....|...
gi 1655220517 2760 ASKTKEIEVQTDKVPEEQLvsmTTVETTKKVFN 2792
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELE---THIEEYDREFN 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2471-2701 |
1.86e-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: 63.24 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2471 AIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2550
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2551 KAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrLQSTREADDLKKAIAELEKEREKLKRDAQELQNKsKETASA 2630
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAAL-RAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2631 QQEQMEQQKAMLQQtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2701
Cdd:COG4942 172 ERAELEALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1599-1828 |
2.05e-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: 62.86 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1599 SKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1678
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1679 DELKRKSE--AEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKL 1754
Cdd:COG4942 97 AELEAQKEelAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 1755 EESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRL--RLRAEEEAQRKSLAQEEAEKQK 1828
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1864-2619 |
2.54e-09 |
|
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: 63.97 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1864 EQIAQQKLSAEQEYIRlKADFEHAEQQRGL---LDNELQRLKNEVNAAEKQRRQLEDELAKVRSemdaLLQMKIQAEKVS 1940
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1941 QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEvALKA 2020
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2021 kEAENERLKRQAedeayqrKLLEDQaaqhkhdiqEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERAS 2100
Cdd:pfam05483 205 -QAENARLEMHF-------KLKEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2101 KEKSDLEVELKklkgIADETQKskakaeeeaeklkklaaEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKA 2180
Cdd:pfam05483 268 DKANQLEEKTK----LQDENLK-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2181 AEANKLKDKAEKELEKqvilaKEAAQKSTAAEQKAQDVlskNKEDLL--SQEKLRDEFENAKKLAQAAETAKEKAEKEAA 2258
Cdd:pfam05483 327 CQLTEEKEAQMEELNK-----AKAAHSFVVTEFEATTC---SLEELLrtEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2259 LLRQKAEEAEKLKKA-AEDEaaKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQV 2337
Cdd:pfam05483 399 FKNNKEVELEELKKIlAEDE--KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2338 EKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK 2417
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2418 LLAEEAE---KMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2494
Cdd:pfam05483 557 FIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2495 KAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ---------------AKAEEEATRF 2559
Cdd:pfam05483 637 KVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQY 716
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2560 KKQADE--AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2619
Cdd:pfam05483 717 DKIIEErdSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
204-298 |
2.97e-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: 57.35 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 204 KTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 275
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1655220517 276 VNIRNDDIADGNPKLTLGLIWTI 298
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1604-2061 |
3.10e-09 |
|
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: 63.49 E-value: 3.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1604 LEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEdelKR 1683
Cdd:NF033838 71 LSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEAT---KK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1684 KSEAEKEAARQKQK-----ALDELQKHKMQAEEAERRLKQAEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESL 1758
Cdd:NF033838 148 VEEAEKKAKDQKEEdrrnyPTNTYKTLELEIAESDVEVKKAELELVKE---------------------EAKEPRDEEKI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1759 KKEQGTVLQLQEEAEKLRKQEEEANKAREqaekeletwrlkanEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDakkk 1838
Cdd:NF033838 207 KQAKAKVESKKAEATRLEKIKTDREKAEE--------------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG---- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1839 AKAEEAALKQKENAEKELEKQrTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRlknevNAAEKQRRQLEDE 1918
Cdd:NF033838 269 VLGEPATPDKKENDAKSSDSS-VGEETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1919 LAKVRSEM-DALLQMkIQAEKVSQSNTEKSKQLLEtealKMKQLAEEAARLrsvaEEAKKQRQLAEDEAARQRAEAEKIl 1997
Cdd:NF033838 343 IAESDVKVkEAELEL-VKEEAKEPRNEEKIKQAKA----KVESKKAEATRL----EKIKTDRKKAEEEAKRKAAEEDKV- 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1998 KEKLAainEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKllEDQAAQHKHDIQEKITQLQ 2061
Cdd:NF033838 413 KEKPA---EQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQA--EEDYARRSEEEYNRLTQQQ 471
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1329-2080 |
4.69e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1329 RLHSERDAELEhyRQLAGSLLERWQAVFAQIDLRqRELSLLGRHMNSYKQSYEWLIQWL---REARLRQEKIEAAPVwDS 1405
Cdd:PRK04863 282 RVHLEEALELR--RELYTSRRQLAAEQYRLVEMA-RELAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIERYQA-DL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1406 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLK----DYE--FQILAYRALQDPIA-SPLKKPK-----MESAS 1473
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqlaDYQqaLDVQQTRAIQYQQAvQALERAKqlcglPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1474 DNI---IQEYVT-----------LRTRYSELSTLTSQYIKfILETQRRLEDD-------EKASEKLKEDEKKRMAEIQAQ 1532
Cdd:PRK04863 438 DNAedwLEEFQAkeqeateellsLEQKLSVAQAAHSQFEQ-AYQLVRKIAGEvsrseawDVARELLRRLREQRHLAEQLQ 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1533 lETQKQLAEghaksvAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELtqlknlsEQEIRSKNQQLEEAQVSRR 1612
Cdd:PRK04863 517 -QLRMRLSE------LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEEL-------EARLESLSESVSEARERRM 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1613 KLEEEIHLIRIQLQTTIKQKS---TADDELQKLRDQAAEA----EKVRKAAQEEAERLRK--QVNEETQKKKNA-EDELK 1682
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPawlAAQDALARLREQSGEEfedsQDVTEYMQQLLEREREltVERDELAARKQAlDEEIE 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAE-KEAARQKQKA----------------LDElqkhkmqAEEAERRLKQAeeekvRQIKVVEEVaqKTAATQLQAM 1745
Cdd:PRK04863 663 RLSQPGgSEDPRLNALAerfggvllseiyddvsLED-------APYFSALYGPA-----RHAIVVPDL--SDAAEQLAGL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1746 ---------------SFSEKTTKLEEslkKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETwrlkanealrLRLRA 1810
Cdd:PRK04863 729 edcpedlyliegdpdSFDDSVFSVEE---LEKAVVVKIADRQWRYSRFPEVPLFGRAAREKRIEQ----------LRAER 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 EEEAQRksLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKqrtfaeqiAQQKLSaEQEyiRLKADFEHAEQQ 1890
Cdd:PRK04863 796 EELAER--YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQ--------LNRRRV-ELE--RALADHESQEQQ 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1891 rglLDNELQRLKNEVNAAEK--------QRRQLEDELAKVRSEMDALLqmkiQAEKVSQSNtEKSKQLLETEALKMKQLA 1962
Cdd:PRK04863 863 ---QRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAE----EAKRFVQQH-GNALAQLEPIVSVLQSDP 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1963 EEAARLRSVAEEAKKQRQlaedeAARQRAEAEKILKEKLAAineatrLKTEAEVALKAKEAE-NERLKRQAEDEAYQRKL 2041
Cdd:PRK04863 935 EQFEQLKQDYQQAQQTQR-----DAKQQAFALTEVVQRRAH------FSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTR 1003
|
810 820 830
....*....|....*....|....*....|....*....
gi 1655220517 2042 LEDQAAQHKHDIQEKiTQLQSSSVSELDRQKNIVEETLR 2080
Cdd:PRK04863 1004 AREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQELKQ 1041
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1602-2110 |
4.75e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.01 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1602 QQLEEAQVSRRKLEEEI-HLIRIQlqttikqksTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQVNEETQKKK 1675
Cdd:COG4913 235 DDLERAHEALEDAREQIeLLEPIR---------ELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1676 NAEDELKRKSEAEKEAARQKQKALDELQKHKMQA-EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS----FSEK 1750
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1751 TTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwRLKANealRLRLRAEEEAQRKSLAQE----EAEK 1826
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--SLERR---KSNIPARLLALRDALAEAlgldEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 Q--------KTEAERdakkkakaeeaalkqKENA-EKELEKQRT-----------FAEQIAQQKLSAEQEYIRLKADFEH 1886
Cdd:COG4913 461 PfvgelievRPEEER---------------WRGAiERVLGGFALtllvppehyaaALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1887 AEQQRGLLDNELQRLKNEVNAAekqRRQLEDELA------KVRSEMD------------------ALLQMKIQAEKVSQ- 1941
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPF---RAWLEAELGrrfdyvCVDSPEElrrhpraitragqvkgngTRHEKDDRRRIRSRy 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1942 ----SNTEKsKQLLETEAlkmKQLAEEAARLRSVAEEAKKQRQLAED--EAARQRAE-----------AEKI--LKEKLA 2002
Cdd:COG4913 603 vlgfDNRAK-LAALEAEL---AELEEELAEAEERLEALEAELDALQErrEALQRLAEyswdeidvasaEREIaeLEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2003 AINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ- 2081
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAa 758
|
570 580 590
....*....|....*....|....*....|.
gi 1655220517 2082 --KKVVEEEIHIIRINFERASKEKSDLEVEL 2110
Cdd:COG4913 759 lgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2463-2736 |
4.81e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2463 KMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGfqksLEAERKRQLEISAEAEKLKLRV 2542
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2543 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE-TVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQ 2621
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2622 NKSKEtasaqqeqmeqqkamlqqtfLTEKElllKRERDVEDEKKKLQKHLED------EVNKAKALKDEQQR-QQKLMDE 2694
Cdd:PRK03918 328 ERIKE--------------------LEEKE---ERLEELKKKLKELEKRLEEleerheLYEEAKAKKEELERlKKRLTGL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1655220517 2695 EKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2736
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1511-1834 |
6.92e-09 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 62.05 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1511 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvakaeleAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQ-- 1588
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEFNQKRAK--------FKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1589 --LKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKqkstaDDELQ---KLRDQAAEAEKVRKAAQEEAERL 1663
Cdd:pfam03528 75 aeMENIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVR-----EYEVQfhrRLEQERAQWNQYRESAEREIADL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1664 RKQVNEeTQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvAQKTAATQLQ 1743
Cdd:pfam03528 150 RRRLSE-GQEEENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELNHYLE-AEKSCRTDLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1744 amsfsekttkLEESLKKEQGTVLQlqEEAEKLRKQEEEANKAREQAEKE---------------LETWRLKANEALRL-- 1806
Cdd:pfam03528 228 ----------MYVAVLNTQKSVLQ--EDAEKLRKELHEVCHLLEQERQQhnqlkhtwqkandqfLESQRLLMRDMQRMes 295
|
330 340 350
....*....|....*....|....*....|...
gi 1655220517 1807 -----RLRAEEEAQRKSlaQEEAEKQKTEAERD 1834
Cdd:pfam03528 296 vltseQLRQVEEIKKKD--QEEHKRARTHKEKE 326
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2419-2801 |
7.85e-09 |
|
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: 62.05 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLaeeaaRLSVEAEetarqRKTAEAELAEQRALAEKMLK--EKMQAIQEATKLKAEaEELQKQKNQAQEK- 2495
Cdd:pfam05483 83 LYKEAEKIKKW-----KVSIEAE-----LKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLE-EEIQENKDLIKENn 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2496 -AKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSsAQAKAEEEATRFKKQADEAKVR-LQET 2573
Cdd:pfam05483 152 aTRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELR-VQAENARLEMHFKLKEDHEKIQhLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2574 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKR--DAQELQNKSKETASAQQE----QMEQQKAMLQQTFL 2647
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQleEKTKLQDENLKELIEKKDhltkELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2648 TEKELllkrERDVEDEKKKLQKHLED------EVNKAKA-------------------LKDEQQRQQKLMDEekkkLQAI 2702
Cdd:pfam05483 311 TQKAL----EEDLQIATKTICQLTEEkeaqmeELNKAKAahsfvvtefeattcsleelLRTEQQRLEKNEDQ----LKII 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2703 MDEAVKKQKEAEAEMKNKQ-KEMEALE-KKRLEQEKLLADENKKLREKLESLEVTSKQAAS--KTKEIEVQtdkvpeEQL 2778
Cdd:pfam05483 383 TMELQKKSSELEEMTKFKNnKEVELEElKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFllQAREKEIH------DLE 456
|
410 420
....*....|....*....|...
gi 1655220517 2779 VSMTTVETTKKVFNGSVEAVKKD 2801
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1633-2083 |
7.96e-09 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 62.38 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1633 STADDELQkLRDQAAEAEKVRKAAQEEaerlrkqVNEETQKKKNAEDElkRKSEAEKeaARQKQKALDELQKhkMQAEEa 1712
Cdd:PRK10929 20 ATAPDEKQ-ITQELEQAKAAKTPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPK--LSAEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1713 eRRLKQAEEEKVRQIkvveEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1792
Cdd:PRK10929 85 -RQQLNNERDEPRSV----PPNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1793 LEtwrlkaneALRLRLRAEEEAQRKSLaQEEAEKQKTEAErdakkkakaeeaalkqkenaekELEkqrtfaeqIAQqkLS 1872
Cdd:PRK10929 160 LQ--------TLGTPNTPLAQAQLTAL-QAESAALKALVD----------------------ELE--------LAQ--LS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1873 A--EQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAaekqRRQLEDELAKVRSEMdallqmkiQAEKVSQSNTEKSKQL 1950
Cdd:PRK10929 199 AnnRQELARLRSELAKKRSQQ--LDAYLQALRNQLNS----QRQREAERALESTEL--------LAEQSGDLPKSIVAQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1951 LETEALKMkQLAEEAARLRSVAEeakKQRQLAEDeaARQRAEAEKILKEKL------AAINEATRlkteAEVALKAKEAE 2024
Cdd:PRK10929 265 KINRELSQ-ALNQQAQRMDLIAS---QQRQAASQ--TLQVRQALNTLREQSqwlgvsNALGEALR----AQVARLPEMPK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2025 NERLKRQAEDEAYQRKLLEDQAAQhkhdiQEKITQLQSSSVSEL-DRQKNIVEETLRQKK 2083
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNK-----QPQLRQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2446-2642 |
7.98e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2446 QRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAER 2525
Cdd:PRK09510 68 QQQQKSAKRAEEQ-------RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA--KQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2526 KRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF------KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDL 2599
Cdd:PRK09510 139 AKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKaeaeaaKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220517 2600 KKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAML 2642
Cdd:PRK09510 217 KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2260-2620 |
8.04e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 61.83 E-value: 8.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2260 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKE--------AEQAL 2331
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELsasseelsEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2332 KQKSQVEKELGLVKLQLD-ETDKQKALMDE-ELQRVKAQVNDAVKQKAQVENElskvkmqmDELLKLKVRIEEENLRLMQ 2409
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2410 KNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKmqaiQEATKLKAEAEELQKQK 2489
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2490 NQAQ-EKAKKLLEDKQ-------------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2555
Cdd:pfam07888 268 DRTQaELHQARLQAAQltlqladaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2556 ATRFKkqaDEAKVRLQETEkqttetvvqkletqrlqstREADDLKKAIAELEKEREKLKRDAQEL 2620
Cdd:pfam07888 348 LGREK---DCNRVQLSESR-------------------RELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2164-2772 |
8.31e-09 |
|
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: 62.44 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQ------DVLSKNKEDLLSQEK-LRDE 2235
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANsELTEARTERDQFSQesgnldDQLQKLLADLHKREKeLSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2236 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLK---KAAEDEAAKQAKAQKDAerlrkeaeaeaakraaaeaaaLKQ 2312
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEallKAMKSECQGQMERQMAA---------------------IQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2313 KQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDE 2392
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE---ATNAEITKLRSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2393 LLKLK--------VRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARlsveaeetarqrkTAEAelaeqralaekM 2464
Cdd:pfam15921 533 LQHLKnegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR-------------TAGA-----------M 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2465 LKEKMQAIQEATKLKAEAEELqkqknqaqekakKLLEDKQEIQQRldketqgfqkSLEAeRKRQLEIsaeaEKLKLrvke 2544
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEF------------KILKDKKDAKIR----------ELEA-RVSDLEL----EKVKL---- 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 lssaqAKAEEEATRfkkqadeakvrlqetekqttetVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDaqeLQNKS 2624
Cdd:pfam15921 638 -----VNAGSERLR----------------------AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---FRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2625 KE---TASAQQEQMEQQKAMLQQTFLTekellLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEkkklqa 2701
Cdd:pfam15921 688 EEmetTTNKLKMQLKSAQSELEQTRNT-----LKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA------ 756
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2702 iMDEAvkkqkeaeaemkNKQKEMEALEKKRLEQE-KLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2772
Cdd:pfam15921 757 -MTNA------------NKEKHFLKEEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
202-301 |
8.58e-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: 56.36 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILH 301
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2316-2557 |
8.75e-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: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2316 ADAEMAKHKKEAEQALKQKSQVEKelglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL- 2394
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2395 KLKVRIeeenlRLMQKNKDNTQKLLA-EEAEKMKSLAEEAARLSVEAE---ETARQRKTAEAELAEQRALAEKMLKEKMQ 2470
Cdd:COG3883 87 ELGERA-----RALYRSGGSVSYLDVlLGSESFSDFLDRLSALSKIADadaDLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2471 AIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQA 2550
Cdd:COG3883 162 LKAE---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
....*..
gi 1655220517 2551 KAEEEAT 2557
Cdd:COG3883 239 AAAAAAS 245
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
317-416 |
9.18e-09 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 56.23 E-value: 9.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYrQSNQ--ENLEQAFSVAERELGVTRLL 394
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1655220517 395 DPEDVDVAHPDEKSIITYVSSL 416
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1682-2115 |
1.06e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1682 KRKSEAEKEAARQKQKALDELqkhkmqaEEAERRLKQAEEEKVRQIKVVEEVAQKTAatQLQAMSFSEKTTKLEESLKKE 1761
Cdd:COG4717 53 KEADELFKPQGRKPELNLKEL-------KELEEELKEAEEKEEEYAELQEELEELEE--ELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1762 QGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkanealrlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKkkaka 1841
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELR---------ELEEELEELEAELAELQEELEELLEQLSLA----- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1842 eeaalkqkenAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR--------- 1912
Cdd:COG4717 190 ----------TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1913 --RQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQR 1990
Cdd:COG4717 260 alLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1991 AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRKLLEDQAAQHKHDIQEKITQLQSSSVSEL 2068
Cdd:COG4717 340 LELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2069 DRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKG 2115
Cdd:COG4717 420 ELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1634-1873 |
1.28e-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: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1634 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1713
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1714 RRLKQAEeekvRQIKVVEEVAQ----KTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQ 1788
Cdd:COG3883 93 RALYRSG----GSVSYLDVLLGsesfSDFLDRLSALSkIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1789 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQ 1868
Cdd:COG3883 169 AKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
....*
gi 1655220517 1869 QKLSA 1873
Cdd:COG3883 248 GAGAA 252
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1503-1833 |
1.28e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 61.04 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMKEdasqrqglavdaekQKQNI 1582
Cdd:pfam02029 53 SGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDP-----------TIADEKESVAE--------------RKENN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1583 QLEltqlknlseqeirSKNQQLEEAQVSRRKLEEEIHliriqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAER 1662
Cdd:pfam02029 108 EEE-------------ENSSWEKEEKRDSRLGRYKEE------ETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1663 LRKQV-NEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtq 1741
Cdd:pfam02029 169 VPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ----NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEV-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1742 lqamsFSEKTTKLEESLKKEQGTVlqlQEEAEKLRKQEEEANKAREQAEKELEtWRLKANEALRLRlRAEEEAQRKSLAQ 1821
Cdd:pfam02029 243 -----FLEAEQKLEELRRRRQEKE---SEEFEKLRQKQQEAELELEELKKKRE-ERRKLLEEEEQR-RKQEEAERKLREE 312
|
330
....*....|..
gi 1655220517 1822 EEAEKQKTEAER 1833
Cdd:pfam02029 313 EEKRRMKEEIER 324
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1295-1724 |
1.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1295 QLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL--AGSLLERWQAVFAQIDLRQRELSLLGRH 1372
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1373 MNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKdyefQILA 1452
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE----EELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1453 YRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFI-----------LETQRRLEDDEKASEKLKED 1521
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1522 EKKRM---AEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlSEQEIR 1598
Cdd:COG4717 311 PALEEleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE--DEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1599 SKNQQLEEaqvsRRKLEEEIHLIRIQLQTTIKQKSTADDELQK--LRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKN 1676
Cdd:COG4717 389 AALEQAEE----YQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1677 AE--DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKV 1724
Cdd:COG4717 465 LEedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2383-2780 |
1.47e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2383 LSKVKMQMDELLKLKVRIEEENLRLMQKNkdntQKLLAEEAEKMKSLAEEAARLsveaEETARQRKTAEAELAEQRALae 2462
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREE-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2463 kmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRV 2542
Cdd:COG4717 118 ---LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2543 KELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIA------------------ 2604
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2605 -----------------ELEKEREKLKRDAQELQNKSKETASAQQEQMEQ----------QKAMLQQTFLTEKELLLKRE 2657
Cdd:COG4717 275 iagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELlaalglppdlSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2658 RDVEDEKKKLQKHLEDEVN---KAKALKDEQQRQQKLMDEEKKKlqaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQ 2734
Cdd:COG4717 355 EAEELEEELQLEELEQEIAallAEAGVEDEEELRAALEQAEEYQ------ELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1655220517 2735 EklLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVS 2780
Cdd:COG4717 429 E--LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA 472
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2310-2644 |
1.71e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.51 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLdeTDKQKALmdEELQRVKAQVNDAVKQKAQVENELskvkmQ 2389
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEA---RLEAAEEEVDSLKSQL--ADYQQAL--DVQQTRAIQYQQAVQALEKARALC-----G 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2390 MDELlklkvriEEENLrlmqknKDNTQKLLAEEAEKMKSLAEEAARLSVeAEETARQRktaEAELAEQRALAEKMlkEKM 2469
Cdd:COG3096 431 LPDL-------TPENA------EDYLAAFRAKEQQATEEVLELEQKLSV-ADAARRQF---EKAYELVCKIAGEV--ERS 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2470 QAIQEATKLKAEAEELQKQKNQAQEKAKKL--LEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSS 2547
Cdd:COG3096 492 QAWQTARELLRRYRSQQALAQRLQQLRAQLaeLEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2548 AQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREkLKRDAQELQ 2621
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARapawlAAQDALERLREQSGEALADSQEVTAAMQQlLERERE-ATVERDELA 650
|
330 340
....*....|....*....|...
gi 1655220517 2622 nksketasAQQEQMEQQKAMLQQ 2644
Cdd:COG3096 651 --------ARKQALESQIERLSQ 665
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
321-416 |
1.80e-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: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 321 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-----------------------EN 376
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 377 LEQAFSVAER-----------ELG-VTRLLDPEDVDVAHPDEKSIITYVSSL 416
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1311-1757 |
1.85e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1311 DRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREA 1390
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1391 RLRQEKieaapvwdsKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQIlaYRALQDPiasplkKPKME 1470
Cdd:COG4717 129 PLYQEL---------EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL--EELLEQL------SLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1471 SASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKA 1550
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1551 ELEAQEL------------------KLKMKEDASQRQGLAVDAEKQKQNIQLELTQL---KNLSEQEIRSKNQQLEEAQV 1609
Cdd:COG4717 272 ILTIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALglpPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1610 SRRKLEEEIHLIRIQ-LQTTIKQ-----KSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE-----ETQKKKNAE 1678
Cdd:COG4717 352 LLREAEELEEELQLEeLEQEIAAllaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEleellEALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1679 DELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEE 1756
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAelEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
.
gi 1655220517 1757 S 1757
Cdd:COG4717 512 E 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1900-2581 |
2.49e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.42 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1900 RLKNEVNAAEKQRRQLEDELAKVRSEM--------DALLQMKIQAEKVSQSNTE------KSKQL---LETEALKMKQLA 1962
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1963 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEaevaLKAKEAENERLKRQAEDEAYQRKLL 2042
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2043 EDQaaqhKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFErASKEKSDLEVELKKLKGIADETQK 2122
Cdd:TIGR04523 179 EKE----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ-LKDNIEKKQQEINEKTTEISNTQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2123 skakaeeeaeklkklaaeeerkrreaeeKVKKIAAAEEEAARQRKAAQDEVERLKQKAaeanklkdkaeKELEKQviLAK 2202
Cdd:TIGR04523 254 ----------------------------QLNQLKDEQNKIKKQLSEKQKELEQNNKKI-----------KELEKQ--LNQ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2203 EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENA---------------KKLAQAAETAKEKAEKEAALLRQKAEEA 2267
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2268 EKLKKAAED--EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQ-KQEADAEMAKHKKEAEQALKQKSQVEKELGLV 2344
Cdd:TIGR04523 373 EKLKKENQSykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2345 KLQLDETDKQKALMDEELQRVKAQVNdavKQKAQVENELSKVKMQMDELLKLKvrieEENLRLMQKNKDNTQkllaeeae 2424
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSIN---KIKQNLEQKQKELKSKEKELKKLN----EEKKELEEKVKDLTK-------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2425 KMKSLAEEAARLSVEAEETARQRKTAEAELAE--QRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLED 2502
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2503 KQEIQQRLDKETQgfqksLEAERKRQLE-ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETV 2581
Cdd:TIGR04523 598 KKDLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2164-2514 |
2.90e-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: 59.91 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKqkaAEANKLKDKAEKELEKQvilakEAAQKSTAAEQKAQDVLSKNKEDllSQEKLRDEFENAKKLA 2243
Cdd:pfam07888 73 RQRRELESRVAELK---EELRQSREKHEELEEKY-----KELSASSEELSEEKDALLAQRAA--HEARIRELEEDIKTLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2244 QAAETAKEKAEKeaalLRQKAEEAEKLKKAAEDE-AAKQAKAQKDAERLRKEAE--AEAAKRAAAEAAALKQKQEADAEM 2320
Cdd:pfam07888 143 QRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQTEEELRSLSKefQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2321 AKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQ-------RVKAQVNDAVKQKAQVENELSKVKMQMDEL 2393
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQARLQAAQLTLQLADASLALREG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2394 lKLKVRIEEENLRL-MQKNKDNTQKLLAEEAEKMKSLAEEAArlsveaeetarQRKTAEAELAEQRALAEKMLKEKMQAI 2472
Cdd:pfam07888 299 -RARWAQERETLQQsAEADKDRIEKLSAELQRLEERLQEERM-----------EREKLEVELGREKDCNRVQLSESRREL 366
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655220517 2473 QEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKET 2514
Cdd:pfam07888 367 QE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2408-2673 |
2.95e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.88 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2408 MQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEaTKLKAEAEELQK 2487
Cdd:pfam02029 68 TAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE-IREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2488 QKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAK 2567
Cdd:pfam02029 147 TEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2568 VRLQETEKQTTETVVQKLET-QRLQSTREADDlKKAIAELEKEREKLKRDAQELQ---NKSKETASAQQEQMEQQKAMLQ 2643
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAeQKLEELRRRRQ-EKESEEFEKLRQKQQEAELELEelkKKREERRKLLEEEEQRRKQEEA 305
|
250 260 270
....*....|....*....|....*....|....
gi 1655220517 2644 QTFLTEKELLLKRERDVEDEK----KKLQKHLED 2673
Cdd:pfam02029 306 ERKLREEEEKRRMKEEIERRRaeaaEKRQKLPED 339
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1752-2113 |
3.16e-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: 59.91 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1752 TKLEESLKkEQGTVLQLQEEAEKLRKQEeeankaREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1831
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKE------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1832 ERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQ 1911
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1912 RRQLEDELAKVRSEMD----ALLQMKIQAEKVSQSNTEKSKQLLETEALK--MKQLAEEAARLRSVAEEAKkqRQLAEDE 1985
Cdd:pfam07888 187 LRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1986 AARQRAEAEkILKEKLAAINEATRLkTEAEVALKAKEA----ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQ 2061
Cdd:pfam07888 265 AQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2062 SSSVsELDRQKNIveeTLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKL 2113
Cdd:pfam07888 343 KLEV-ELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1195-1720 |
3.73e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.92 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1195 SELEGLKKDLNSITEKTEEIlaspqqSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTIDIVIRNTKDAEDTVKSYES 1274
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENI------KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1275 RLR--DVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKmTRLHSERDAELEHYRQlAGSLLERW 1352
Cdd:PRK01156 257 EIKtaESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHA-IIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1353 QAVFAQIDLRQRE--------LSLLGRHMN--SYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEI 1422
Cdd:PRK01156 335 QKDYNDYIKKKSRyddlnnqiLELEGYEMDynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1423 EKNKDQIENCQKDAKAYIDSLKDYEFQILAYRA-LQDPIASPLKKPKM-ESASDNIIQEYVTLRTRyselstltsqyikf 1500
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMEmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSR-------------- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1501 ILETQRRLEDDEKASEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDaekqkq 1580
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESE-EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN------ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 niqleltQLKNLSEQEIRSKNQQLEEAQVSRRKLeeEIHLIRIQLQTTIKQKSTADDELQKLR----DQAAEAEKVRKAA 1656
Cdd:PRK01156 554 -------RYKSLKLEDLDSKRTSWLNALAVISLI--DIETNRSRSNEIKKQLNDLESRLQEIEigfpDDKSYIDKSIREI 624
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1657 QEEAERLRKQVNeETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE 1720
Cdd:PRK01156 625 ENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2322-2616 |
3.81e-08 |
|
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: 58.67 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2322 KHKKEAEQALKQKSQvEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK-------AQVENELSKVKmQMDELL 2394
Cdd:pfam15905 64 KSQKNLKESKDQKEL-EKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKtslsasvASLEKQLLELT-RVNELL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2395 KLKVrieeenlrlmqkNKDNTQKllaeeaeKMKSLAEEAARLsveaeetarqRKTAEAELAEQRALAEKMLKeKMQAIQe 2474
Cdd:pfam15905 142 KAKF------------SEDGTQK-------KMSSLSMELMKL----------RNKLEAKMKEVMAKQEGMEG-KLQVTQ- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2475 aTKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAErKRQLEISAEAEKLKLRVKELSSAQAKAEE 2554
Cdd:pfam15905 191 -KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVE-KYKLDIAQLEELLKEKNDEIESLKQSLEE 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2555 EATRFKKQADEAKVRLQETEKQtTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRD 2616
Cdd:pfam15905 269 KEQELSKQIKDLNEKCKLLESE-KEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2455-2680 |
3.88e-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: 59.01 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2455 AEQRALAEKMLKEKMQAIQEATK----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLE 2530
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAA----LEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2531 ISAEAEKLKLRVKE-LSSAQAKAEEEATRFKKQADEAK--VRLQETEKQTTETVVQKLETQRlqstREADDLKKAIAELE 2607
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLSPEDFLdaVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2608 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKEL--LLKRERDVEDEKKKLQKHLEDEVNKAKA 2680
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELaeLQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1479-1969 |
3.98e-08 |
|
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: 59.84 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1479 EYVTLRTRyseLSTLTSQYikfiletqrrlEDDEKASEKLKED---EKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQ 1555
Cdd:pfam10174 304 ELLALQTK---LETLTNQN-----------SDCKQHIEVLKESltaKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1556 ELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQeIRSKNQQLEEAQVSRRKLEEEihliriqlqttikqKSTA 1635
Cdd:pfam10174 370 DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQ-LRDKDKQLAGLKERVKSLQTD--------------SSNT 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1636 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKmqAEEAERR 1715
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA--SSLASSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1716 LKQAEEEKVRQIkvveEVAQKTaatqlqamsfsEKTTKLEESLKKEQGTVLQLQ---EEAEKLRKQEEEANKAREQAEK- 1791
Cdd:pfam10174 513 LKKDSKLKSLEI----AVEQKK-----------EECSKLENQLKKAHNAEEAVRtnpEINDRIRLLEQEVARYKEESGKa 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1792 ELETWRLKanEALRlRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEkELEKQRTfaEQIAQQKL 1871
Cdd:pfam10174 578 QAEVERLL--GILR-EVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQ-LLEEARR--REDNLADN 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1872 SAEQEYIRLKADFEHAEQQrglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL 1951
Cdd:pfam10174 652 SQQLQLEELMGALEKTRQE---LDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDANIALL 728
|
490
....*....|....*...
gi 1655220517 1952 ETEALKMKQLAEEAARLR 1969
Cdd:pfam10174 729 ELSSSKKKKTQEEVMALK 746
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2165-2646 |
4.51e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2165 QRKAAQDEVERLKQKAAEANKLKDKAEkELEKQvilaKEAAQkstAAEQKAQDVLSKNKEDLLSQEKLRDEFEnakKLAQ 2244
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIE-RYEEQ----REQAR---ETRDEADEVLEEHEERREELETLEAEIE---DLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2245 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADA------ 2318
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAhneeae 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2319 ----EMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELl 2394
Cdd:PRK02224 346 slreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2395 KLKVRIEEENLRLMQKNKDNTQKLLA-----------EEAEKMKSLAE--------EAARLSVEAEETARQRKTAEAE-- 2453
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEagkcpecgqpvEGSPHVETIEEdrerveelEAELEDLEEEVEEVEERLERAEdl 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2454 ---------LAEQRALAEKMLKEKMQAIQE-----------ATKLKAEAEELQKQKNQAQEKAKKLLE-------DKQEI 2506
Cdd:PRK02224 505 veaedrierLEERREDLEELIAERRETIEEkreraeelrerAAELEAEAEEKREAAAEAEEEAEEAREevaelnsKLAEL 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2507 QQRLDketqgfqkSLEAERKRQLEIsAEAEKLKLRVKELSSAQAKAEEE------ATRFKKQADEAKV---RLQE--TEK 2575
Cdd:PRK02224 585 KERIE--------SLERIRTLLAAI-ADAEDEIERLREKREALAELNDErrerlaEKRERKRELEAEFdeaRIEEarEDK 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2576 QTTETVVQKLETQRLQSTREADDLKKAI-------AELEKEREKLKR-------------DAQELQNKSKET-ASAQQEQ 2634
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIgavenelEELEELRERREAlenrvealealydEAEELESMYGDLrAELRQRN 735
|
570
....*....|..
gi 1655220517 2635 MEQQKAMLQQTF 2646
Cdd:PRK02224 736 VETLERMLNETF 747
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1698-2291 |
4.70e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1698 ALDELQKHKMQAEEAERRLKQAEEeKVRQIKVVEEVAQKTAATQLQAmsfsektTKLEESlkKEQGTVLQLQEEAEKLRK 1777
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAARERL-------AELEYL--RAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1778 QEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQ-EEAEKQKTEAERdakkkakaeeaalkQKENAEKEL 1856
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLER--------------ELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1857 EKQRTFAEQIAQQKLSAEQEYIRLKAdfeHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiqa 1936
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER----- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1937 ekvSQSN-TEKSKQLLEteALKmKQLAEEAARLRSVAEEAkkqrQLAEDEAARQRAeAEKIL--------------KEKL 2001
Cdd:COG4913 434 ---RKSNiPARLLALRD--ALA-EALGLDEAELPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAAL 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2002 AAINeATRLKTEAeVALKAKEAENERLKRQAEDEAYQRKL----------LEDQAAQHKHDIQ-EKITQL---------- 2060
Cdd:COG4913 503 RWVN-RLHLRGRL-VYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCvDSPEELrrhpraitra 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2061 ----QSSSVSELDRQKNIVEE------TLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEE 2130
Cdd:COG4913 581 gqvkGNGTRHEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2131 AEKLKKLaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKqkaaEANKLKDKAEKELEKQVILAKEAAQKSTA 2210
Cdd:COG4913 661 IDVASAE--------------------------REIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2211 AEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEE-AEKLKKAAEDEAAKQAKAQKDAE 2289
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElRENLEERIDALRARLNRAEEELE 790
|
..
gi 1655220517 2290 RL 2291
Cdd:COG4913 791 RA 792
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1854-2290 |
5.36e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1854 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQ 1931
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1932 mkiqaekvsqsntekskqlletealKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLK 2011
Cdd:COG4717 154 -------------------------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2012 TEAEVALKAKEAENERLKRQAEDEayqRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHI 2091
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2092 IRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQD 2171
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2172 EvERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdLLSQEKLRDEFENAKKLAQAAETAKE 2251
Cdd:COG4717 366 E-ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE-LEELLEALDEEELEEELEELEEELEE 443
|
410 420 430
....*....|....*....|....*....|....*....
gi 1655220517 2252 KAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAER 2290
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELEELK 482
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2187-2628 |
5.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2187 KDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKlaqaaetakekaekEAALLRQKAEE 2266
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA--------------ELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2267 AEKLKKAAEDEAAKQAKAQKDAErlRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKS-QVEKELGLVK 2345
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAE--LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2346 LQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQmDELLKLKVRIEEENLRL----MQKNKDNTQKLLAE 2421
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLallgLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2422 EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA--------IQEATKLKAEAEELQKQKNQAQ 2493
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlsPEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2494 EKAKKLleDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVrlqET 2573
Cdd:COG4717 358 ELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL---EE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2574 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKERE--KLKRDAQELQNKSKETA 2628
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELA 489
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1654-1840 |
5.68e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1654 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEV 1733
Cdd:PRK09510 75 KRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----------QAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQKTAATQlqAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA-NKAREQAEKELETwRLKANEALRLRLRAEE 1812
Cdd:PRK09510 145 AKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAaAKAAAEAKKKAEA-EAKKKAAAEAKKKAAA 221
|
170 180
....*....|....*....|....*...
gi 1655220517 1813 EAQRKSLAQEEAEKQKTEAERDAKKKAK 1840
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4198-4234 |
6.10e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.33 E-value: 6.10e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1655220517 4198 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4234
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1545-2122 |
6.56e-08 |
|
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: 58.99 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1545 KSVAKAELEAQELKLKMKED--ASQRQGLAvdaekqKQNIQLELTQLKNLSEQ-EIRSKnqQLEEAqvsrRKLEEEIHLI 1621
Cdd:pfam07111 18 QDVLERRLDTQRPTVTMWEQdvSGDGQGPG------RRGRSLELEGSQALSQQaELISR--QLQEL----RRLEEEVRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1622 RiqlQTTIKQKstaddelQKLRDQAAEAEKV---RKAAQEEAERLR-----------------------------KQVNE 1669
Cdd:pfam07111 86 R---ETSLQQK-------MRLEAQAMELDALavaEKAGQAEAEGLRaalagaemvrknleegsqreleeiqrlhqEQLSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1670 ETQKKKNAEDELKRKSEA-EKEAARQKQKALDELQKHKMQAEEAE---RRLKQAEEEKVRQIKVVEEVAQ---------- 1735
Cdd:pfam07111 156 LTQAHEEALSSLTSKAEGlEKSLNSLETKRAGEAKQLAEAQKEAEllrKQLSKTQEELEAQVTLVESLRKyvgeqvppev 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1736 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRK----QEEEANKARE-----------QAEKELETWRLKA 1800
Cdd:pfam07111 236 HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHmlalQEEELTRKIQpsdslepefpkKCRSLLNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1801 NeALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIA-----------QQ 1869
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMElsraqearrrqQQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1870 KLSAEQEYIRLKADFEHAEQQRglLDNELQRLKNEVNAAEKQRRQLEDELAKVRSeMDALLQMKIQAEKVSQSNTEKSKQ 1949
Cdd:pfam07111 395 QTASAEEQLKFVVNAMSSTQIW--LETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKVALAQLRQESCPPPPP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1950 LLETEA---LKMKQLAEEAARLRSvaeEAKKQRQLAEDEA--ARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 2024
Cdd:pfam07111 472 APPVDAdlsLELEQLREERNRLDA---ELQLSAHLIQQEVgrAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2025 NERLKRQ--AEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRinfERASKE 2102
Cdd:pfam07111 549 VARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQ---HRATQE 625
|
650 660
....*....|....*....|
gi 1655220517 2103 KSDLEvELKKLKgiaDETQK 2122
Cdd:pfam07111 626 KERNQ-ELRRLQ---DEARK 641
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1742-1988 |
6.74e-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: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1742 LQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQRKSLAQ 1821
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA----ALARRIR-ALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1822 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELE---KQRTFAEqiAQQKLSAEQEYIRlkADFEHAEQQRGLLDnEL 1898
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLD--AVRRLQYLKYLAP--ARREQAEELRADLA-EL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1899 QRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQ 1978
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1655220517 1979 RQLAEDEAAR 1988
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1406-1953 |
6.77e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1406 KALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPIASPLKKPKMESASDNIIqeYVTLRT 1485
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL--LSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1486 RYSELSTLTSQYIKFIlETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEda 1565
Cdd:TIGR04523 209 KIQKNKSLESQISELK-KQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1566 sqrqglavdAEKQKQNIQLELTQLKNLSEQ--------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1637
Cdd:TIGR04523 286 ---------LEKQLNQLKSEISDLNNQKEQdwnkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1638 ELQKLRDQAAEA----EKVRKAAQ---EEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1710
Cdd:TIGR04523 357 ENSEKQRELEEKqneiEKLKKENQsykQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1711 EAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE 1790
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRE-------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1791 KELETwrlkanealrlrLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaEQIAQQK 1870
Cdd:TIGR04523 510 EKVKD------------LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN---KEIEELK 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1871 lsaeQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQL 1950
Cdd:TIGR04523 575 ----QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
...
gi 1655220517 1951 LET 1953
Cdd:TIGR04523 651 KET 653
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1640-1833 |
7.24e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.64 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1640 QKLRDQAAEAEKVRKAAQEEAERLRKQvneetqKKKNAEDE-LKRKSEAEKEaARQKQKaldELQKhkmqaeeAERRLKQ 1718
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE------ALLEAKEEiHKLRNEFEKE-LRERRN---ELQK-------LEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1719 AEEEKVRQikvveevaqktaatqlqamsfSEKTTKLEESLKKEQGTVLQLQEEAEklrKQEEEANKAREQAEKELETW-R 1797
Cdd:PRK12704 94 KEENLDRK---------------------LELLEKREEELEKKEKELEQKQQELE---KKEEELEELIEEQLQELERIsG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1655220517 1798 LKANEA---LRLRLRAEEEAQRKSLAQEEAEKQKTEAER 1833
Cdd:PRK12704 150 LTAEEAkeiLLEKVEEEARHEAAVLIKEIEEEAKEEADK 188
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2360-2752 |
7.36e-08 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 59.30 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2360 EELQRVKAQVNDAvkQKAQVEnELSKVKMQMDELLKLKVRIEEenlrlMQKNKDNTQKLLAEEAEKMKSLAEEaaRLSVE 2439
Cdd:PRK10929 30 QELEQAKAAKTPA--QAEIVE-ALQSALNWLEERKGSLERAKQ-----YQQVIDNFPKLSAELRQQLNNERDE--PRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2440 AEETArqrktaeAELaEQRAL--AEKMLKEKMQAIQEATKLKAEAEELQkQKNQAQEKAKKLLedkQEIQQRLdkETQGF 2517
Cdd:PRK10929 100 PNMST-------DAL-EQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL---NEIERRL--QTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2518 QKSLEAERKRQLeISAEAEKLKLRVKELSSAQAKA--EEEATR-----FKKQADEAKVRLQETEKQTTETVVQKLEtQRL 2590
Cdd:PRK10929 166 PNTPLAQAQLTA-LQAESAALKALVDELELAQLSAnnRQELARlrselAKKRSQQLDAYLQALRNQLNSQRQREAE-RAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2591 QSTR----EADDLKKAI-AELEKERE---KLKRDAQELqnkskETASAQQEQMEQQKAMLQQTFLTekellLKRERDVED 2662
Cdd:PRK10929 244 ESTEllaeQSGDLPKSIvAQFKINRElsqALNQQAQRM-----DLIASQQRQAASQTLQVRQALNT-----LREQSQWLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2663 EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaiMDEAVKKQKEaeaEMKNKQKEMEALEKkrlEQEKLLADEN 2742
Cdd:PRK10929 314 VSNALGEALRAQVARLPEMPKPQQLDTEMAQLRVQRLR--YEDLLNKQPQ---LRQIRQADGQPLTA---EQNRILDAQL 385
|
410
....*....|
gi 1655220517 2743 KKLREKLESL 2752
Cdd:PRK10929 386 RTQRELLNSL 395
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1567-1765 |
8.35e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1567 QRQGLAVDAEKQKQNIQleltqlknlsEQEIRSKNQQLEEAQVSRRKLEEEihliRIQLQTTIKQKSTADDELQKLRDQA 1646
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE----------QQQAEELQQKQAAEQERLKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1647 AEAEKV-----RKAAQEEAERLR---KQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ 1718
Cdd:PRK09510 135 EEAAAKaaaaaKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220517 1719 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEEslKKEQGTV 1765
Cdd:PRK09510 215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA--AKAAAEV 259
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1626-1997 |
8.48e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1626 QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQvneetqkkKNAEDELKRKSEAEKEAArQKQKALDELQKH 1705
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER--------REALQRLAEYSWDEIDVA-SAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1706 KMQAEEAERRLKQAEEekvrqikvveevaqktaatQLQAmsfsekttkLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA 1785
Cdd:COG4913 677 LERLDASSDDLAALEE-------------------QLEE---------LEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1786 REQAEKELETWRLKANEALRLRLraeeEAQRKSLAQEEAEKQKTEAERDakkkakAEEAALKQKENAEKELEKQRT---- 1861
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELRENLEE------RIDALRARLNRAEEELERAMRafnr 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1862 ---FAEQIAQQKLSAEQEYIRL------------KADFEHA--EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRS 1924
Cdd:COG4913 799 ewpAETADLDADLESLPEYLALldrleedglpeyEERFKELlnENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPF 878
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1925 EMDALLQMKIQAEKVSQSNTEKSkqlletealKMKQLAEEAARLRSVAEEAKKQR------QLAEDEAARQRAEAEKIL 1997
Cdd:COG4913 879 GPGRYLRLEARPRPDPEVREFRQ---------ELRAVTSGASLFDEELSEARFAAlkrlieRLRSEEEESDRRWRARVL 948
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1603-1833 |
8.68e-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: 58.42 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1603 QLEEAQVSRRKLEEEIHLIRiqlQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQE-------EAERLRKQ-VNEETQKK 1674
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMR---RLEVERKRREQEEQRRLQQEQLERAEKMREELEleqqrrfEEIRLRKQrLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1675 KNAEDELKRKSEAEKEAARQKQ----KALDELQKHKMQaEEAERrlkqAEEEKVRQikvveevaqktaatqlqamsfsek 1750
Cdd:pfam15709 404 EEEERKQRLQLQAAQERARQQQeefrRKLQELQRKKQQ-EEAER----AEAEKQRQ------------------------ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1751 tTKLEESLKKEQGTVLQLQEEA--EKLRKQEEEANKAREQAEKeletwrlkanealrlRLRAEEEAQRksLAQEEAEKQK 1828
Cdd:pfam15709 455 -KELEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKARLEAEE---------------RRQKEEEAAR--LALEEAMKQA 516
|
....*
gi 1655220517 1829 TEAER 1833
Cdd:pfam15709 517 QEQAR 521
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
197-304 |
9.01e-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: 53.85 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 267
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655220517 268 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 304
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
312-416 |
9.20e-08 |
|
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: 53.17 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 312 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGV 390
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*...
gi 1655220517 391 TRLLDPEDVdvAHPD--EKSIITYVSSL 416
Cdd:cd21313 80 PQVITPEEI--IHPDvdEHSVMTYLSQF 105
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1644-1998 |
9.40e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQ--KHKMQAEEaERRLKQAEE 1721
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEafLDRTAKRE-ERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1722 EKVRQIKVVEEVAQKTAATQLQAMsfSEKTTKLEESLKKEQ-GTVLQLQEEAEKLRKQEEEANKAREQAEKeletwrlka 1800
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKE--NNEEEENSSWEKEEKrDSRLGRYKEEETEIREKEYQENKWSTEVR--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1801 nealrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqEYIRL 1880
Cdd:pfam02029 151 --------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNG-----EEEVT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1881 KADFEHAEQQRGLLDNELQRLKNEV-----NAAEKQRRQLEDelaKVRSEMDALLQMKIQA----EKVSQSNTEKSKqLL 1951
Cdd:pfam02029 218 KLKVTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAelelEELKKKREERRK-LL 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655220517 1952 ETEALKMKQlaEEAARLRSVAEEAKKQRQlaedEAARQRAEA-EKILK 1998
Cdd:pfam02029 294 EEEEQRRKQ--EEAERKLREEEEKRRMKE----EIERRRAEAaEKRQK 335
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1287-2087 |
9.47e-08 |
|
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: 58.90 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1287 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDA--------------ELEHYRQLAGSLLERW 1352
Cdd:TIGR00606 241 KSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELkmekvfqgtdeqlnDLYHNHQRTVREKERE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1353 QAVFaqidlrQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKI-EAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1431
Cdd:TIGR00606 321 LVDC------QRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHqEHIRARDSLIQSLATRLELDGFERGPFSERQIKN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1432 CQKDAKAYIDSLKDYEFQILAyrALQDPIASPLK-----KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQR 1506
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCA--DLQSKERLKQEqadeiRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1507 RLEDDEKASEKLKEDEK-KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQL- 1584
Cdd:TIGR00606 473 ILELDQELRKAERELSKaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIr 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1585 --------ELTQL-------KNLSE------QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD------ 1637
Cdd:TIGR00606 553 kiksrhsdELTSLlgyfpnkKQLEDwlhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvc 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1638 -------ELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1710
Cdd:TIGR00606 633 gsqdeesDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1711 EAERRLKQAEEE-----------------KVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA- 1772
Cdd:TIGR00606 713 STESELKKKEKRrdemlglapgrqsiidlKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVt 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1773 --EKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1850
Cdd:TIGR00606 793 imERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1851 NAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDA 1928
Cdd:TIGR00606 873 KLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1929 LLQMKIQAEKVSQSNTEKSKQLLETEALKMK-QLAEEAARLRSVAEEAKKQRQLAEDEAARqraeaEKILKEKLaainea 2007
Cdd:TIGR00606 953 IHGYMKDIENKIQDGKDDYLKQKETELNTVNaQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----ERWLQDNL------ 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2008 TRLKTEAEValkaKEAENERlkRQAEDEAYQRKLLEDQAAQHKhdIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEE 2087
Cdd:TIGR00606 1022 TLRKRENEL----KEVEEEL--KQHLKEMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2359-2578 |
9.77e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2359 DEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSV 2438
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2439 EAEETARQRKTAEA--------ELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRL 2510
Cdd:COG3883 94 ALYRSGGSVSYLDVllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2511 DK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2578
Cdd:COG3883 174 EAqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1848-2048 |
1.15e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1848 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAK------ 1921
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1922 ----VRSEMDALLQMKIQAEKVSQSntekskQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 1997
Cdd:COG3883 97 rsggSVSYLDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1998 KEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQ 2048
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2479-2730 |
1.17e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2479 KAEAEELQKQKNQAqEKAKKLLEDKQeiqQRLDKEtqgfqkslEAERKRQLEISAEAeklklRVKELSSAQAKAEEEATR 2558
Cdd:PRK05035 435 KAEIRAIEQEKKKA-EEAKARFEARQ---ARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2559 FKKQADEAKVRLQETEKQTTETV-------VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA--- 2628
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIaarearkAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdp 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2629 --SAQQEQMEQQKAMLQQTFLTEKElllKRERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2706
Cdd:PRK05035 578 kkAAVAAAIARAKAKKAAQQAASAE---PEEQVAEVDPKKAA--VAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260
....*....|....*....|....*
gi 1655220517 2707 VK-KQKEAEAEMKNKQKEMEALEKK 2730
Cdd:PRK05035 653 ARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1477-1923 |
1.24e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1477 IQEYVTLRTRYSELSTLTSQYIKfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAksvAKAELEAQE 1556
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA---LEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1557 LKL-KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTA 1635
Cdd:COG4717 146 ERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1636 DDELQKLRDQAAEAEKVRKAAQEEAE-RLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1714
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1715 RLKQAEEEkvrqikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQgtVLQLQEEAEKLRKQEEEANKAREQAEKE-- 1792
Cdd:COG4717 306 ELQALPAL--------EELEEEELEELLAALGLPPDLSPEELLELLDR--IEELQELLREAEELEEELQLEELEQEIAal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1793 LETWRLKANEALRLRLRAEEEAQrkslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLS 1872
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQ-----ELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1873 AEQEYIRLKADFEHAEQqrgllDNELQRLKNEVNAAEKQRRQLEDELAKVR 1923
Cdd:COG4717 451 LREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALK 496
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2311-2754 |
1.51e-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: 57.83 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEADAEMAK-HKKEAEQALKQKSQVEkELGLVKLQLDETDKQkalmdeeLQRVKAQVNDAVKQKAQVENELSKVKMQ 2389
Cdd:pfam05557 48 DRNQELQKRIRLlEKREAEAEEALREQAE-LNRLKKKYLEALNKK-------LNEKESQLADAREVISCLKNELSELRRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2390 -MDELLKLKvRIEEENLRLMQKNKDNTQKllAEEAEKMKSLAEEAARLSVEAEEtarQRKTAEAELA--EQRALAEKMLK 2466
Cdd:pfam05557 120 iQRAELELQ-STNSELEELQERLDLLKAK--ASEAEQLRQNLEKQQSSLAEAEQ---RIKELEFEIQsqEQDSEIVKNSK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2467 EKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEKLKLRVK--E 2544
Cdd:pfam05557 194 SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLERE----EKYREEAATLELEKEKLEQELQSWVKlaQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 LSSAQAKAEEEATRFKKQADEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnKS 2624
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQREIVLKE-ENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQ-RR 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2625 KETASAQQEQMeqqKAMLQQ--TFLTEKE---LLLKRERDVEDEKKKLQKHLEDEvnkakalkdEQQRQQKLMDEEKKKL 2699
Cdd:pfam05557 348 VLLLTKERDGY---RAILESydKELTMSNyspQLLERIEEAEDMTQKMQAHNEEM---------EAQLSVAEEELGGYKQ 415
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2700 QAIMDEA---VKKQKEAEAEMKNKQKEMEALekkRLEQEKLLAdENKKLREKLESLEV 2754
Cdd:pfam05557 416 QAQTLERelqALRQQESLADPSYSKEEVDSL---RRKLETLEL-ERQRLREQKNELEM 469
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2591-2739 |
1.72e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.48 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2591 QSTREADDLKK-AIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQKamlqqtflteKELLLKRERDVEDEKKKLQK 2669
Cdd:PRK12704 46 EAKKEAEAIKKeALLEAKEEIHKLRNEF-EKELRERRNELQKLEKRLLQK----------EENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2670 HLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIM----DEA-------VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2738
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERISgltaEEAkeillekVEEEARHEAAVLIKEIEEEAKEEADKKAKEIL 194
|
.
gi 1655220517 2739 A 2739
Cdd:PRK12704 195 A 195
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1673-2385 |
1.72e-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: 57.72 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1673 KKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEevaQKTAATQLQAMSFSEKTT 1752
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN-------KIKILE---QQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1753 KLEESLKKeqgTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLrlraEEEAQRKSLAQEEAEKQKTEAE 1832
Cdd:TIGR04523 100 KLNSDLSK---INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK----EKELEKLNNKYNDLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1833 RDAKKKAKAEEaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN-------ELQRLKNEV 1905
Cdd:TIGR04523 173 NELNLLEKEKL----NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDniekkqqEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1906 NAAEKQRRQLEDELAKVRsemDALLQMKIQAEKVSQSNTEKSKQL--LETEALKMKQLAEEAArLRSVAEEAKKQRqlae 1983
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLnqLKSEISDLNNQKEQDW-NKELKSELKNQE---- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1984 deaaRQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQlqss 2063
Cdd:TIGR04523 321 ----KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2064 sVSELDRQKNIVEETLRQKkvvEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEER 2143
Cdd:TIGR04523 393 -INDLESKIQNQEKLNQQK---DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2144 KRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANK----LKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVL 2219
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEkvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2220 SKNKEdlLSQEKLRDEfenakklaqaaetakekaekeaalLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEA 2299
Cdd:TIGR04523 549 KDDFE--LKKENLEKE------------------------IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2300 AKRAAAEAAALKQKQEADAEMAKHKKEAEQALK---QKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQK 2376
Cdd:TIGR04523 603 KEIEEKEKKISSLEKELEKAKKENEKLSSIIKNiksKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELM 682
|
....*....
gi 1655220517 2377 AQVENELSK 2385
Cdd:TIGR04523 683 KDWLKELSL 691
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2164-2778 |
2.20e-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: 57.75 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEqkaqdvLSKNKEDLLsqeklrDEFENAKKLA 2243
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSRE------IVKSYENEL------DPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2244 QAAETAKEKAEKEAALLRQKAEEAEKLKKaaEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEaaalKQKQEADAEMAKH 2323
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNS--ELELKMEKVFQGTDEQLNDLYHNHQRTVREKE----RELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2324 KKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVN-DAVKQKAQVENELSKVKMQMDELLKLKVRIEE 2402
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2403 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIqeatklKAEA 2482
Cdd:TIGR00606 412 QLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR------KAER 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2483 EELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfqkSLEAERKRQLEISAEAEKLKlRVKELSSAQAKAEEEATRFKKQ 2562
Cdd:TIGR00606 486 ELSKAEKNSLTETLKKEVKSLQNEKADLDR-------KLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2563 ADEAKVRLQE--TEKQTTETVVQKLETQRLQSTREADDLKKAIAELE-------KEREKLKRDAQELQNKSKETASAQQE 2633
Cdd:TIGR00606 558 HSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEqnknhinNELESKEEQLSSYEDKLFDVCGSQDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2634 QMEQQKAMLQQTFLTEKELLLKRERDVEDEkkkLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEA 2713
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGATAVYSQ---FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2714 EAEMKNKQKEME---ALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKV-PEEQL 2778
Cdd:TIGR00606 715 ESELKKKEKRRDemlGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImPEEES 783
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
317-414 |
2.22e-07 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 52.48 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 317 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALL-DMSQVYRQSNQENLEQAFSVAERELGVTRLLD 395
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1655220517 396 PEDVDVAHPDEKSIITYVS 414
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1468-1778 |
2.44e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1468 KMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLE----DDEKASEKLKEDEKKrMAEIQAQLETQKQLAEGH 1543
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEqleqEEEKLKERLEELEED-LSSLEQEIENVKSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1544 AKSVAKAELEAQELKLKMKE----------DASQRQGLAVDAEKQKQNIQL--------ELTQLKNLSEQEIRSKNQQLE 1605
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLreieqklnRLTLEKEYLEKEIQELQEQRI 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1606 EAQVSRRKLEEEIHLIRIQ---LQTTIKQKSTADDELQK-----------LRDQAAEAEKVRKAAQEEAERLRKQVNEET 1671
Cdd:TIGR02169 844 DLKEQIKSIEKEIENLNGKkeeLEEELEELEAALRDLESrlgdlkkerdeLEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1672 QKKKNAEDELKRKSEAEKEAARQKQKALDeLQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAatqlqamSFSEKT 1751
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD-------ELKEKR 995
|
330 340
....*....|....*....|....*..
gi 1655220517 1752 TKLEEslkkEQGTVLQLQEEAEKLRKQ 1778
Cdd:TIGR02169 996 AKLEE----ERKAILERIEEYEKKKRE 1018
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1882-2738 |
2.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1882 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkIQAEKVSQSNTEKSKQLLetealkmkQ 1960
Cdd:PRK04863 272 ADYmRHANERRVHLEEALE-LRRELYTSRRQLAAEQYRLVEMARELAEL----NEAESDLEQDYQAASDHL--------N 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1961 LAEEAARLRSvaeeaKKQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDeaYQRK 2040
Cdd:PRK04863 339 LVQTALRQQE-----KIERYQADLEELEERLE------EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD--YQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2041 LLEDQ--AAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGI 2116
Cdd:PRK04863 406 LDVQQtrAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2117 ADETQKSKAKAEEEAEKLKKLAAEEERKRREaeekvkkiaaaeeeaarQRKAAQDEVERLKQKAAEANKLKDKAEKELEK 2196
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQ-----------------QLRMRLSELEQRLRQQQRAERLLAEFCKRLGK 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2197 QVILAKEAAQKSTAAEQKAQDvLSKNKEDLLSQ-EKLRDEFENAKKLAQAaetakekaekeaalLRQKAEEAEKLKKAAE 2275
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLES-LSESVSEARERrMALRQQLEQLQARIQR--------------LAARAPAWLAAQDALA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2276 DEAAKQAKAQKDAERLRkeaeaeaakraaaeaaalkqkqEADAEMAKHKKEAEQalkQKSQVEKELGLVKLQLDETDKQK 2355
Cdd:PRK04863 614 RLREQSGEEFEDSQDVT----------------------EYMQQLLERERELTV---ERDELAARKQALDEEIERLSQPG 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2356 ALMDEELQRVKAQVN--------------DAV--------KQKAQVENELSKVKMQM----------------------- 2390
Cdd:PRK04863 669 GSEDPRLNALAERFGgvllseiyddvsleDAPyfsalygpARHAIVVPDLSDAAEQLagledcpedlyliegdpdsfdds 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2391 ----DELLK-LKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQRKTAEAELAE 2456
Cdd:PRK04863 749 vfsvEELEKaVVVKIADRQWRysrfpevplFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQRLHQAFSRFIGS 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2457 QRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR---LDKETqgFQKSLEAERKrQ 2528
Cdd:PRK04863 826 HLAVAfeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRlnlLADET--LADRVEEIRE-Q 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2529 LEISAEAEK--------LKLRVKELSSAQAKAEEEATrFKKQADEAKVRLQETEKQT---TEtVVQKLEtqRLQSTREAD 2597
Cdd:PRK04863 903 LDEAEEAKRfvqqhgnaLAQLEPIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAfalTE-VVQRRA--HFSYEDAAE 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2598 DLKKAIAELEKEREKLKRdAQELQNKSKETASAQQEQMEQQKAMLQQtfltekellLKRERDV-EDEKKKLQKHLE---- 2672
Cdd:PRK04863 979 MLAKNSDLNEKLRQRLEQ-AEQERTRAREQLRQAQAQLAQYNQVLAS---------LKSSYDAkRQMLQELKQELQdlgv 1048
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2673 --DEVNKAKALKDEQQRQQKLMDEEKKKlqaimDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2738
Cdd:PRK04863 1049 paDSGAEERARARRDELHARLSANRSRR-----NQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2317-2542 |
2.65e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2317 DAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELL 2394
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2395 klkvrieeenlrlmqkNKDNTQKLLAEEAEKMKSLAEEAARLSveaeETARQRKTAEAELAEQRALAEKMLKEKMQAIQ- 2473
Cdd:COG3206 261 ----------------QSPVIQQLRAQLAELEAELAELSARYT----PNHPDVIALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2474 EATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIqQRLDKETQGFQKSLEA--ERKRQLEISAEAEKLKLRV 2542
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAEL-RRLEREVEVARELYESllQRLEEARLAEALTVGNVRV 390
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2170-2668 |
2.75e-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: 57.54 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2170 QDEVERLKQKAAEANKLK-DKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDLLSQEK--LRDEFENAKKLAQAA 2246
Cdd:pfam12128 374 TAKYNRRRSKIKEQNNRDiAGIKDKLAKI----REARDRQLAVAEDDLQALESELREQLEAGKleFNEEEYRLKSRLGEL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2247 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAK--AQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHK 2324
Cdd:pfam12128 450 KLRLNQATATPELLLQLENFDERIERAREEQEAANAEveRLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2325 KEAEQAL-----KQKSQVEKELGLV--KLQLDETDKQKALMDE-------------ELQRVkaQVNDAVKQKAQVENELS 2384
Cdd:pfam12128 530 FPQAGTLlhflrKEAPDWEQSIGKVisPELLHRTDLDPEVWDGsvggelnlygvklDLKRI--DVPEWAASEEELRERLD 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2385 KVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEetARQRKTAEAELAEQRALAEKM 2464
Cdd:pfam12128 608 KAEEALQSAREKQAAAEEQ-LVQANGELEKASREETFARTALKNARLDLRRLFDEKQ--SEKDKKNKALAERKDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2465 LKEKMQAIQEATKLKAEAEELQKQKNQA----QEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKrQLEISAEAEKLKL 2540
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREArtekQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK-ALETWYKRDLASL 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2541 RVKELSSAQAKAE--------EEATRFKKQADEAKVRLQET-------EKQTTETVVQKLETQRLQSTREADDLKKAIAE 2605
Cdd:pfam12128 764 GVDPDVIAKLKREirtlerkiERIAVRRQEVLRYFDWYQETwlqrrprLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2606 LEKEREKLkRDAQELQNKSKETASAQQEQM---------EQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQ 2668
Cdd:pfam12128 844 LEMERKAS-EKQQVRLSENLRGLRCEMSKLatlkedansEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1129-1914 |
3.04e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1129 YNTMVSSAEQGEQDESVCKTYLTKIKDLRLKLdgceSRTVTRLRQPVDKEPLKACAQKTAEQMKVQSELEGLKKDLNSIt 1208
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISEL----EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1209 EKTEEILASPQQSSSAPM--LRSELDVTLKKMDHVYG-LSSVYLDKLKTIDIVirntKDAEDTVKSYESRLRDVSKVPAE 1285
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLakLEAEIDKLLAEIEELEReIEEERKRRDKLTEEY----AELKEELEDLRAELEEVDKEFAE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1286 EK-EVEAHRSQLKAMRAEAEADQATFDRLQDELK-----------AATSVSDKMTRLHSERD---AELEHYRQLAGSLLE 1350
Cdd:TIGR02169 383 TRdELKDYREKLEKLKREINELKRELDRLQEELQrlseeladlnaAIAGIEAKINELEEEKEdkaLEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1351 RWQAVFAQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLTQEKKLLEEIEKNKDQIE 1430
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1431 NC------------QKDAKAYIDSLKDYE---FQILAYRALQDPiASPLKKPKMESASDNIIqEYVTLRTRYSELstlts 1495
Cdd:TIGR02169 543 VAagnrlnnvvvedDAVAKEAIELLKRRKagrATFLPLNKMRDE-RRDLSILSEDGVIGFAV-DLVEFDPKYEPA----- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1496 qyIKFILETQRRLEDDEKASEKLkedEKKRMAEIQAQL------ETQKQLAEGHAKSVAKAEL-EAQELKLKMKEDASQR 1568
Cdd:TIGR02169 616 --FKYVFGDTLVVEDIEAARRLM---GKYRMVTLEGELfeksgaMTGGSRAPRGGILFSRSEPaELQRLRERLEGLKREL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1569 QGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAE 1648
Cdd:TIGR02169 691 SSLQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1649 AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA-RQKQKALDELQKHKMQAEEAerrlKQAEEEKVRQI 1727
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlREIEQKLNRLTLEKEYLEKE----IQELQEQRIDL 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KV-VEEVAQKTAATQLqamsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrl 1806
Cdd:TIGR02169 846 KEqIKSIEKEIENLNG-------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK--- 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1807 RLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRtfaeqIAQQKLSAEQEYIRLKADFEH 1886
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA-----LEPVNMLAIQEYEEVLKRLDE 990
|
810 820
....*....|....*....|....*...
gi 1655220517 1887 AEQQRGLLDNELQRLKNEVNAAEKQRRQ 1914
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1511-1720 |
3.21e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1511 DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHA-KSVAKAELEAQELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQL 1589
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQK-KQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1590 KNLSEQeirsknQQLEEAQvsrRKLEEEihliriqlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1669
Cdd:PRK09510 148 KAEAEA------KRAAAAA---KKAAAE-------------AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1670 ETQKKKNAEDELKRKSEAEK--EAARQKQKALDELQKHKMQAEEAERRLKQAE 1720
Cdd:PRK09510 206 EAKKKAAAEAKKKAAAEAKAaaAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2361-2767 |
3.25e-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: 56.67 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2361 ELQRVKAQVndavkqkAQVENElskvKMQMDellklkvrIEEENLRLMQKNKDNTQKL-LAEEAEKMKSLAEEAARLSvE 2439
Cdd:pfam05557 3 ELIESKARL-------SQLQNE----KKQME--------LEHKRARIELEKKASALKRqLDRESDRNQELQKRIRLLE-K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2440 AEETARQRKTAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK 2519
Cdd:pfam05557 63 REAEAEEALREQAELNRLK---KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2520 SLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEatrfkkqadEAKVRLQETEKQTTETVVQKLETqrlqstreaddl 2599
Cdd:pfam05557 140 RLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKEL---------EFEIQSQEQDSEIVKNSKSELAR------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2600 kkaIAELEKEREKLKRDAQELqNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkrerDVEDEKKKLQKHLEDEVNKAK 2679
Cdd:pfam05557 199 ---IPELEKELERLREHNKHL-NENIENKLLLKEEVEDLKRKLEREEKYREEAA-----TLELEKEKLEQELQSWVKLAQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2680 ALKDEQQRQQKLMDEEKKKLQaimDEAVKKQK--EAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSK 2757
Cdd:pfam05557 270 DTGLNLRSPEDLSRRIEQLQQ---REIVLKEEnsSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
410
....*....|
gi 1655220517 2758 QAASKTKEIE 2767
Cdd:pfam05557 347 RVLLLTKERD 356
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2498-2769 |
3.45e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRLDKETQGFQKSLEAERKRQ---LEISAEA---EKLKLRVKELSSA---------QAKAEEEATRFKKQ 2562
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPVKGsnvIEISYTSpdpELAAAVANALAEAyleqnlelrREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2563 ADEAKVRLQETEKQttetvVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2640
Cdd:COG3206 184 LPELRKELEEAEAA-----LEEFRQKNglVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2641 MLQQTFLTEkelLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeavkkqkEAEAEMKNK 2720
Cdd:COG3206 259 LLQSPVIQQ---LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA----------SLEAELEAL 325
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2721 QKEMEALEKKRLEQEKLLADENKKLRE------KLESLEVTSKQAASKTKEIEVQ 2769
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAElrrlerEVEVARELYESLLQRLEEARLA 380
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2416-2640 |
3.61e-07 |
|
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: 55.62 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEAAR----LSVEAEETARQRKTAEAelAEQRALAEkmLKEKMQAIQEATKLKAEAEELQKQKNQ 2491
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKkeqeRQKKLEQQAEEAEKQRA--AEQARQKE--LEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2492 AQEKAKKLLED--KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEAtrfKKQADEAKVR 2569
Cdd:TIGR02794 121 AEEAKAKQAAEakAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA---KAKAEEAKAK 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2570 LQETEKQTTETVVQKletqrlqstreADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2640
Cdd:TIGR02794 198 AEAAKAKAAAEAAAK-----------AEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAA 257
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2479-2721 |
4.05e-07 |
|
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: 55.62 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2479 KAEAEELQKQKNQAQEKAKKLLEDKQEIQQRldKETQGFQKSLEAERKRQLEISAEAEKLKlrvkelsSAQAKAEEEATR 2558
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEKAA-------KQAEQAAKQAEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2559 FKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAqELQNKSKETASAQQEQMEQQ 2638
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA-EAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2639 KAMLQQTFLTEKELLLKRERD------VEDEKKKLQKHLEDEVNKAKALKDEQQRQ--QKLMDEEKKKLQAIMDEAVKKQ 2710
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEaaaaaaAEAERKADEAELGDIFGLASGSNAEKQGGarGAAAGSEVDKYAAIIQQAIQQN 275
|
250
....*....|.
gi 1655220517 2711 KEAEAEMKNKQ 2721
Cdd:TIGR02794 276 LYDDPSFRGKT 286
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1756-2201 |
4.06e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1756 ESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANealRLRLRAEEEAQRKSLAQEEAEKQKTEAERDA 1835
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1836 KKKAKAeeaalkQKENAEKEL-EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ 1914
Cdd:COG4717 158 LRELEE------ELEELEAELaELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1915 LEDE--------------------------------LAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLA 1962
Cdd:COG4717 232 LENEleaaaleerlkearlllliaaallallglggsLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1963 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEA--YQRK 2040
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEelRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2041 LLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK-KVVEEEIHIIRINFERASKEKSDLEVELKKLKGiade 2119
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQLEE---- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2120 tqkskakaeeeaeklkklaaeeerkrreaeekvkkiaaaeeeaarqrkaaQDEVERLKQKAAEA-NKLKDKAEKELEKQV 2198
Cdd:COG4717 468 --------------------------------------------------DGELAELLQELEELkAELRELAEEWAALKL 497
|
...
gi 1655220517 2199 ILA 2201
Cdd:COG4717 498 ALE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2392-2753 |
4.24e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2392 ELLKLKVRIEEENLRLMqknkdNTQKLLAEEAEKMKSLAE--EAAR----LSVEAEETARQRKTAEAELAEqralAEKML 2465
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQdyQAASdhlnLVQTALRQQEKIERYQADLEE----LEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2466 KEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDkqeIQQRLD-KETQG--FQKSLEA-ERKRQL--EISAEAEKLK 2539
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD---YQQALDvQQTRAiqYQQAVQAlERAKQLcgLPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2540 LRVKELssaQAKaEEEATRFKKQAdEAKVRLQETEKQTTETVVQKLetQRLQSTREADDLKKAIAELEKEREKLKRDAQE 2619
Cdd:PRK04863 442 DWLEEF---QAK-EQEATEELLSL-EQKLSVAQAAHSQFEQAYQLV--RKIAGEVSRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2620 LQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVED---EKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEE 2695
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQlqeELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2696 KKKLQAI------MDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLE 2753
Cdd:PRK04863 595 IQRLAARapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1887-2073 |
4.43e-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: 54.16 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1887 AEQQRGLLDneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLETEalkMKQLAEEAA 1966
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1967 RLRSVAEEAKKQRQLA-----EDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQrkl 2041
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE--- 153
|
170 180 190
....*....|....*....|....*....|..
gi 1655220517 2042 LEDQAAQHKHDIQEKITQLQSSSVSELDRQKN 2073
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1555-2112 |
4.79e-07 |
|
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: 56.19 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1555 QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQ-EIRSKNQQLEEAQVsrrkleeeihliriqlqttiKQks 1633
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEAQA--------------------KQ-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1634 taDDELQKLRDQAAE---AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAE 1710
Cdd:pfam05701 99 --DSELAKLRVEEMEqgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1711 EAErrlKQAEEEKVRQIKVVEEVAQKTAAtQLQAmsfSEKttKLEESLKKEQGTvLQLQEEaekLRKQEEEANKAREQ-- 1788
Cdd:pfam05701 177 EIE---KTVEELTIELIATKESLESAHAA-HLEA---EEH--RIGAALAREQDK-LNWEKE---LKQAEEELQRLNQQll 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1789 AEKELETwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAeeaalkqkENAEKELEKQRTFAEqiaq 1868
Cdd:pfam05701 244 SAKDLKS-KLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL--------ASAKKELEEVKANIE---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1869 qKLSAEQEYIRLKADFEHAEqqrglLDNE---LQRLKNEVNAAEKQRRQLEDELAKVRSEMdALLQMKiqaekvsqsnTE 1945
Cdd:pfam05701 311 -KAKDEVNCLRVAAASLRSE-----LEKEkaeLASLRQREGMASIAVSSLEAELNRTKSEI-ALVQAK----------EK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1946 KSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA-- 2023
Cdd:pfam05701 374 EAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlq 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2024 ENERLKRQAEDEAYQRKLL----------------EDQAaqhKHDIQEKITQLQSSSVSELdRQKNIVEETLRQKKVVEE 2087
Cdd:pfam05701 454 ESESSAESTNQEDSPRGVTlsleeyyelskraheaEELA---NKRVAEAVSQIEEAKESEL-RSLEKLEEVNREMEERKE 529
|
570 580
....*....|....*....|....*
gi 1655220517 2088 EIHIIRINFERASKEKSDLEVELKK 2112
Cdd:pfam05701 530 ALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1488-1762 |
5.35e-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: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1488 SELSTLTSQYIKFILE---TQRRLEDDEKA---SEKLKEDEKKRMAEI---QAQLETQKQLA---EGHAKSVA-KAELEA 1554
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLESTDQNAletNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1555 --QELKlKMKEDASQRQGLAVDAEKQKQNIQLELTQ--LKNLSEQEIRSKnqqleeaQVSRRKLEEeihliriqlqttIK 1630
Cdd:NF012221 1618 vtKELT-TLAQGLDALDSQATYAGESGDQWRNPFAGglLDRVQEQLDDAK-------KISGKQLAD------------AK 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1631 QKSTadDELQKLRDQAAEAEkvrkAAQEEAERLRKQVNEETQKKKNAEDelKRKseaeKEAARQKQKALDELQKHKMQAE 1710
Cdd:NF012221 1678 QRHV--DNQQKVKDAVAKSE----AGVAQGEQNQANAEQDIDDAKADAE--KRK----DDALAKQNEAQQAESDANAAAN 1745
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 1711 EAERRLKQaeeekvrqikvvEEVAQKTAATQLQAmsfSEKTTKLEESLKKEQ 1762
Cdd:NF012221 1746 DAQSRGEQ------------DASAAENKANQAQA---DAKGAKQDESDKPNR 1782
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1636-1794 |
5.43e-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: 54.16 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1636 DDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKsEAEKEAARQKQKAL----------DELQKH 1705
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIEEVEARIKKYeeqlgnvrnnKEYEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1706 KMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamsfsEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKA 1785
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELE-------AELAELEAELEEKKA---ELDEELAELEAELEELEAE 164
|
....*....
gi 1655220517 1786 REQAEKELE 1794
Cdd:COG1579 165 REELAAKIP 173
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4301-4329 |
6.47e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 6.47e-07
10 20
....*....|....*....|....*....
gi 1655220517 4301 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4329
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1502-1817 |
6.68e-07 |
|
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: 54.92 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQN 1581
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1582 IQLELTQLKNLSEQEIRSKNQQleeaqvsrrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAE 1661
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELE---------KEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1662 RLRKQVNEETQKKKNAEDELKRKS-EAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1740
Cdd:pfam13868 196 AQDEKAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE 275
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1741 QLQamsfsekttkleeslKKEQGTVLQLQEEAEKLRKQEEEANKAREQA-EKELETWRLKANEALRLRLRAEEEAQRK 1817
Cdd:pfam13868 276 IEQ---------------EEAEKRRMKRLEHRRELEKQIEEREEQRAAErEEELEEGERLREEEAERRERIEEERQKK 338
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1612-1932 |
7.76e-07 |
|
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: 54.54 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1612 RKLEEEIHLIRIQL----QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEA 1687
Cdd:pfam13868 9 RELNSKLLAAKCNKerdaQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1688 EKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK--VVEEVAQKTAATQLQAMSFSEKTTKLEESLK-KEQGT 1764
Cdd:pfam13868 89 RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLReeIDEFNEEQAEWKELEKEEEREEDERILEYLKeKAERE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1765 VLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEA 1844
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKA--ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1845 ALKQKENAEKELEKQ------RTFAEQIAQQKLSAEQEYIRLKAdfEHAEQQRGLLDNELQRL---KNEVNAAEKQRRQL 1915
Cdd:pfam13868 247 LKERRLAEEAEREEEefermlRKQAEDEEIEQEEAEKRRMKRLE--HRRELEKQIEEREEQRAaerEEELEEGERLREEE 324
|
330
....*....|....*..
gi 1655220517 1916 EDELAKVRSEMDALLQM 1932
Cdd:pfam13868 325 AERRERIEEERQKKLKE 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2406-2599 |
8.08e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2406 RLMQKNKDNT------QKLLAEEA-EKMKSLAEEAARL-SVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EAT 2476
Cdd:PRK09510 66 RQQQQQKSAKraeeqrKKKEQQQAeELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2477 KLKAEAEE--LQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgfQKSLEAERKRQLEISAEAEKLKL-RVKELSSAQAKAE 2553
Cdd:PRK09510 146 KAKAEAEAkrAAAAAKKAAAEAKKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEaKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220517 2554 EEATRFKKQADEAKVRLQETEKQTTEtvvqKLETQRLQSTREADDL 2599
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKA----AEKAAAAKAAAEVDDL 262
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1576-1987 |
8.20e-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: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1655
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEDELKRKSEaekeaarQKQKALDELQKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQ 1735
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQ-------RVLERETELERMKERAKKAGAQRKEEEAER-------KQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1736 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRlkaneALRLRLRAEE--- 1812
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR-----SLQERLNASErkv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1813 EAQRKSLAQEEAEKQKTEAErdakkkakaeeAALKQKENAEKELE-KQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQR 1891
Cdd:pfam07888 254 EGLGEELSSMAAQRDRTQAE-----------LHQARLQAAQLTLQlADASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1892 glLDNELQRLKNEVNAAEKQRRQLEDELAKVR-------SEMDALLQMKIQAEKVSQSntEKSKQLLETEALkMKQLAEE 1964
Cdd:pfam07888 323 --LSAELQRLEERLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQK--EKEQLQAEKQEL-LEYIRQL 397
|
410 420
....*....|....*....|...
gi 1655220517 1965 AARLRSVAEEAKKQRQLAEDEAA 1987
Cdd:pfam07888 398 EQRLETVADAKWSEAALTSTERP 420
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1279-1959 |
8.27e-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: 55.61 E-value: 8.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1279 VSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSvsDKMTRLHSERDAELEHYRQLAGSLL---ERWQAV 1355
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSA--ELNQLLRTLDDQWKEKRDELNGELSaadAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1356 FAQID-LRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIENCQK 1434
Cdd:pfam12128 321 RSELEaLEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA--LTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1435 DAKAYIDSLKDYEFQILAYRALQDPIasplkKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIkfiletqrrLEDDEKA 1514
Cdd:pfam12128 399 LAKIREARDRQLAVAEDDLQALESEL-----REQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT---------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1515 SEKLKEDEKKRMAEIQAQlETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAvDAEKQKQNIQLELTQLKNLSE 1594
Cdd:pfam12128 465 QLENFDERIERAREEQEA-ANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA-LDELELQLFPQAGTLLHFLRK 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1595 QEI---RSKNQQLEEAQVSRRKLEEEI----------------HLIRIQlqttIKQKSTADDELQKLRDQAAEAekvRKA 1655
Cdd:pfam12128 543 EAPdweQSIGKVISPELLHRTDLDPEVwdgsvggelnlygvklDLKRID----VPEWAASEEELRERLDKAEEA---LQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIkvveEVAQ 1735
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSL----EAQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1736 KTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAE---KELETWR------LKANEALRL 1806
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKaelKALETWYkrdlasLGVDPDVIA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1807 RLRAEEEAQRKSLAQEEAEKQKTEAERDakkkaKAEEAALKQKENAEKELEKQRTFAEQIaQQKLSAEQEYIRLKadfeh 1886
Cdd:pfam12128 772 KLKREIRTLERKIERIAVRRQEVLRYFD-----WYQETWLQRRPRLATQLSNIERAISEL-QQQLARLIADTKLR----- 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1887 aeqqrglldneLQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEkVSQSNTEKSKQLLETEALKMK 1959
Cdd:pfam12128 841 -----------RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDAN-SEQAQGSIGERLAQLEDLKLK 901
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1440-1744 |
8.56e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1440 IDSLKDYEFQILAYRALQDPIASPLKKPKMESASD-NIIQeyVTLRTRYSELS-----TLTSQYIKFILEtqRRLEDDEK 1513
Cdd:COG3206 100 VDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGsNVIE--ISYTSPDPELAaavanALAEAYLEQNLE--LRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1514 ASEKLKEdekkRMAEIQAQLEtqkqlaeghaksvaKAELEAQELKlkmkedasQRQGLaVDAEKQKQNIQLELTQLknls 1593
Cdd:COG3206 176 ALEFLEE----QLPELRKELE--------------EAEAALEEFR--------QKNGL-VDLSEEAKLLLQQLSEL---- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1594 eqeirskNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST--ADDELQKLRDQAAEAEKVRKAAQE-------EAERLR 1664
Cdd:COG3206 225 -------ESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALR 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1665 KQVNEETQKKKNAEDELKRKSEAEKEAARQK----QKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAT 1740
Cdd:COG3206 298 AQIAALRAQLQQEAQRILASLEAELEALQAReaslQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
....
gi 1655220517 1741 QLQA 1744
Cdd:COG3206 378 RLAE 381
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1694-1911 |
8.66e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1694 QKQKALDELQKHKMQAEEAERRLKQ---AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1770
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQkqaAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1771 EAEKLRkQEEEANKAREQAEKELETWRLKANEAlRLRLRAEEEAQRKslAQEEAEKQKTEAERDAKKKAKAEEAALKQKE 1850
Cdd:PRK09510 150 EAEAKR-AAAAAKKAAAEAKKKAEAEAAKKAAA-EAKKKAEAEAAAK--AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1851 NAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRGLLDNELQRLKNEVNAAEKQ 1911
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAA----------AAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2372-2576 |
8.91e-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: 54.77 E-value: 8.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2372 AVKQKAQVENELSKVKMQMDELLKLKVRIEEEnLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAE 2451
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2452 AELAEQRALAEKMLKE--KM----------------QAIQEATKLKAEAEELQKQKNQAQEKAKKLledkQEIQQRLDKE 2513
Cdd:COG4942 97 AELEAQKEELAELLRAlyRLgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAEL----AALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2514 TQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2576
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1967-2778 |
9.03e-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: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1967 RLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVAlKAKEAENERLK-RQAEDEAYQRKLledq 2045
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKnRLKEIEHNLSKI---- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2046 aaqhkHDIQEKITQLQSSsvsELDRQKNIVEETLRQKKV---VEEEIHIIRINFERASKEKSDLEVEL-KKLKGIADETQ 2121
Cdd:TIGR00606 265 -----MKLDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKERELVDCqRELEKLNKERR 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2122 kskakaeeeAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILA 2201
Cdd:TIGR00606 337 ---------LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2202 KEAAQkstaaeqkaqdVLSKNKEDLLSQEKLRDEFENAKK-LAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAK 2280
Cdd:TIGR00606 408 KTAAQ-----------LCADLQSKERLKQEQADEIRDEKKgLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2281 QAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQeadAEMAKHKKEAEQALKQKSQVEKELGlvklQLDETDKQKALMDE 2360
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEK---ADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2361 ELQRVKAQVNDAV----------KQKAQVENELSKVKMQMDELLKlKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLA 2430
Cdd:TIGR00606 550 QIRKIKSRHSDELtsllgyfpnkKQLEDWLHSKSKEINQTRDRLA-KLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2431 EEAArlSVEAEETARQRKTAEAELA-EQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQR 2509
Cdd:TIGR00606 629 FDVC--GSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2510 LDKETQGFQKSLEAERKRQLEISAEAE----KLKLRVKELSSAQAKAEEEATRFKkqadEAKVRLQETEKQTtETVVQKL 2585
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEMLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQ----RLKNDIEEQETLL-GTIMPEE 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2586 ETQRLQSTrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkreRDVEDEKK 2665
Cdd:TIGR00606 782 ESAKVCLT-DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELN----RKLIQDQQ 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2666 KLQKHLEDEVNKAKALK-----DEQQRQQklMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2740
Cdd:TIGR00606 857 EQIQHLKSKTNELKSEKlqigtNLQRRQQ--FEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
810 820 830
....*....|....*....|....*....|....*...
gi 1655220517 2741 ENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2778
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1848-2047 |
9.21e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1848 QKENAEKELEKQRTFAEQIAQQKLSAEQEyirlkadfehAEQQRglldneLQRLKNEVNAAEKQRRQLEDELAKvrsemd 1927
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQ------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1928 ALLQMKiQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARlrsVAEEAKKQrqlAEDEAARQRAEAEKILKEKLAAINEA 2007
Cdd:PRK09510 127 AALKQK-QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAKAA 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220517 2008 TRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAA 2047
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1593-1792 |
1.02e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1593 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE--- 1669
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1670 ETQKKKNAEDELK------------RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKT 1737
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 1738 AATQLQAmsfsektTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKE 1792
Cdd:COG3883 174 EAQQAEQ-------EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2472-2685 |
1.05e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2472 IQEATKLKAEAEelQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKElssAQAK 2551
Cdd:PRK09510 67 QQQQQKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERL--------KQLEKERLAAQEQKKQAEEAAKQAAL---KQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2552 AEEEAtrfKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQ 2631
Cdd:PRK09510 134 AEEAA---AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2632 QEQMEQQKAmlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQ 2685
Cdd:PRK09510 211 AAAEAKKKA--------AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1285-1834 |
1.13e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1285 EEKEVEAHRSQLKaMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQR 1364
Cdd:pfam05483 200 EELRVQAENARLE-MHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1365 elsLLGRHMNSYKQSYEWLIQWLREARLRQEKieaaPVWDSKALKEQLTQEKKLLEEIEKNKD-QIENCQKDAKAYIDSL 1443
Cdd:pfam05483 279 ---LQDENLKELIEKKDHLTKELEDIKMSLQR----SMSTQKALEEDLQIATKTICQLTEEKEaQMEELNKAKAAHSFVV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1444 KDYEFQILAYRALQDPiasplKKPKMESASDNIIQEYVTLRTRYSELSTLTS---------QYIKFILETQRRLEDDEKA 1514
Cdd:pfam05483 352 TEFEATTCSLEELLRT-----EQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkevelEELKKILAEDEKLLDEKKQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1515 SEKLKEDEK--------------KRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAE---- 1576
Cdd:pfam05483 427 FEKIAEELKgkeqelifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKeltq 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1577 ---------------------------KQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTI 1629
Cdd:pfam05483 507 easdmtlelkkhqediinckkqeermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1630 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqKKKNAEDELKRKSEAEKEAARQK-QKALDELQKH-KM 1707
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN-KQLNAYEIKVNKLELELASAKQKfEEIIDNYQKEiED 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1708 QAEEAERRLKQAEEEKV---RQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLqeeaekLRKQEEEANK 1784
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGL------YKNKEQEQSS 739
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1785 AREQAEKELETWRlkaNEALRLRLRAEEEaqrkslaQEEAEKQKTEAERD 1834
Cdd:pfam05483 740 AKAALEIELSNIK---AELLSLKKQLEIE-------KEEKEKLKMEAKEN 779
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1711-2122 |
1.20e-06 |
|
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: 55.13 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1711 EAERRLKQAEEEKVRQikvveEVAQKTAATQLQAmsfseKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKA-REQA 1789
Cdd:pfam05557 6 ESKARLSQLQNEKKQM-----ELEHKRARIELEK-----KASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAlREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1790 ekeletwrlkanEALRLRLRAEEEAQRKslaQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1869
Cdd:pfam05557 76 ------------ELNRLKKKYLEALNKK---LNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1870 klsaEQEYirlKADFEHAEQQRGLLDNELQRLKnevnAAEKQRRQLEDELAKvrSEMDALLQMKIQAEKVSQSNTEKSKQ 1949
Cdd:pfam05557 141 ----LDLL---KAKASEAEQLRQNLEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1950 LLETEALKMKQLAEEAARLRSVAEEAKkqRQLAEDEAARQRAEAEKILKEKLAA-INEATRLKTEAEVALKAKEAENERL 2028
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLK--RKLEREEKYREEAATLELEKEKLEQeLQSWVKLAQDTGLNLRSPEDLSRRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2029 KR-QAEDEAY-QRKLLEDQAAQHKH----DIQEKITQLQSSSVSE---LDRQKNIVEETLRQKKVVEEEIHIIRINFERA 2099
Cdd:pfam05557 286 EQlQQREIVLkEENSSLTSSARQLEkarrELEQELAQYLKKIEDLnkkLKRHKALVRRLQRRVLLLTKERDGYRAILESY 365
|
410 420
....*....|....*....|....*.
gi 1655220517 2100 SKEKSDLEVELKKL---KGIADETQK 2122
Cdd:pfam05557 366 DKELTMSNYSPQLLeriEEAEDMTQK 391
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1649-2090 |
1.23e-06 |
|
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: 54.76 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1649 AEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAArQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIK 1728
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEK-KQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1729 VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgTVLQLQEEAEKLRKQEEEANKAREqaeKELETWRLKANealrlrl 1808
Cdd:pfam09731 122 SEQEKEKALEEVLKEAISKAESATAVAKEAKDD--AIQAVKAHTDSLKEASDTAEISRE---KATDSALQKAE------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1809 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAlkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1888
Cdd:pfam09731 190 ALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPE--HLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIF 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1889 qqrglldNELQRLKNEVNAAEKQRrqLEDELAKVRSEMDALlqmkiqaekvsqsntekSKQLLEtealkmKQLAEEAARL 1968
Cdd:pfam09731 268 -------PDIIPVLKEDNLLSNDD--LNSLIAHAHREIDQL-----------------SKKLAE------LKKREEKHIE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1969 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaaineatRLKTEAEVALKAKEAENE---RLKRQAED-EAYQRKLLED 2044
Cdd:pfam09731 316 RALEKQKEELDKLAEELSARLEEVRAADEAQL--------RLEFEREREEIRESYEEKlrtELERQAEAhEEHLKDVLVE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2045 QAAQ----HKHDIQEKITQ---LQSSSVSELDRQKNIVEETLRQKKVVEEEIH 2090
Cdd:pfam09731 388 QEIElqreFLQDIKEKVEEeraGRLLKLNELLANLKGLEKATSSHSEVEDENR 440
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2165-2342 |
1.26e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2165 QRKAAQDEVERL-----KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEdllsqeklrdefENA 2239
Cdd:PRK09510 100 QERLKQLEKERLaaqeqKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA------------AEA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2240 KKLAQAAETAKEKAEKeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAaAEAAALKQKQEADAE 2319
Cdd:PRK09510 168 KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA-AAKAAAEAKAAAEKA 241
|
170 180
....*....|....*....|...
gi 1655220517 2320 MAKHKKEAEQALKQKSQVEKELG 2342
Cdd:PRK09510 242 AAAKAAEKAAAAKAAAEVDDLFG 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2164-2562 |
1.34e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAK-EAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFEN--AK 2240
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERLEELRELEEELEELEAelAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2241 KLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEAD--- 2317
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlli 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2318 -AEMAKHKKEAEQALKQKSQVEK----ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV----KM 2388
Cdd:COG4717 255 aAALLALLGLGGSLLSLILTIAGvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppDL 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2389 QMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSL-------AEEAARLSVEAEETARQRKTAEAELAEQRALA 2461
Cdd:COG4717 335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeagveDEEELRAALEQAEEYQELKEELEELEEQLEEL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2462 EKMLKEKMQAIQEATkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdkETQGFQKSLEAERKRQLEISAEAEKLKLR 2541
Cdd:COG4717 415 LGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEE 491
|
410 420
....*....|....*....|.
gi 1655220517 2542 VKELSSAQAKAEEEATRFKKQ 2562
Cdd:COG4717 492 WAALKLALELLEEAREEYREE 512
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1885-2011 |
1.44e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 55.02 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1885 EHAEQQ-RGLLdnELQRLKNEVnAAEKQRRqledelakvrsemdALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAE 1963
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRT--------------KLLELQAESAAVESSGQSRAEALAEAEARLIEAEAE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 1964 -EAARLRSVAE--------EAKKQRQLAEDEAARQRAEAEkILKEKLAAINEATRLK 2011
Cdd:PTZ00491 736 vEQAELRAKALrieaeaelEKLRKRQELELEYEQAQNELE-IAKAKELADIEATKFE 791
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1686-2050 |
1.57e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1686 EAEKEAARQKQKaldelqkhkmQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEqgtv 1765
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDR---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1766 LQLQEEAEKLRKQEEEankareQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEaekqKTEAERDAKKKAKAEEAA 1845
Cdd:pfam02029 68 TAKREERRQKRLQEAL------ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEE----KRDSRLGRYKEEETEIRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1846 LKQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSE 1925
Cdd:pfam02029 138 KEYQENKWSTEVRQA--EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKK-VKYESKVFLDQKRGHPEVKSQNGEE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1926 MDALLQMKIQAEKVSQSNT----EKSKQLLETEaLKMKQLAEEAARLRSVAEEAKKQRQLaedEAARQRAEAEKILKEKL 2001
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSqereEEAEVFLEAE-QKLEELRRRRQEKESEEFEKLRQKQQ---EAELELEELKKKREERR 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2002 AAINEATRLKTEAEVALKAKEAENERL------KRQAEDEAYQRKLLEDQAAQHK 2050
Cdd:pfam02029 291 KLLEEEEQRRKQEEAERKLREEEEKRRmkeeieRRRAEAAEKRQKLPEDSSSEGK 345
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2314-2539 |
1.75e-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: 54.26 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2314 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMDEL 2393
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEEL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2394 LKlKVRIEEENLRLMQKNKDNTQKL---LAEEAEKMKSLAE--EAARLSVEAEETARQRKTAEAELAEQRALAE-KMLKE 2467
Cdd:pfam05667 383 EK-QYKVKKKTLDLLPDAEENIAKLqalVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiKELRE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2468 KMQAIQEATKLKaeaEELQKQKNQAQEKAKKlleDKQ---------EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKL 2538
Cdd:pfam05667 462 KIKEVAEEAKQK---EELYKQLVAEYERLPK---DVSrsaytrrilEIVKNIKKQKEEITKILSDTKSLQKEINSLTGKL 535
|
.
gi 1655220517 2539 K 2539
Cdd:pfam05667 536 D 536
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1276-1834 |
1.83e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1276 LRDVSKVPAEEKEVEAHRSQLKAMRAEAEAdQATFDRLQDELKAATSVS----DKMTRLHSERDAELEHYRQLAGSLLER 1351
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNlddeDELEQLQEELEARLESLSESVSEARER 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1352 wqavfaQIDLRQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapVWDSKALKEQLTQEKKLLEEIEKNKDQIEN 1431
Cdd:PRK04863 581 ------RMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEE--FEDSQDVTEYMQQLLERERELTVERDELAA 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1432 CQKDAKAYIDSL------KDYEFQILAYR----------------------ALQDPIASPLKKPKMESASDNIIQEYVTL 1483
Cdd:PRK04863 653 RKQALDEEIERLsqpggsEDPRLNALAERfggvllseiyddvsledapyfsALYGPARHAIVVPDLSDAAEQLAGLEDCP 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1484 RTRYselstltsqyikFILETQRRLEDDEKASEKLKEDEKKRMAEIQ------------------AQLETQKQLAEGHAK 1545
Cdd:PRK04863 733 EDLY------------LIEGDPDSFDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgraareKRIEQLRAEREELAE 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1546 SVAKAELEAQELKlKMKEDASQRQG--LAV-----------DAEKQKQNIQLELTQLKNlSEQEIRSKNQQLEEAQVSRR 1612
Cdd:PRK04863 801 RYATLSFDVQKLQ-RLHQAFSRFIGshLAVafeadpeaelrQLNRRRVELERALADHES-QEQQQRSQLEQAKEGLSALN 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1613 KLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE---------DELKR 1683
Cdd:PRK04863 879 RLLPRLNLL-------------ADETLA---DRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSvlqsdpeqfEQLKQ 942
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1684 K---SEAEKEAARQKQKALDEL--QKHKMQAEEAERRLKQAEE--EKVRQIKVVEEVAQKTAATQL-----QAMSFSEKT 1751
Cdd:PRK04863 943 DyqqAQQTQRDAKQQAFALTEVvqRRAHFSYEDAAEMLAKNSDlnEKLRQRLEQAEQERTRAREQLrqaqaQLAQYNQVL 1022
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1752 TKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRLRLRAEEEAqrkslaqEEAEK 1826
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQELQDLGVPadsgaEERARARRDELHARLSANRSRRNQLEKQLTFCEAEM-------DNLTK 1095
|
....*...
gi 1655220517 1827 QKTEAERD 1834
Cdd:PRK04863 1096 KLRKLERD 1103
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
199-298 |
1.84e-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: 49.96 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 199 DRVQKKTFTKWVNKHLMKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 274
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1655220517 275 LVNIRNDDIADGNPKLTLGLIWTI 298
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2421-2749 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2421 EEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEatKLKAEAEELQKQKNQAQEKAKKLL 2500
Cdd:pfam13868 6 DELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEE--EEEKEEERKEERKRYRQELEEQIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2501 EDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEakvRLQETEKQTTET 2580
Cdd:pfam13868 84 EREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2581 VVQKLETQrlqstreaddlkkaiAELEKEREKLKRDAQELQNKsketASAQQEQMEQQKAMLQqtfltekELLLKRERDv 2660
Cdd:pfam13868 161 LKEKAERE---------------EEREAEREEIEEEKEREIAR----LRAQQEKAQDEKAERD-------ELRAKLYQE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2661 EDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQaimdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLAD 2740
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
....*....
gi 1655220517 2741 ENKKLREKL 2749
Cdd:pfam13868 290 EHRRELEKQ 298
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2553-2747 |
2.11e-06 |
|
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: 53.80 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2553 EEEATRFKKQADEAKVRLQETEKQTTETvvqklETQRLQSTREADDLKKAIAELEKERE---------KLKRDAQELQNK 2623
Cdd:pfam15709 330 QEKASRDRLRAERAEMRRLEVERKRREQ-----EEQRRLQQEQLERAEKMREELELEQQrrfeeirlrKQRLEEERQRQE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2624 SKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEdekkklqkhledEVNKAKALKDEQQRQQKLMDEEKKKLQAIM 2703
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE------------EAERAEAEKQRQKELEMQLAEEQKRLMEMA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1655220517 2704 DEA-VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLRE 2747
Cdd:pfam15709 473 EEErLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1574-1832 |
2.15e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.99 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1574 DAEKQKQNIQLELTQLKnlseQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVR 1653
Cdd:COG1340 12 ELEEKIEELREEIEELK----EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1654 KAAQEEAERLRKQVNEETQKKKNaEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1733
Cdd:COG1340 88 NELREELDELRKELAELNKAGGS-IDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQkTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR-------- 1805
Cdd:COG1340 167 AE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKelrelrke 245
|
250 260
....*....|....*....|....*...
gi 1655220517 1806 -LRLRAEEEAQRKSLAQEEAEKQKTEAE 1832
Cdd:COG1340 246 lKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2360-2605 |
2.16e-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: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2360 EELQRVKAQVNDAVKQKAQveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVE 2439
Cdd:COG4913 235 DDLERAHEALEDAREQIEL----LEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2440 AEETARQRKTAEAELaeqRALAEKMLKEKMQAIQEatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQk 2519
Cdd:COG4913 311 LERLEARLDALREEL---DELEAQIRGNGGDRLEQ---LEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2520 sleaerkrqleisAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvVQKLETQRLQSTREADDL 2599
Cdd:COG4913 384 -------------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE-----IASLERRKSNIPARLLAL 445
|
....*.
gi 1655220517 2600 KKAIAE 2605
Cdd:COG4913 446 RDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2262-2712 |
2.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2262 QKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEKEL 2341
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---------LEELREELEKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2342 GLVKLQLDETDKQKalmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAE 2421
Cdd:COG4717 142 AELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2422 EAEKMKSLAEEAARLSVEAEETARQRKTAEAE--------------LAEQRALAEKMLKEKMQAIQEATKLKAEAEELQK 2487
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2488 QKNQAQEKAKKLLEDKQEIQQRldkETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRfKKQADEAK 2567
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEE---ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-EELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2568 VRLQETEKQTTETVVQKLETQrlqstREADDLKKAIAELEKEREKLKRDAQE-LQNKSKETASAQQEQMEQQKAMLQQtf 2646
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQA-----EEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEEELEELEE-- 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2647 ltEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQRQQKLMDEE---KKKLQAIMDEAVKKQKE 2712
Cdd:COG4717 447 --ELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYRE 511
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1681-1942 |
2.83e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1681 LKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEeKVRQIKvveevaqktaaTQLQAMSFSEKTTKLEESLKk 1760
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEA-ALEEFR-----------QKNGLVDLSEEAKLLLQQLS- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1761 eqgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKak 1840
Cdd:COG3206 223 ------ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI-- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1841 aeeaalkqkeNAEKELEKQRtfaEQIAQQklsAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEV---NAAEKQRRQLED 1917
Cdd:COG3206 295 ----------ALRAQIAALR---AQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEARLaelPELEAELRRLER 358
|
250 260
....*....|....*....|....*
gi 1655220517 1918 ELAKVRSEMDALLQmKIQAEKVSQS 1942
Cdd:COG3206 359 EVEVARELYESLLQ-RLEEARLAEA 382
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1767-2011 |
2.95e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1767 QLQEEAEKLRKQEEEANKAREQAEKELEtwrlkanealrlrlraeeeaQRKSLAQEEAEKQKTEAERDakkkakaeeaal 1846
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDARE--------------------QIELLEPIRELAERYAAARE------------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1847 kQKENAEKELEKQRTFAEQIAQQKLSAEQEyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLE-DELAKVRSE 1925
Cdd:COG4913 270 -RLAELEYLRAALRLWFAQRRLELLEAELE--ELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1926 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAIN 2005
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
....*.
gi 1655220517 2006 EATRLK 2011
Cdd:COG4913 427 EIASLE 432
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2481-2767 |
3.09e-06 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 52.65 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2481 EAEELQKQKNQAQEKAKKLLEDKQEIQQrLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE---EAT 2557
Cdd:pfam09728 2 AARELMQLLNKLDSPEEKLAALCKKYAE-LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKlcrELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2558 RFKKQADEAKVRLQETEKQTTETVVQKLETqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETAsAQQEQMEQ 2637
Cdd:pfam09728 81 KQNKKLKEESKKLAKEEEEKRKELSEKFQS-------TLKDIQDKMEEKSEKNNKLREENEELREKLKSLI-EQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2638 Q-KAMLQQTFLTEKELLLKRERDVEDEKKKLQkhlEDEVNKAKALkdeqQRQQKLMDEEKKKLQAIMDEAVKKQKEAE-- 2714
Cdd:pfam09728 153 HfEKLLKTKELEVQLAEAKLQQATEEEEKKAQ---EKEVAKAREL----KAQVQTLSETEKELREQLNLYVEKFEEFQdt 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2715 ------------AEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:pfam09728 226 lnksnevfttfkKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLE 290
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1497-2034 |
3.37e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1497 YIKFILETQRRLEDDEKaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEdasqrqglavdAE 1576
Cdd:PRK01156 195 SNLELENIKKQIADDEK-SHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKT-----------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1577 KQKQNIQLELTQLKNLSEQEIRSKNqqlEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQKLRDQaaeaekVRKAA 1656
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHAI------IKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1657 QEEAERlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVV----EE 1732
Cdd:PRK01156 333 VLQKDY------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1733 VAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ-----------EEEANKAREQAEKELETWRLKAN 1801
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1802 EALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLK 1881
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1882 -ADFEHAEQQRGLLDNE-LQRLKNEVNA----AEKQRRQLEDELAKVRSEMDALLQmKIQAEkvsQSNTEKSKQLLETEA 1955
Cdd:PRK01156 567 rTSWLNALAVISLIDIEtNRSRSNEIKKqlndLESRLQEIEIGFPDDKSYIDKSIR-EIENE---ANNLNNKYNEIQENK 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1956 LKMKQLAEEAARLRSVAEEaKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2034
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1926-2377 |
3.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1926 MDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQLAEDEAARQRAEAEKILKEKLAAI 2004
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2005 NEATRLKTEAEVALKAKEAENERLKRQAED-EAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQ 2081
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2082 KKVVEEEIHIIRINFERASKEKSDLEVELKKLK----------------------GIADETQKSKAKAEEEAEKLKKLAA 2139
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAAleerlkearlllliaaallallGLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2140 EEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEA-AQKSTAAEQKAQDV 2218
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2219 LSKNKEDLLSQEKLRDEFEnakklaqaaetakekaekeaalLRQKAEEAEKLKKAaedeaakQAKAQKDAERLRKEAEAE 2298
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEE----------------------LRAALEQAEEYQEL-------KEELEELEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2299 AAKRAAAEAAALKQK-QEADAEMAKHKKEAEQALKQKSQVEKELGLVklqldETDKQKALMDEELQRVKAQVNDAVKQKA 2377
Cdd:COG4717 419 EELLEALDEEELEEElEELEEELEELEEELEELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2311-2700 |
3.77e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 52.76 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQM 2390
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2391 dELLKLKVR-IEEENLRLMQKNKdnTQKLLAEE--AEKMKSLAEEAARLSVEAE-ETARQRKTAEAELAEQRALAEKM-- 2464
Cdd:pfam15742 86 -KHCQQKIReLELEVLKQAQSIK--SQNSLQEKlaQEKSRVADAEEKILELQQKlEHAHKVCLTDTCILEKKQLEERIke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2465 -------LKEKMQAIQEATK-LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdKETQGFQKSLEAERKRQLEISAEAE 2536
Cdd:pfam15742 163 aseneakLKQQYQEEQQKRKlLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI-QQQEAQLKQLENEKRKSDEHLKSNQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2537 KLKlrvKELSSAQAKAE---EEATRFKKQADeAKVRlQETEKQTTETVvqKLETQRLQSTREADDLKKAIAELEKEREKL 2613
Cdd:pfam15742 242 ELS---EKLSSLQQEKEalqEELQQVLKQLD-VHVR-KYNEKHHHHKA--KLRRAKDRLVHEVEQRDERIKQLENEIGIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2614 krdaqelqnksketasaqQEQMEQQKAMlQQTFLTEKELLLKrerdvedEKKKLQKHL---EDEVNKAKALKDEQQRQQK 2690
Cdd:pfam15742 315 ------------------QQQSEKEKAF-QKQVTAQNEILLL-------EKRKLLEQLteqEELIKNNKRTISSVQNRVN 368
|
410
....*....|
gi 1655220517 2691 LMDEEKKKLQ 2700
Cdd:pfam15742 369 FLDEENKQLQ 378
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2564-2782 |
3.96e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.29 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2564 DEAKVRLQEtEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQ 2643
Cdd:PRK00409 505 EEAKKLIGE-DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2644 QtfltEKELLLKRERDVEDEKKKLQkhledevnKAKALKDEQQRqqklMDEEKKKLQAIMDEAVKKQKEAEAEMKNK--- 2720
Cdd:PRK00409 584 K----EADEIIKELRQLQKGGYASV--------KAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKVGDEVKyls 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2721 --QKeMEALEKKRlEQEKLLADENKKLREKLESLEVTSKQaasKTKEIEVQTDKVPEEQLVSMT 2782
Cdd:PRK00409 648 lgQK-GEVLSIPD-DKEAIVQAGIMKMKVPLSDLEKIQKP---KKKKKKKPKTVKPKPRTVSLE 706
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1437-1760 |
4.19e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1437 KAYIDSLKDYEFQILAYRalqdpIASPLKKPKMESASDNIIQEYV---TLRTRYSELstltsQYIKFILETQRRLEDDEK 1513
Cdd:COG5022 813 RSYLACIIKLQKTIKREK-----KLRETEEVEFSLKAEVLIQKFGrslKAKKRFSLL-----KKETIYLQSAQRVELAER 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1514 ASEKLKEDEKKRMAEIQAQLETQKQLAEgHAKSVAKAELEaqelKLKMKEDASQRqglavdAEKQKQNIQLELTQLKNLS 1593
Cdd:COG5022 883 QLQELKIDVKSISSLKLVNLELESEIIE-LKKSLSSDLIE----NLEFKTELIAR------LKKLLNNIDLEEGPSIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1594 EQEIRsknQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLR--------- 1664
Cdd:COG5022 952 KLPEL---NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKelpvevael 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1665 ----KQVNEETQKKK--NAEDELKRKSEAEKEAARQKQKALdELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTa 1738
Cdd:COG5022 1029 qsasKIISSESTELSilKPLQKLKGLLLLENNQLQARYKAL-KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNR- 1106
|
330 340
....*....|....*....|..
gi 1655220517 1739 atqlQAMSFSEKTTKLEESLKK 1760
Cdd:COG5022 1107 ----NLVKPANVLQFIVAQMIK 1124
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2312-2734 |
4.37e-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: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2312 QKQEADAEMAKHKKEAEQAlkqKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVndavkqkAQVENELSKVKMQMD 2391
Cdd:pfam07888 35 RLEECLQERAELLQAQEAA---NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2392 ELLKLKVRIEEENLRLMQKNKDNTQKLLaEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlAEKMLKEKMQA 2471
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA-ERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2472 IQEatKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRqleisaeaeklklrvKELSSAQAK 2551
Cdd:pfam07888 183 TEE--ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALL---------------EELRSLQER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2552 AEeeatrfkkqadeakvrlqeTEKQTTETVVQKLETQRLQSTReaddlkkAIAELEKEReklkRDAQELQNKSKETASAQ 2631
Cdd:pfam07888 246 LN-------------------ASERKVEGLGEELSSMAAQRDR-------TQAELHQAR----LQAAQLTLQLADASLAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2632 QE---QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVK 2708
Cdd:pfam07888 296 REgraRWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV 375
|
410 420
....*....|....*....|....*.
gi 1655220517 2709 KQKEAEAEMKNKQKEMEALekKRLEQ 2734
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYI--RQLEQ 399
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1527-1783 |
4.37e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1527 AEIQAQLET---QKQLAEghAKSVAKAELEaQELKL-----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIR 1598
Cdd:PRK11281 39 ADVQAQLDAlnkQKLLEA--EDKLVQQDLE-QTLALldkidRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1599 SKNQQLEEAQVSRRkLEEeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE 1678
Cdd:PRK11281 116 ETLSTLSLRQLESR-LAQ----TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1679 DELKRKSEAE------KEAARQK------------QKALDELQKHKMQAEEA---------ERRLKQAEeekvrqiKVVE 1731
Cdd:PRK11281 191 PSQRVLLQAEqallnaQNDLQRKslegntqlqdllQKQRDYLTARIQRLEHQlqllqeainSKRLTLSE-------KTVQ 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 1732 EVAQKTAATQLQAMSFsekttkleesLKKEQGTVLQLqeeAEKLRKQEEEAN 1783
Cdd:PRK11281 264 EAQSQDEAARIQANPL----------VAQELEINLQL---SQRLLKATEKLN 302
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2392-2558 |
4.46e-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: 52.70 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2392 ELLKLKVRIEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA 2471
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKK-QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2472 IQeatklKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDK--ETQGFQKSLEAERKRqLEISAEAEKLKLRVKelssAQ 2549
Cdd:pfam05262 278 NQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKasEKEAEDKELEAQKKR-EPVAEDLQKTKPQVE----AQ 347
|
....*....
gi 1655220517 2550 AKAEEEATR 2558
Cdd:pfam05262 348 PTSLNEDAI 356
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
197-305 |
4.72e-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: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 267
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220517 268 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2583-2778 |
5.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2583 QKLETQ-RLQSTREA-DDLKKAIAELEKEREKLKRDA------QELQN-----------KSKETASAQQEQMEQQKAMLQ 2643
Cdd:TIGR02168 173 RRKETErKLERTRENlDRLEDILNELERQLKSLERQAekaeryKELKAelrelelallvLRLEELREELEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2644 QTFLTEKELLLKRERDVEDEKKKLQKhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKN---- 2719
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEElesk 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2720 ---KQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2778
Cdd:TIGR02168 332 ldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2582-2753 |
5.13e-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: 51.08 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2582 VQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETasaqqeqmeqqkamlqQTFLTEKELLLKrerDVE 2661
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL----------------EKEIKRLELEIE---EVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2662 DEKKKLQKHLeDEVNKAKALK------DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2735
Cdd:COG1579 73 ARIKKYEEQL-GNVRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170
....*....|....*...
gi 1655220517 2736 KLLADENKKLREKLESLE 2753
Cdd:COG1579 152 AELEAELEELEAEREELA 169
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2181-2737 |
5.27e-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: 53.30 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2181 AEANKLKDKAEKELEKQVI-LAKEAAQKSTAA--EQKAQDVLSKNKE---DLLSQEKLRDEFENAKKLAQAAETAKekae 2254
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRtLDDQWKEKRDELngELSAADAAVAKDRselEALEDQHGAFLDADIETAAADQEQLP---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2255 keaaLLRQKAEEAEKLKKAAED-----EAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKH----KK 2325
Cdd:pfam12128 351 ----SWQSELENLEERLKALTGkhqdvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALeselRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2326 EAEQALK----QKSQVEKELGLVKLQLD------ETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDE--- 2392
Cdd:pfam12128 427 QLEAGKLefneEEYRLKSRLGELKLRLNqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQase 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2393 --------LLKLKVRIEEENLRLMQKN--------------KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETAR----- 2445
Cdd:pfam12128 507 alrqasrrLEERQSALDELELQLFPQAgtllhflrkeapdwEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYgvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2446 -QRKTAEAELAEQRALAEKMLKEKmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQeiqqrldketQGFQKSleAE 2524
Cdd:pfam12128 587 lKRIDVPEWAASEEELRERLDKAE-EALQSAREKQAAAEEQLVQANGELEKASREETFAR----------TALKNA--RL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2525 RKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFKKQAD----EAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK 2600
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKN-KALAERKDSANERLNSLEAQLKqldkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLA 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2601 KAIAELEKEREKLKR--DAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVED-----------EKKKL 2667
Cdd:pfam12128 733 LLKAAIAARRSGAKAelKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRL 812
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2668 QKHLEDEVNKAKALKDEQQRQQKlmdEEKKKLQAIMdeavkkqKEAEAEMKNKQKEMEALEKKRLEQEKL 2737
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIA---DTKLRRAKLE-------MERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1872-2072 |
5.29e-06 |
|
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: 52.16 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1872 SAEQEYIRLKAdfehaeQQRGLLDNELQRLKNEVNAAE--KQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQ 1949
Cdd:TIGR02794 47 AVAQQANRIQQ------QKKPAAKKEQERQKKLEQQAEeaEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1950 LLETEA--LKMKQLAEEAARLRSVAEEAKKQRQL-----AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKE 2022
Cdd:TIGR02794 121 AEEAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2023 AENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQK 2072
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
783-875 |
5.32e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 48.09 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 783 HTFVTAATKELMWLNEKEEEEVNYDWSDRNTNMTAKKDNYSGLMRELELREKKVNGVQTTGDKLLRDGHPGRKTIEAFTA 862
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1655220517 863 ALQTQWSWILQLC 875
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
201-302 |
5.35e-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: 48.57 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 201 VQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 276
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1655220517 277 NIRNDDIADGNPKLTLGLIWTIILHF 302
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2424-2739 |
5.75e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2424 EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2503
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2504 QEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEatrfkkqadeakvrlQETEKQTTE---T 2580
Cdd:COG1340 81 DELNEKL--------NELREELDELRKELAELNKAGGSIDKLRKEIERLEWR---------------QQTEVLSPEeekE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2581 VVQKLE--TQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETAsaqqEQMEQQKAMLQQTFLTEKELllkreR 2658
Cdd:COG1340 138 LVEKIKelEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEADEL-----R 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2659 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLL 2738
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEELK 288
|
.
gi 1655220517 2739 A 2739
Cdd:COG1340 289 L 289
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2414-2789 |
5.95e-06 |
|
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: 52.65 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2414 NTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKtAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKNqAQ 2493
Cdd:pfam15709 170 HAERELIDKAKRRKGTKTDKTKTPKREREGKVHGE-AEAAVGKSR---ESKAEKKSELISKGKKTGAKRKRTQKERN-LE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2494 EKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQakaeeeatrfkkQADEAKVRLQET 2573
Cdd:pfam15709 245 VAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVSIDGRSSPT------------QTFVVTGNMESE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2574 EKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELl 2653
Cdd:pfam15709 313 EERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2654 lkRERDVEDEKkklQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEmeaLEKKRLE 2733
Cdd:pfam15709 392 --RKQRLEEER---QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKE---LEMQLAE 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2734 QEKLLADENKKlrEKLESLEvtSKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKK 2789
Cdd:pfam15709 464 EQKRLMEMAEE--ERLEYQR--QKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2310-2561 |
6.18e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.45 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKE----AEQALKQKSQVEKELGLVKLQLDETDKQKALMDE---ELQRVKAQVNDAVKQKAQVENE 2382
Cdd:COG1340 14 EEKIEELREEIEELKEKrdelNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2383 LSKVKMQMDELL-------KLKVRIE-------------EENLRLMQKNKDNTQKLlaEEAEKMKSLAEEAARLSVEAEE 2442
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIErlewrqqtevlspEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2443 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKetqgFQKSLE 2522
Cdd:COG1340 172 LRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELK 247
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220517 2523 AERKRQLEISaeaeklklRVKELSSAQAKAEEEATRFKK 2561
Cdd:COG1340 248 KLRKKQRALK--------REKEKEELEEKAEEIFEKLKK 278
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2168-2381 |
6.24e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2168 AAQDEVERLKQKAAEANKLKDKAEKELEKQvilAKEAAQKSTAAEQKAQDVlskNKEDLLSQEKLRDEFENAKKLAQAAE 2247
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQ---AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2248 TAKEKAEKEAALLRQKAEEAEK----LKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAemakh 2323
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAKraaaAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA----- 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2324 KKEAEQALKQKSQVEKELGLVKlqldETDKQKALMDEELQRVKAQVNDAVKQKAQVEN 2381
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1381-1795 |
6.41e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.65 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1381 EWLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAY------- 1453
Cdd:COG5185 157 ETGIIKDIFGKLTQELNQNLK--KLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEiinieea 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1454 -RALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRleDDEKASEKLKEDEKKRMAEI-QA 1531
Cdd:COG5185 235 lKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK--QFENTKEKIAEYTKSIDIKKaTE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1532 QLETQKQLAEGHAK-SVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVS 1610
Cdd:COG5185 313 SLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKES 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1611 ----RRKLEEEIHLIRIQLQTTIKQKSTADDELQ----KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelK 1682
Cdd:COG5185 393 ldeiPQNQRGYAQEILATLEDTLKAADRQIEELQrqieQATSSNEEVSKLLNELISELNKVMREADEESQ---------S 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKE- 1761
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALEn 543
|
410 420 430
....*....|....*....|....*....|....*.
gi 1655220517 1762 --QGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1795
Cdd:COG5185 544 liPASELIQASNAKTDGQAANLRTAVIDELTQYLST 579
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1505-1702 |
6.52e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1505 QRRLEDDEKasEKLKEDEKKRMAEIQAQL--ETQKQLAEGHAKSVAKAeleaqelKLKMKEDASQRQGLAVDAEKQKQNI 1582
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAKQaaLKQKQAEEAAAKAAAAA-------KAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1583 QLELTQLKnlseQEIRSKNQQLEEAQVsrrKLEEEihliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAEr 1662
Cdd:PRK09510 171 AEAEAAKK----AAAEAKKKAEAEAAA---KAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA- 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220517 1663 lrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1702
Cdd:PRK09510 232 ---------AEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1849-2037 |
6.53e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1849 KENAEKELEKQRTFAEQIAQQKLS-AEQEYIRLKADFEhaeqqrglldNELQRLKNEVNAAEKQRRQLEDELAKvrsEMD 1927
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQKEENLDR---KLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1928 ALLQMKIQAEKVSQSNTEKSKQLletealkmKQLAEEAARLRsvaeeaKKQRQLAEDEAARQRAEAEKILKEKLaainea 2007
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQEL--------EKKEEELEELI------EEQLQELERISGLTAEEAKEILLEKV------ 163
|
170 180 190
....*....|....*....|....*....|
gi 1655220517 2008 tRLKTEAEVALKAKEAENErLKRQAEDEAY 2037
Cdd:PRK12704 164 -EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1568-1916 |
6.60e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1568 RQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAA 1647
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1648 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQI 1727
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR 1807
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1808 LRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHA 1887
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340
....*....|....*....|....*....
gi 1655220517 1888 EQQRGLLDNELQRLKNEVNAAEKQRRQLE 1916
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2412-2645 |
6.78e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2412 KDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQ 2491
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2492 AQEKAKKLLEDKQEIQQRLDK-----ETQGFQ------KSLEAERKRQLEISAEAEKLKlrvKELSSAQAKAEEEATRFK 2560
Cdd:COG3883 84 RREELGERARALYRSGGSVSYldvllGSESFSdfldrlSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2561 KQADEAKVRLQEtekqttetvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2640
Cdd:COG3883 161 ALKAELEAAKAE------------LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*
gi 1655220517 2641 MLQQT 2645
Cdd:COG3883 229 AAAAA 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1193-1722 |
6.84e-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: 52.92 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1193 VQSELEGLKKDLNSITEKTE--EILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKT-----IDIVIRNTKDA 1265
Cdd:pfam12128 359 LEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEFNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1266 EDTVKSYES----RLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEhy 1341
Cdd:pfam12128 439 EYRLKSRLGelklRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE-- 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1342 rQLAGSLLERWQAVFAQidlRQRELSLLGRHMNSYKQSYEWLI---QWLRE-------------------ARLRQEKIEA 1399
Cdd:pfam12128 517 -ERQSALDELELQLFPQ---AGTLLHFLRKEAPDWEQSIGKVIspeLLHRTdldpevwdgsvggelnlygVKLDLKRIDV 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1400 aPVW--DSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEfqILAYRALQDpiasplkkpkmesASDNII 1477
Cdd:pfam12128 593 -PEWaaSEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREE--TFARTALKN-------------ARLDLR 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1478 QEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEK----LKEDEKKRMAEIQAQLETQKQLAEGhAKSVA----K 1549
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKkhqaWLEEQKEQKREARTEKQAYWQVVEG-ALDAQlallK 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1550 AELEAQELKLKMKEDASQRQ------GLAVDAE---KQKQNIQLELTQLKNLS--EQEIRSKNQQLEEAQVSRR------ 1612
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWykrdlaSLGVDPDviaKLKREIRTLERKIERIAvrRQEVLRYFDWYQETWLQRRprlatq 815
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1613 --KLEEEIHLIRIQL-------QTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAE----- 1678
Cdd:pfam12128 816 lsNIERAISELQQQLarliadtKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGErlaql 895
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1655220517 1679 DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1722
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREED 939
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1399-1667 |
6.98e-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: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1399 AAPVWDSKALKEQLTQE-KKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRAlqdpiasplkkpkmesasdnii 1477
Cdd:COG4942 12 ALAAAAQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1478 qeyvTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQEL 1557
Cdd:COG4942 70 ----RIRALEQELAALEAE----LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1558 KLKMKEDASQRQGLAVDAEkqkqniqlELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD 1637
Cdd:COG4942 142 KYLAPARREQAEELRADLA--------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
250 260 270
....*....|....*....|....*....|
gi 1655220517 1638 ELQKLRDQAAEAEKVRKAAQEEAERLRKQV 1667
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1691-1860 |
7.27e-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: 50.69 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1691 AARQKQKALDELQKHKMQAEEAERRLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQE 1770
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1771 EAEKLRKQEEEANKARE--QAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQ 1848
Cdd:COG1579 74 RIKKYEEQLGNVRNNKEyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|..
gi 1655220517 1849 KENAEKELEKQR 1860
Cdd:COG1579 154 LEAELEELEAER 165
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2325-2686 |
7.60e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.27 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2325 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMD-EELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEE 2403
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINiEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2404 NLRLMQKNKDNTQKLLAEEAEKMKSLAEE---------------AARLSVEAEETARQRKTAEAELAEQRALAEKMLKEK 2468
Cdd:COG5185 276 SSKRLNENANNLIKQFENTKEKIAEYTKSidikkatesleeqlaAAEAEQELEESKRETETGIQNLTAEIEQGQESLTEN 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2469 MQAIQEATK---LKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEisaeaeklklRVKEL 2545
Cdd:COG5185 356 LEAIKEEIEnivGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR----------QIEEL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2546 SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREaddLKKAIAELEKEREKLKRDAQELQNKSK 2625
Cdd:COG5185 426 QRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRS---VRSKKEDLNEELTQIESRVSTLKATLE 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2626 ETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhlEDEVNKAKALKDEQQ 2686
Cdd:COG5185 503 KLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP--ASELIQASNAKTDGQ 561
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2260-2767 |
8.17e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2260 LRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKSQVEK 2339
Cdd:PRK01156 192 LKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAM-----------DDYNNLKSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2340 ELGLVKLQLDETDKQKALmDEELQRVkaqVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEEnlrlMQKNKDNTQKLl 2419
Cdd:PRK01156 261 AESDLSMELEKNNYYKEL-EERHMKI---INDPVYKNRNYINDYFKYKNDIENKKQILSNIDAE----INKYHAIIKKL- 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2420 aEEAEKMKSLAEEAARlsvEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2499
Cdd:PRK01156 332 -SVLQKDYNDYIKKKS---RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2500 LEDKQEIQQRLDK---ETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQEtekq 2576
Cdd:PRK01156 408 KKELNEINVKLQDissKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEE---- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2577 ttetvvqkletqrlqstrEADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2656
Cdd:PRK01156 484 ------------------KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2657 ERDVEDEKKKLQKHLED------EVNKAKALKD--EQQRQQKLMDEEKKKLQAI---MDEAVKKQKEAEAEMKNKQKEME 2725
Cdd:PRK01156 546 DKYEEIKNRYKSLKLEDldskrtSWLNALAVISliDIETNRSRSNEIKKQLNDLesrLQEIEIGFPDDKSYIDKSIREIE 625
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1655220517 2726 AlEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:PRK01156 626 N-EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSII 666
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1503-1795 |
8.30e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-----LAEGHAKSVAKAELEAQ----ELKLKMKEDASQrQGLAV 1573
Cdd:PRK04778 116 LIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrkslLANRFSFGPALDELEKQlenlEEEFSQFVELTE-SGDYV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1574 DAEKQKQNIQLELTQLKNLSEQ--EIRSKNQ-----QLEEAQVSRRKLEEE-IHLIRIQLQTTIKQKSTADDELQKL--R 1643
Cdd:PRK04778 195 EAREILDQLEEELAALEQIMEEipELLKELQtelpdQLQELKAGYRELVEEgYHLDHLDIEKEIQDLKEQIDENLALleE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL----QKHKMQAEEAERRlKQA 1719
Cdd:PRK04778 275 LDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIdrvkQSYTLNESELESV-RQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1720 EEEKVRQIKVVEEVAQKTAAtqlQAMSFSEKTTKLEESLK------KEQgtvLQLQEEAEKLRKQEEEANKAREQAEKEL 1793
Cdd:PRK04778 354 EKQLESLEKQYDEITERIAE---QEIAYSELQEELEEILKqleeieKEQ---EKLSEMLQGLRKDELEAREKLERYRNKL 427
|
..
gi 1655220517 1794 ET 1795
Cdd:PRK04778 428 HE 429
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2310-2653 |
9.27e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQK-QEADAEMAKHKKEAEQALKQKSQVEKElglVKLQLDETDKQKALMDE------ELQRVKAQVNDAVKQ--KAQVE 2380
Cdd:PRK10929 28 ITQElEQAKAAKTPAQAEIVEALQSALNWLEE---RKGSLERAKQYQQVIDNfpklsaELRQQLNNERDEPRSvpPNMST 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2381 NELSKvkmqmdELLKLKVRIEEENlRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRAL 2460
Cdd:PRK10929 105 DALEQ------EILQVSSQLLEKS-RQAQQEQDRAREI-SDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2461 AekmlkekMQAiqEATKLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAE-AE 2536
Cdd:PRK10929 177 A-------LQA--ESAALKALVDELelaQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2537 KL-------------KLRV-KELSSA---QAKAEEEATRFKKQADEAKVRLQETEKQTTETvVQKL-------ETQRLQS 2592
Cdd:PRK10929 248 LLaeqsgdlpksivaQFKInRELSQAlnqQAQRMDLIASQQRQAASQTLQVRQALNTLREQ-SQWLgvsnalgEALRAQV 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2593 TREAD-----DLKKAIAELEKER-------EKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtflTEKELL 2653
Cdd:PRK10929 327 ARLPEmpkpqQLDTEMAQLRVQRlryedllNKQPQLRQIRQADGQPLTAEQNRILDAQLR-------TQRELL 392
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2436-2774 |
9.63e-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: 52.06 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2436 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL----------KAEAEELQK--------QKNQAQEKAK 2497
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAalagaemvRKNLEEGSQR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRLDKETQGFQKSLE--AERKRQLEISAEAEKLKL--RVKELSSAQAKAEEEATRFKKQAD--EAKVRLQ 2571
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEelEAQVTLV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2572 ET-EKQTTETVVQKLETQRLQSTREadDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEK 2650
Cdd:pfam07111 221 ESlRKYVGEQVPPEVHSQTWELERQ--ELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2651 EL------LLKRERD-VEDEKKKLQKHLEDEVNKAKALKDE-QQRQQKLMDEEKKklQAIMDEAVK-KQKEAEAE---MK 2718
Cdd:pfam07111 299 EFpkkcrsLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsAK 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2719 NKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVP 2774
Cdd:pfam07111 377 GLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIP 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2365-2728 |
1.00e-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: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2365 VKAQVNDAVKQKAQVENELSKVKMQMDELLKlkvriEEENLRLMQKNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETA 2444
Cdd:pfam12128 198 VKSMIVAILEDDGVVPPKSRLNRQQVEHWIR-----DIQAIAGIMKIRPEFTKL-QQEFNTLESAELRLSHLHFGYKSDE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2445 RQrktaEAELAEQRALAEKMLKEKMQAiqeatkLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK----S 2520
Cdd:pfam12128 272 TL----IASRQEERQETSAELNQLLRT------LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadieT 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2521 LEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVvqkLETQRLQSTREADDLK 2600
Cdd:pfam12128 342 AAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKI---REARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2601 KAIAELEKEREKLKRDAQELQNKSKETAsaqqeqmEQQKAMLQQTFLTEKELLLKRERDvedekkklqkhleDEVNKAKA 2680
Cdd:pfam12128 419 ALESELREQLEAGKLEFNEEEYRLKSRL-------GELKLRLNQATATPELLLQLENFD-------------ERIERARE 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2681 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2728
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE 526
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4086-4124 |
1.05e-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: 1.05e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1655220517 4086 YLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTAFEL 4124
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2344-2574 |
1.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2344 VKLQLDETDKQKALMDEELQRVKAQVNDAvkqkaqvENELSKVKMQMDEllklkVRIEEENLRLMQKNKDNTQKLLAEEA 2423
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQKNGL-----VDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2424 EkmksLAEEAARLSvEAEETARQRKTAEAELAEQRALAekmlkekmQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDK 2503
Cdd:COG3206 234 E----LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQ--------QLRAQLAELEAELAELSARYTPNHPDVIALRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2504 QEIQQRLDKETQGFQKSLEAE----RKRQLEISAEAEKLKLRVKELSSAQAKAEE---EATRFKKQADEAKVRLQETE 2574
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1601-1789 |
1.13e-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: 51.00 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1601 NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAEDE 1680
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK-QAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1681 LKRKSEAEKEaarqkQKALDELQKhkmQAEEaERRLKQAEEEKVRQikvvEEVAQKTAATQLQAMSFSEKTTKLEESLKK 1760
Cdd:TIGR02794 132 AKAKAEAEAE-----RKAKEEAAK---QAEE-EAKAKAAAEAKKKA----EEAKKKAEAEAKAKAEAEAKAKAEEAKAKA 198
|
170 180
....*....|....*....|....*....
gi 1655220517 1761 EQGTVLQLQEEAEKLRKQEEEANKAREQA 1789
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1640-1826 |
1.22e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1640 QKLRDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAEDELKRKSEAE--------KEAARQKQKALDELQKHKM---- 1707
Cdd:PRK00409 530 RELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQKGGYasvk 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1708 --QAEEAERRLKQAEEEKVRQIKVveevaQKTAATQLQA------MSFSEKTTKLEESLKKEqgtvLQLQEEAEKLR--- 1776
Cdd:PRK00409 606 ahELIEARKRLNKANEKKEKKKKK-----QKEKQEELKVgdevkyLSLGQKGEVLSIPDDKE----AIVQAGIMKMKvpl 676
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1777 KQEEEANKAREQAEKELETWRLKANEA---LRLR-LRAEEeaqrkslAQEEAEK 1826
Cdd:PRK00409 677 SDLEKIQKPKKKKKKKPKTVKPKPRTVsleLDLRgMRYEE-------ALERLDK 723
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1362-1913 |
1.28e-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: 51.67 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1362 RQRELSLLGRHMNSYKQSYEWLIQWLREARLRQEKIEAAPVWDSKALKEQLT---QEKKLLEEIEKNKDQIENCQKDAKA 1438
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1439 YIDSLKD--YEFQILAYRALQDPIASPLKKPKMESASDNI---IQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEK 1513
Cdd:pfam05557 105 VISCLKNelSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1514 ASEKLK--EDEKKRMAEIQAQLETQ----KQLAEGHA-KSVAKAELEAQELKLKMKEDAsqrQGLAVDAEKQKQNIQLEL 1586
Cdd:pfam05557 185 DSEIVKnsKSELARIPELEKELERLrehnKHLNENIEnKLLLKEEVEDLKRKLEREEKY---REEAATLELEKEKLEQEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1587 TQLKNLSEQ---EIRSK---NQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEA 1660
Cdd:pfam05557 262 QSWVKLAQDtglNLRSPedlSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNEETQKK-------KNAEDELKrKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEV 1733
Cdd:pfam05557 342 RRLQRRVLLLTKERdgyrailESYDKELT-MSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQKTAATQLQAMSFSEKTTKLE-ESLKKEQGTvLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKAnealrLRLRAEE 1812
Cdd:pfam05557 421 ERELQALRQQESLADPSYSKEEvDSLRRKLET-LELERQRLREQKNELEMELERRCLQGDYDPKKTKV-----LHLSMNP 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1813 EAQRKSLAQEEAEKQKTEAERdakkkakaeeaALKQKENAEKELEKQRTFAEQIAQQklsAEQEYIRLKADFEHAEQQrg 1892
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIER-----------LKRLLKKLEDDLEQVLRLPETTSTM---NFKEVLDLRKELESAELK-- 558
|
570 580
....*....|....*....|.
gi 1655220517 1893 lldneLQRLKNEVNAAEKQRR 1913
Cdd:pfam05557 559 -----NQRLKEVFQAKIQEFR 574
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2420-2645 |
1.28e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2420 AEEAEKMKSLAEEAARLSVEAEETARQRKTAEAE--LAEQRALAEKMLKEKMQAIQE------ATKLKAEAEELQKQKNQ 2491
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQNLELRREEARKALefLEEQLPELRKELEEAEAALEEfrqkngLVDLSEEAKLLLQQLSE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2492 AQEKAKKLLEDKQEIQQRLDKetqgFQKSLEAERKRQLEISAEAEKLKLRvKELSSAQAKAEEEATRFK------KQADE 2565
Cdd:COG3206 224 LESQLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPVIQQLR-AQLAELEAELAELSARYTpnhpdvIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2566 AKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2643
Cdd:COG3206 299 QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElyESLLQRLEEAR 378
|
..
gi 1655220517 2644 QT 2645
Cdd:COG3206 379 LA 380
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1544-1738 |
1.29e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1544 AKSVAKAEL-EAQELKLKMKEDASQRqglavdAEKQKQNIQL----ELTQLKNLSEQEIRSKNQQLEeaqvsrrkleeei 1618
Cdd:PRK12704 25 RKKIAEAKIkEAEEEAKRILEEAKKE------AEAIKKEALLeakeEIHKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1619 hliriQLQTTIKQK-STADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQkqk 1697
Cdd:PRK12704 86 -----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1655220517 1698 aldelqkhkMQAEEAErrlKQAEEEKVRQIKVVEEVAQKTA 1738
Cdd:PRK12704 158 ---------ILLEKVE---EEARHEAAVLIKEIEEEAKEEA 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2625-2767 |
1.36e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2625 KETASAQQEQMEQQ-KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKalKDEQQRQQKLMDEE---KKKLQ 2700
Cdd:PRK12704 26 KKIAEAKIKEAEEEaKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERR--NELQKLEKRLLQKEenlDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2701 AImdeaVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLrEKLESL--------------EVTSKQAASKTKEI 2766
Cdd:PRK12704 104 LL----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaeeakeillekveEEARHEAAVLIKEI 178
|
.
gi 1655220517 2767 E 2767
Cdd:PRK12704 179 E 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2439-2579 |
1.37e-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: 49.92 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2439 EAEETARQRKTAEAELAEQRalaekmlKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KE 2513
Cdd:COG1579 18 ELDRLEHRLKELPAELAELE-------DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2514 TQGFQKSLEAERKRQ-------LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTE 2579
Cdd:COG1579 91 YEALQKEIESLKRRIsdledeiLELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2459-2717 |
1.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2459 ALAEKMLKEKMQAIQEATK-----LKAEAEELQKQKNQAQEKAKKLLEDKQEIQqrLDKETQGFQKSLEAERKRQLEISA 2533
Cdd:COG3206 156 ALAEAYLEQNLELRREEARkalefLEEQLPELRKELEEAEAALEEFRQKNGLVD--LSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2534 EAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvQKLETQRLQSTREADDLKkaiaELEKEREKL 2613
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVI----ALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2614 KRDAQELQNKSKETASAQQEQMEQQKAMLQQTfltekelllkrerdvedekkklqkhLEDEVNKAKALKDEQQRQQKLMd 2693
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEALQAREASLQAQ-------------------------LAQLEARLAELPELEAELRRLE- 357
|
250 260
....*....|....*....|....
gi 1655220517 2694 EEKKKLQAIMDEAVKKQKEAEAEM 2717
Cdd:COG3206 358 REVEVARELYESLLQRLEEARLAE 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1817-2018 |
1.39e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1817 KSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN 1896
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1897 ELQ--RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALK-------MKQLAEEAAR 1967
Cdd:COG4717 124 LLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslateeeLQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1968 LRSVAEEAKKQRQLAEDEAARQRAEAEKiLKEKLAAINEATRLKTEAEVAL 2018
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEARLLLL 253
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2443-2766 |
1.41e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2443 TARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-LLEDKQEI----QQRL-DKETQG 2516
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRfSLLKKETIylqsAQRVeLAERQL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2517 FQKSLEAERKRQL-EISAEAEKLKLRVK--ELSSAQAKAE---EEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL 2590
Cdd:COG5022 885 QELKIDVKSISSLkLVNLELESEIIELKksLSSDLIENLEfktELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVES 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2591 QSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEqqkamlqqtfLTEKELLLKRERDVEDEKKKLQKH 2670
Cdd:COG5022 965 KLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGA----------LQESTKQLKELPVEVAELQSASKI 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2671 LEDEVNKAKALKDEQQrQQKLMDEEKKKLQAIMdEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2750
Cdd:COG5022 1035 ISSESTELSILKPLQK-LKGLLLLENNQLQARY-KALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPA 1112
|
330
....*....|....*.
gi 1655220517 2751 SLEVTSKQAASKTKEI 2766
Cdd:COG5022 1113 NVLQFIVAQMIKLNLL 1128
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1767-2041 |
1.42e-05 |
|
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: 50.81 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1767 QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQktEAERdakkkakAEEAAL 1846
Cdd:pfam15558 43 KRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQ--ENQR-------QEKLER 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1847 KQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEM 1926
Cdd:pfam15558 114 ARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1927 DALLqMKIQAEKVSQSNTEKSKQLLETEALKMKQLA----EEAARLRSVAEEAKKQRQ--------LAEDEAARQRAEAE 1994
Cdd:pfam15558 194 EELL-RRLSLEQSLQRSQENYEQLVEERHRELREKAqkeeEQFQRAKWRAEEKEEERQehkealaeLADRKIQQARQVAH 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1655220517 1995 KILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKL 2041
Cdd:pfam15558 273 KTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1548-1744 |
1.50e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1548 AKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEI-HLIRIQ-- 1624
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELgERARALyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1625 -------LQTTIKQKSTAD-----DELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAA 1692
Cdd:COG3883 98 sggsvsyLDVLLGSESFSDfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 1693 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQA 1744
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
202-309 |
1.53e-05 |
|
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: 47.73 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 268
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655220517 269 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 309
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2311-2498 |
1.54e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEADAEMAKHKKEAEQA--LKQKSQVE----KELGLVKLQLDETDKQKAlmDEELQRVKAQVNDAVKQKAQVENELS 2384
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAE--EAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2385 KVKMQMDELLKLKVRIEEENLRL----MQKNKDNTQKLLAEEAEKMKSLAEEAARlsveAEETARQRKTAEaelAEQRAL 2460
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKaeaeAAKKAAAEAKKKAEAEAAAKAAAEAKKK----AEAEAKKKAAAE---AKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655220517 2461 AEKmlkeKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2498
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1566-1776 |
1.60e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1566 SQRQGLAVD----AEKQKQNIQLELTQL-KNLSEQEIRSKnQQLEEAQvsrrKLEEEIHLIRIQLQttiKQKSTADDELQ 1640
Cdd:PRK00409 494 AKRLGLPENiieeAKKLIGEDKEKLNELiASLEELERELE-QKAEEAE----ALLKEAEKLKEELE---EKKEKLQEEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1641 KLRDQAA-EAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQA 1719
Cdd:PRK00409 566 KLLEEAEkEAQQAIKEAKKEADEIIKELRQLQKGGYAS-----VKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVG 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1720 EEEKVRQIK----VVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1776
Cdd:PRK00409 641 DEVKYLSLGqkgeVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1865-2082 |
1.70e-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: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1865 QIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRqlEDELAKVrsemdALLQMKIQAEKVSQSNT 1944
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--AEQAAKQ-----AEEKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1945 EKSKQLletEALKMKQLAEEAAR------LRSVAEEAKKQRQLAEDEA---ARQRAEAE-KILKEKLAAINEATRLKTEA 2014
Cdd:TIGR02794 131 EAKAKA---EAEAERKAKEEAAKqaeeeaKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEaKAKAEEAKAKAEAAKAKAAA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2015 EVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQK 2082
Cdd:TIGR02794 208 EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1693-1877 |
1.71e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1693 RQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVvEEVAQKTAATQLQAmsfsekttkleeslKKEQGTVLQLQEEA 1772
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEIAI-AQANREAEEAELEQ--------------EREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1773 EKLRKQEE---EANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1849
Cdd:COG2268 245 ELAKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
|
170 180
....*....|....*....|....*....
gi 1655220517 1850 ENAEKELEKQRTFAEQIAQQKLS-AEQEY 1877
Cdd:COG2268 325 AEAEAEAIRAKGLAEAEGKRALAeAWNKL 353
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1427-1700 |
1.80e-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: 50.77 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1427 DQIENCQKDAKAYIDSLKDYEFQ--------ILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYI 1498
Cdd:pfam05262 79 DHILNLRRILAGYLMAAYGYERSdaetiakfITIYNAVYRGDLDYFKEFYKEVVTKSLTKENAGLARRYDQWPGKTQIVI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1499 KFileTQRRLED-----------DEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKsvaKAELEAQELKLKMKEDASQ 1567
Cdd:pfam05262 159 PL---KKNILSGnvsdvdtdsisDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAK---RAQQLKEELDKKQIDADKA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1568 RQGLAV---DAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEeihliriQLQTTIKQKstaDDELQKLRD 1644
Cdd:pfam05262 233 QQKADFaqdNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE-------KAQIEIKKN---DEEALKAKD 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 1645 QAAEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALD 1700
Cdd:pfam05262 303 HKAFDLK-QESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3217-3250 |
1.87e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.87e-05
10 20 30
....*....|....*....|....*....|....
gi 1655220517 3217 LLEAQAATGFVIDPVKNEKVSVDDAVKSGLVGPE 3250
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2664-2773 |
1.92e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2664 KKKLQKHLEDEVNKAKALKDEQQRQQKlmDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK 2743
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAE--AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|
gi 1655220517 2744 KLREKLESLEVTSKQAASKTKEIEVQTDKV 2773
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1593-2080 |
1.98e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1593 SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLrKQVNEETQ 1672
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-SMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1673 KKKNAEDELKRkseAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEekvrQIKVVEEVAQKTAATQLQAMSFSEKTT 1752
Cdd:PRK01156 274 YYKELEERHMK---IINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA----EINKYHAIIKKLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1753 KLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR------LRAEEEAQRKSLAQEEAEK 1826
Cdd:PRK01156 347 RYDD-LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQeidpdaIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 QKTEAERDAKKKAKAEEAALKQKENAEKEL---------EKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNE 1897
Cdd:PRK01156 426 SSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1898 LQRL-KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKqlaeeaarlRSVAEEAK 1976
Cdd:PRK01156 506 KEYLeSEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS--LKLEDLDSK---------RTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1977 KQRQLAEDEAARQRAEaekilkEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAY----QRKLLEDQAAQhKHD 2052
Cdd:PRK01156 575 AVISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEK 647
|
490 500
....*....|....*....|....*...
gi 1655220517 2053 IQEKITQLQSSSVSELDRQKNIVEETLR 2080
Cdd:PRK01156 648 LRGKIDNYKKQIAEIDSIIPDLKEITSR 675
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4084-4121 |
2.02e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 2.02e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 4084 KKYLEGVSCIAGVFVESTKERLSIYQAMKKNMIRPGTA 4121
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1896-2056 |
2.07e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1896 NELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQA-EKVSQSNTEKSKQLLET---EALKMKQLAEEAARLRSV 1971
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEAakqAALKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1972 AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKH 2051
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
....*
gi 1655220517 2052 DIQEK 2056
Cdd:PRK09510 225 AAAAK 229
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2964-3000 |
2.10e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.10e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655220517 2964 TKFLDVQLATGGIIDPVNSHRLPLQTAYKQGQFDPDM 3000
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1187-1722 |
2.13e-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: 51.20 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1187 TAEQMK--VQSELEGLKKDLNSITEKTEEILASPQQSSSAPMLRSELDVTLKKMDHVYGLSSVYLDKLKTI--------- 1255
Cdd:TIGR00606 602 SLEQNKnhINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLtdenqsccp 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1256 --DIVIRNTKDAEDTVKSYESRLRDV-SKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHS 1332
Cdd:TIGR00606 682 vcQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1333 ERDAELEHYRQLAGSL---LERWQAVFAQIDLRQRelslLGRHMNSYKQSYEWLIQWLREARLRQEKIEAapvwdSKALK 1409
Cdd:TIGR00606 762 RLKNDIEEQETLLGTImpeEESAKVCLTDVTIMER----FQMELKDVERKIAQQAAKLQGSDLDRTVQQV-----NQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1410 EQLTQEKKLLEEIEKNKDQIENCQKDA---KAYIDSLKDYEFQILAYRALQDPIAsplkkpkmesasdniiQEYVTLRTR 1486
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIqhlKSKTNELKSEKLQIGTNLQRRQQFE----------------EQLVELSTE 896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1487 YSELSTLTSQYIKFILETQRRLEDDEKASEKL--KEDEKKRMAEIQAQLetqkqlaeghaksvakaeleaqelklkMKED 1564
Cdd:TIGR00606 897 VQSLIREIKDAKEQDSPLETFLEKDQQEKEELisSKETSNKKAQDKVND---------------------------IKEK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1565 ASQRQGLAVDAEKQkqnIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRD 1644
Cdd:TIGR00606 950 VKNIHGYMKDIENK---IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKR 1026
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1645 QAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAldELQKHKMQAEEAERRLKQAEEE 1722
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGY--EKEIKHFKKELREPQFRDAEEK 1102
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2312-2576 |
2.35e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.72 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2312 QKQEAD-AEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKAlmdeelQRVKAQVNDAVKQ-----KAQVENELSK 2385
Cdd:PRK05035 441 IEQEKKkAEEAKARFEARQARLEREKAARE---------ARHKKAA------EARAAKDKDAVAAalarvKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2386 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAE-----QRAL 2460
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKA-AVAAAIARAKAKKAAQQAANAEAEEEVdpkkaAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2461 AEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfqKSLEAERKRQLEISAEAEKLKL 2540
Cdd:PRK05035 585 AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEP-----EEPVDPRKAAVAAAIARAKARK 659
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655220517 2541 RVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2576
Cdd:PRK05035 660 AAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1524-1811 |
2.43e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1524 KRMAEIQAQLEtqkQLAEGHAKSVAKaeleaqelKLKMKEDASQRQGLAvdaEKQKQNIQLELT----QLKNLSEQEIRS 1599
Cdd:COG2268 116 RDPEEIEELAE---EKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1600 KNQQLEeAQvSRRKLEEeihLIRIQlqttIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKnAED 1679
Cdd:COG2268 182 ENNYLD-AL-GRRKIAE---IIRDA----RIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAK-KKA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1680 ELKRKSEAEKeaArqkqkaldelqkhkmqaeEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttkLEESLK 1759
Cdd:COG2268 252 EERREAETAR--A------------------EAEAAYEIAEANAEREVQRQLEIAEREREIELQEKE-------AEREEA 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1760 KEQGTVlQLQEEAEKLRKQEE---EANKAREQAEKELETWRLKA------NEALRLRLRAE 1811
Cdd:COG2268 305 ELEADV-RKPAEAEKQAAEAEaeaEAEAIRAKGLAEAEGKRALAeawnklGDAAILLMLIE 364
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1406-1795 |
2.50e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.62 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1406 KALKEQLTQEKKLLEEIEKNKDQIENCQKdakayidslkdyefQILAYRALQDPIASPLkkpkmesasDNIIQEYVTLRT 1485
Cdd:pfam06160 107 EELDELLESEEKNREEVEELKDKYRELRK--------------TLLANRFSYGPAIDEL---------EKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1486 RYSELSTlTSQYIK---FILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAksvakaELEAQELKLKmk 1562
Cdd:pfam06160 164 QFEELTE-SGDYLEareVLEKLEEETDALEELMEDIPPLYEELKTELPDQLE---ELKEGYR------EMEEEGYALE-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1563 edasqrqglavdaekqKQNIQLELTQLKN-LSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQK 1641
Cdd:pfam06160 232 ----------------HLNVDKEIQQLEEqLEENLALLENLELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1642 LRDQAAEAEKVRKAAQEEAERLRK--QVNEEtqkkknaedelkrkseaEKEAARQKQKALDELQKhkmqaeeaerrlkqa 1719
Cdd:pfam06160 296 IEDYLEHAEEQNKELKEELERVQQsyTLNEN-----------------ELERVRGLEKQLEELEK--------------- 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 1720 eeekvRQIKVVEEVAQKTAA-TQLQAMsFSEKTTKLEEsLKKEQgtvLQLQEEAEKLRKQEEEANKAREQAEKELET 1795
Cdd:pfam06160 344 -----RYDEIVERLEEKEVAySELQEE-LEEILEQLEE-IEEEQ---EEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4544-4581 |
2.79e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.79e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 4544 QRFLEVQYLTGGLIEPDTTGRVSIDEAVKKGSLDARTA 4581
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1769-1904 |
2.84e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1769 QEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS---LAQEEAEKQKTEAERDakkKAKAEEAA 1845
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETaraEAEAAYEIAEANAERE---VQRQLEIA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1846 LKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADfEHAEQQ----RGLLDNELQRLKNE 1904
Cdd:COG2268 287 EREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2497-2763 |
2.94e-05 |
|
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: 50.07 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2497 KKLLEDKQEIQQR---LDKetqgfQKSLEAERKRQLEisAEAEKLKLRVKELSSAQAKAEEEATRF---KKQADEakvrL 2570
Cdd:pfam05622 3 SEAQEEKDELAQRcheLDQ-----QVSLLQEEKNSLQ--QENKKLQERLDQLESGDDSGTPGGKKYlllQKQLEQ----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2571 QEtekqttetvvqklETQRLQSTReaDDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE-----QMEQQKAMLQQT 2645
Cdd:pfam05622 72 QE-------------ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEEAQALKDEmdilrESSDKVKKLEAT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2646 FLTEKELL-----LKR------ERDVEDEKKKLQkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKkqkeAE 2714
Cdd:pfam05622 137 VETYKKKLedlgdLRRqvklleERNAEYMQRTLQ--LEEELKKANALRGQLETYKRQVQELHGKLSEESKKADK----LE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1655220517 2715 AEMKNKQKEMEALEKkrlEQEKLLAdENKKLREKLESLEVTSKQAASKT 2763
Cdd:pfam05622 211 FEYKKLEEKLEALQK---EKERLII-ERDTLRETNEELRCAQLQQAELS 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2377-2829 |
3.06e-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: 50.61 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2377 AQVENELSKVKMQMDELLKLKVRIEEENLRL--MQKNKDNTQKLLAEE-AEKMKSLAEEAARLSVE--AEETARQRKTAE 2451
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIasRQEERQETSAELNQLlRTLDDQWKEKRDELNGElsAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2452 AELAEQRALA------EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-- 2523
Cdd:pfam12128 324 LEALEDQHGAfldadiETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKir 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2524 -ERKRQL-EISAEAEKLK--LRvKELSSAQAKAEEEATRFKKQADEAKVRL---QETEKQTTETVVQKLETQRLQSTREA 2596
Cdd:pfam12128 404 eARDRQLaVAEDDLQALEseLR-EQLEAGKLEFNEEEYRLKSRLGELKLRLnqaTATPELLLQLENFDERIERAREEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2597 -----DDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQ--------------QKAMLQQTF--LTEKELLLK 2655
Cdd:pfam12128 483 anaevERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkEAPDWEQSIgkVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2656 RERDVE------------------------DEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2711
Cdd:pfam12128 563 TDLDPEvwdgsvggelnlygvkldlkridvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2712 EAEAEMKNKQKEMEAL----EKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQLVSMTT---- 2783
Cdd:pfam12128 643 FARTALKNARLDLRRLfdekQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqv 722
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2784 VETTKKVFNGSV---------------EAVKKDGASPLAFEGIRESVPAERLLEIGVLTKK 2829
Cdd:pfam12128 723 VEGALDAQLALLkaaiaarrsgakaelKALETWYKRDLASLGVDPDVIAKLKREIRTLERK 783
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1595-1865 |
3.13e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1595 QEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEaekVRKAAQEEAERlRKQVNEETQKK 1674
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---LREEAQELREK-RDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1675 KNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE-------KVRQIKVVEEVAQKtaATQLQAMsf 1747
Cdd:COG1340 77 KEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqtevlsPEEEKELVEKIKEL--EKELEKA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1748 sEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ----EEEANKAREQ---AEKELETWRLKANEALRLRLRAEEEAQRksLA 1820
Cdd:COG1340 153 -KKALEKNEKLKELRAELKELRKEAEEIHKKikelAEEAQELHEEmieLYKEADELRKEADELHKEIVEAQEKADE--LH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220517 1821 QEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQ 1865
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1809-2010 |
3.25e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1809 RAEEEAQRKSLAQEEAEKQKTEAERDAkkkakaeeaalkQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAE 1888
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQER------------LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1889 QQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllqMKIQAEKVSQSNTEKSKQLLETEAlkmKQLAEEAARL 1968
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220517 1969 RSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL 2010
Cdd:PRK09510 218 KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2462-2640 |
3.37e-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: 50.00 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2462 EKMLKEKMQAI---QEATKLKA-EAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEK 2537
Cdd:pfam05262 184 EALREDNEKGVnfrRDMTDLKErESQEDAKRAQQLKEELDKKQIDADKAQQKADFA----QDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2538 lklrvkelssAQAKAEEEATRFKKQADEAKVRLQETEKQTTEtvvQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA 2617
Cdd:pfam05262 260 ----------LPKPADTSSPKEDKQVAENQKREIEKAQIEIK---KNDEEALKAKDHKAFDLKQESKASEKEAEDKELEA 326
|
170 180
....*....|....*....|...
gi 1655220517 2618 QElqnKSKETASAQQEQMEQQKA 2640
Cdd:pfam05262 327 QK---KREPVAEDLQKTKPQVEA 346
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1644-1989 |
3.64e-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: 49.95 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE---AEKEAARQKQKALDELQKHKMQAEEAERRLKqaE 1720
Cdd:pfam15709 218 EKKSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETedaSERGAFSSDSVVEDPWLSSKYDAEESQVSID--G 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1721 EEKVRQIKVV-------EEVAQKTAATQLQAMSFSEKTTKleESLKKEQGTVLQLQEEaeklRKQEEEANKAREQAEKEL 1793
Cdd:pfam15709 296 RSSPTQTFVVtgnmeseEERSEEDPSKALLEKREQEKASR--DRLRAERAEMRRLEVE----RKRREQEEQRRLQQEQLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1794 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEaerdakkkakaeeaalkqkenaekelEKQRTFAEQIAQQKLSA 1873
Cdd:pfam15709 370 RAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEE--------------------------ERKQRLQLQAAQERARQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1874 EQEYIRLKAdfehAEQQRGLLDNELQRLknevnAAEKQRR-QLEDELAKvrsEMDALLQMKIQAEKVSQSNTEKSKQLLE 1952
Cdd:pfam15709 424 QQEEFRRKL----QELQRKKQQEEAERA-----EAEKQRQkELEMQLAE---EQKRLMEMAEEERLEYQRQKQEAEEKAR 491
|
330 340 350
....*....|....*....|....*....|....*..
gi 1655220517 1953 TEALKMKQLAEEAARLrsVAEEAKKQRQlaedEAARQ 1989
Cdd:pfam15709 492 LEAEERRQKEEEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1848-2033 |
3.67e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1848 QKENAEKELEKqrtfAEQiAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD 1927
Cdd:COG3206 183 QLPELRKELEE----AEA-ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1928 ALLQmkiqaekvSQSNTEKSKQLLETEAlkmkQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEAE---KIL 1997
Cdd:COG3206 258 ELLQ--------SPVIQQLRAQLAELEA----ELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEaelEAL 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220517 1998 KEKLAAINEA-TRLKTEAEvALKAKEAENERLKRQAE 2033
Cdd:COG3206 326 QAREASLQAQlAQLEARLA-ELPELEAELRRLEREVE 361
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2415-2724 |
3.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2415 TQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2494
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2495 KAKKLLEDKQEIQQRLdKETQGFQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETE 2574
Cdd:COG4372 102 ELESLQEEAEELQEEL-EELQKERQDLEQQRK---QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2575 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLL 2654
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2655 KRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2724
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4294-4322 |
3.71e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 3.71e-05
10 20
....*....|....*....|....*....
gi 1655220517 4294 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4322
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1604-2583 |
3.84e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1604 LEEAQVSRRKLEEEIHLIriqlqtTIKQKSTADD------ELQKLRDQAAEAEKVRKAAqeeaerlRKQVNEETQKKKNA 1677
Cdd:COG3096 245 LEAIRVTQSDRDLFKHLI------TEATNYVAADymrhanERRELSERALELRRELFGA-------RRQLAEEQYRLVEM 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1678 EDELKRKSEAEKEAARQKQKALDELQKHKM---QAEEAERR---LKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKT 1751
Cdd:COG3096 312 ARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIERYqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1752 TKL-------EESLKKEQGTVLQLQEEAEKLRKQE---EEANKAREQAEKELETWRLKANEALRLRLRAEeeaQRKSLAQ 1821
Cdd:COG3096 392 DSLksqladyQQALDVQQTRAIQYQQAVQALEKARalcGLPDLTPENAEDYLAAFRAKEQQATEEVLELE---QKLSVAD 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1822 EEAEkqkteaerdakkkakaeeaalkQKENAEKELEK-----QRTFAEQIAQQKLSaeqEYIRLKADFEHAEQQRGLLdN 1896
Cdd:COG3096 469 AARR----------------------QFEKAYELVCKiagevERSQAWQTARELLR---RYRSQQALAQRLQQLRAQL-A 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1897 ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKvsqsntekskqlletealkmkQLAEEAARLRSVAEEAK 1976
Cdd:COG3096 523 ELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEA---------------------QLEELEEQAAEAVEQRS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1977 KQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAyQRKLLEDQAAQHKHDIQEK 2056
Cdd:COG3096 582 ELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-EATVERDELAARKQALESQ 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2057 ITQLQSSSVSELDRQKNIVEetlRQKKVVEEEIhiirinFERASKEK-----------------SDLEVELKKLKGIADe 2119
Cdd:COG3096 660 IERLSQPGGAEDPRLLALAE---RLGGVLLSEI------YDDVTLEDapyfsalygparhaivvPDLSAVKEQLAGLED- 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2120 tqkSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAaeeeaaRQ-RKAAQDEVERLKQKAAEANKLKDKAEKElekqv 2198
Cdd:COG3096 730 ---CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSD------RQwRYSRFPEVPLFGRAAREKRLEELRAERD----- 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2199 ILAKEAAQksTAAEQKAQDVLSKNKEDLLSQEkLRDEFEnakklaqaaetakekaekeaallrqkaeeaeklkkaAEDEA 2278
Cdd:COG3096 796 ELAEQYAK--ASFDVQKLQRLHQAFSQFVGGH-LAVAFA------------------------------------PDPEA 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2279 AKQAKAQK--DAERlrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKA 2356
Cdd:COG3096 837 ELAALRQRrsELER---------------------ELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRL 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2357 lmdEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELlklkvR---IEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEA 2433
Cdd:COG3096 896 ---EELREELDAAQEAQAFIQQHGKALAQLEPLVAVL-----QsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRR 967
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2434 ARLSVEaeetarqrkTAEAELAEQRALAEKmLKEKM-QAIQEATKLKAEAEELQK---QKNQAQEKAKKLLEDKQEIQQR 2509
Cdd:COG3096 968 PHFSYE---------DAVGLLGENSDLNEK-LRARLeQAEEARREAREQLRQAQAqysQYNQVLASLKSSRDAKQQTLQE 1037
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2510 LDKETQ--GFQKSLEAE---RKRQLEISAEAEKLKLRVKELssaqakaEEEATRFKKQADEAKVRLQETEK---QTTETV 2581
Cdd:COG3096 1038 LEQELEelGVQADAEAEeraRIRRDELHEELSQNRSRRSQL-------EKQLTRCEAEMDSLQKRLRKAERdykQEREQV 1110
|
..
gi 1655220517 2582 VQ 2583
Cdd:COG3096 1111 VQ 1112
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2608-2753 |
4.14e-05 |
|
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: 48.82 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2608 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMlQQTFLTEKELLLKRERDVEDEKKKlqkhlEDEVNKAKALKDEQQR 2687
Cdd:pfam02841 155 EERDKLEAKYNQVPRKGVKAEEVLQEFLQSKEAV-EEAILQTDQALTAKEKAIEAERAK-----AEAAEAEQELLREKQK 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2688 QQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMeALEKKRLEQEKLLadeNKKLREKLESLE 2753
Cdd:pfam02841 229 EEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQER-MLEHKLQEQEELL---KEGFKTEAESLQ 290
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1624-2039 |
4.18e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.91 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1624 QLQTTIKQKSTADDELQKLRDQ----AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL 1699
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAggleAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1700 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQE 1779
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1780 EEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQ 1859
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1860 RTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKV 1939
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1940 SQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALK 2019
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
410 420
....*....|....*....|
gi 1655220517 2020 AKEAENERLKRQAEDEAYQR 2039
Cdd:COG5278 511 AAAEAALAAALAAALASAEL 530
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1650-1825 |
4.21e-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: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1650 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKV 1729
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1730 VEEVAQKTAA---TQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRl 1806
Cdd:pfam05262 260 LPKPADTSSPkedKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1655220517 1807 RLRAEEEAQRKSLAQEEAE 1825
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1809-2000 |
4.32e-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: 49.56 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1809 RAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEK-----ELEKQRTFAE-QIAQQKLSAEQE------ 1876
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKmreelELEQQRRFEEiRLRKQRLEEERQrqeeee 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1877 ---YIRLKADFEHAEQQRGLLDNELQRLknevnaaEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLlet 1953
Cdd:pfam15709 408 rkqRLQLQAAQERARQQQEEFRRKLQEL-------QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERL--- 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220517 1954 EALKMKQLAEEAARLrsvaeEAKKQRQLAEDEAARQRAEAEKILKEK 2000
Cdd:pfam15709 478 EYQRQKQEAEEKARL-----EAEERRQKEEEAARLALEEAMKQAQEQ 519
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1702-2481 |
4.55e-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: 50.22 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1702 LQKHKMQAEEAERRLKQA-EEEKVRQIKVVEEVAQ-KTAATQLQAMSFSEKTTK-LEESLKKEQGTvlQLQEEAEKLRKQ 1778
Cdd:pfam12128 218 LNRQQVEHWIRDIQAIAGiMKIRPEFTKLQQEFNTlESAELRLSHLHFGYKSDEtLIASRQEERQE--TSAELNQLLRTL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1779 EEEANKAREQAEKELETWRLKANEAlRLRLRAEEEaQRKSLAQEEAEKQKTEAERdakkkakaEEAALKQKENAEKELEK 1858
Cdd:pfam12128 296 DDQWKEKRDELNGELSAADAAVAKD-RSELEALED-QHGAFLDADIETAAADQEQ--------LPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1859 QRTfaeqiAQQKLSAEQEYIRLKADFEHAeqqRGLLDNElQRLKNEVNAAEKQRRQLEDELAKVRSEMDallqmkiqaEK 1938
Cdd:pfam12128 366 LTG-----KHQDVTAKYNRRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELR---------EQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1939 VSQSNTEKSKQLLETEAlkmkQLAEEAARLRSV--AEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV 2016
Cdd:pfam12128 428 LEAGKLEFNEEEYRLKS----RLGELKLRLNQAtaTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2017 ALKAKEAENERL-KRQAEDEAYQRKLleDQAAQHKHDIQEKITQLQSSSV-----SELDRQKNIVEETLRQKKVVEEEIH 2090
Cdd:pfam12128 504 ASEALRQASRRLeERQSALDELELQL--FPQAGTLLHFLRKEAPDWEQSIgkvisPELLHRTDLDPEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2091 IIRINFERAS-KEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAeeerkrreaeekvKKIAAAEEEAARQRKAA 2169
Cdd:pfam12128 582 GVKLDLKRIDvPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN-------------GELEKASREETFARTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2170 QDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKsTAAEQKAQDvlskNKEDLLSQEKLRDEFENAKKLAQAaeta 2249
Cdd:pfam12128 649 KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-LEAQLKQLD----KKHQAWLEEQKEQKREARTEKQAY---- 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2250 kekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeaeaakraaaeaaaLKQ-KQEADAEMAKHKKEAE 2328
Cdd:pfam12128 720 -----------WQVVEGALDAQLALLKAAIAARRSGAKAE--------------------LKAlETWYKRDLASLGVDPD 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2329 QALKQKSQVeKELgLVKLQLDETDKQKAL-MDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKlKVRIEEENLR 2406
Cdd:pfam12128 769 VIAKLKREI-RTL-ERKIERIAVRRQEVLrYFDWYQETWLQRRPRLAtQLSNIERAISELQQQLARLIA-DTKLRRAKLE 845
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2407 LMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEEtarqrKTAEAELAEQRALAEKmLKEKMQAIQEATKLKAE 2481
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS-----EQAQGSIGERLAQLED-LKLKRDYLSESVKKYVE 914
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-1679 |
4.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1286 EKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQRE 1365
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1366 LsllgrhmnsykqsyewliqwlreARLRQEKIEAApvwdsKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAyidslkd 1445
Cdd:TIGR02168 756 L-----------------------TELEAEIEELE-----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------- 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1446 yefQILAYRALQDpiasplkkpkmesasdniiqEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKE----- 1520
Cdd:TIGR02168 801 ---LREALDELRA--------------------ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdiesl 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1521 -----DEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLkNLSEQ 1595
Cdd:TIGR02168 858 aaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS----ELRRELEELREKLAQL-ELRLE 932
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1596 EIRSKNQQLEEAQVSRRKLEEEIHliriqlqttIKQKSTADDELQKLRDQAAEAEKVRKA-----------AQEEAER-- 1662
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEA---------EALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieeYEELKERyd 1003
|
410
....*....|....*...
gi 1655220517 1663 -LRKQVNEETQKKKNAED 1679
Cdd:TIGR02168 1004 fLTAQKEDLTEAKETLEE 1021
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2406-2580 |
4.95e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2406 RLMQKNKDNTQKLLAEEaeKMKSLAEEAARlsvEAEETARQRKT-AEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEE 2484
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEE--EAKRILEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2485 LQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKA------EEEATR 2558
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQK-------QQELEKKEEELEELIEEQLQELERISGLTAEEAKEillekvEEEARH 169
|
170 180
....*....|....*....|..
gi 1655220517 2559 fkkqadEAKVRLQETEKQTTET 2580
Cdd:PRK12704 170 ------EAAVLIKEIEEEAKEE 185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1524-1935 |
4.98e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1524 KRMAEIQAQLEtqkQLAEGHAKsvakAELEAQELKlKMKEDASQ--RQGLAV----DAEKQKQNIQLELTQLKNL----- 1592
Cdd:COG3096 785 KRLEELRAERD---ELAEQYAK----ASFDVQKLQ-RLHQAFSQfvGGHLAVafapDPEAELAALRQRRSELERElaqhr 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1593 -SEQEIRSKNQQLEEAQVSRRKLEEEIHLIriqlqttikqkstADDELQklrDQAAEAEKVRKAAQEeAERlrkqvneET 1671
Cdd:COG3096 857 aQEQQLRQQLDQLKEQLQLLNKLLPQANLL-------------ADETLA---DRLEELREELDAAQE-AQA-------FI 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1672 QKKKNAEDELKRKSEAekeaARQKQKALDELQKHKMQAEEAERRLKQaeeekvrQIKVVEEVAQKtaatqLQAMSFSEKT 1751
Cdd:COG3096 913 QQHGKALAQLEPLVAV----LQSDPEQFEQLQADYLQAKEQQRRLKQ-------QIFALSEVVQR-----RPHFSYEDAV 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1752 TKLEESlkkeqgtvlqlQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLR--LRAEEEAQRKSLAQEEAEKQK- 1828
Cdd:COG3096 977 GLLGEN-----------SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLasLKSSRDAKQQTLQELEQELEEl 1045
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1829 -----TEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAE---QIAQQKLS-AEQEY-----------------IRLKA 1882
Cdd:COG3096 1046 gvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEaemDSLQKRLRkAERDYkqereqvvqakagwcavLRLAR 1125
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1883 D-------------FEHAEQQRGLLDNELQRLKNEVNAAEKQR---RQLED------------------------ELAKV 1922
Cdd:COG3096 1126 DndverrlhrrelaYLSADELRSMSDKALGALRLAVADNEHLRdalRLSEDprrperkvqfyiavyqhlrerirqDIIRT 1205
|
490
....*....|...
gi 1655220517 1923 RSEMDALLQMKIQ 1935
Cdd:COG3096 1206 DDPVEAIEQMEIE 1218
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2440-2726 |
5.13e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2440 AEETARQRKTAEAELAEQRAlaekmlkekmqaiqEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQK 2519
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARF--------------EARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2520 SLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEE----EATRFKK---QADEAKVRLQETEKQTTETvvqkletqrlqS 2592
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEkqaaAAADPKKaavAAAIARAKAKKAAQQAANA-----------E 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2593 TREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhLE 2672
Cdd:PRK05035 571 AEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-VA 649
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2673 DEVNKAKALKDEQQRQQklmdeekkkLQAIMDEAVKKQKEAEAEMKNKQKEMEA 2726
Cdd:PRK05035 650 AAIARAKARKAAQQQAN---------AEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2470-2778 |
5.42e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2470 QAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEI---SAEAEKLKLRVKELS 2546
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2547 SAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKE 2626
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2627 TASAQQEQMEQQkamlqqtfltEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEA 2706
Cdd:COG4372 202 LAEAEKLIESLP----------RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2707 VKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2778
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2314-2467 |
5.59e-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: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2314 QEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK------ 2387
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2388 ---MQMDELLKLKVRIEEENLRLMQKnKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2464
Cdd:COG1579 93 alqKEIESLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
...
gi 1655220517 2465 LKE 2467
Cdd:COG1579 172 IPP 174
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1485-2041 |
5.65e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.80 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1485 TRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQ-LAEGHAKSVAKAELEA-QELKLKMK 1562
Cdd:PRK10246 297 ERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTwLAEHDRFRQWNNELAGwRAQFSQQT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1563 EDASQRQGLA--VDAEKQKQNIQLELTQlkNLSEQEIRSKNQQLEEAQVSRRKLeeeihlirIQLQTTIKQkstaddeLQ 1640
Cdd:PRK10246 377 SDREQLRQWQqqLTHAEQKLNALPAITL--TLTADEVAAALAQHAEQRPLRQRL--------VALHGQIVP-------QQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1641 KLRDQAAEAekvRKAAQEEaerlrkqvneetQKKKNAEDELKRKSEAEKEAARQKQKALDELqkhkmqaeeaERRLKQAE 1720
Cdd:PRK10246 440 KRLAQLQVA---IQNVTQE------------QTQRNAALNEMRQRYKEKTQQLADVKTICEQ----------EARIKDLE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1721 EEKVR----QIKVVEEVAQKTAATQLQAMSFSEKTTKLE------ESLKKEQGTVL-QLQEEAEKLRKQEEEANKAREQA 1789
Cdd:PRK10246 495 AQRAQlqagQPCPLCGSTSHPAVEAYQALEPGVNQSRLDalekevKKLGEEGAALRgQLDALTKQLQRDESEAQSLRQEE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1790 EKELETWRlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAeRDAKKKAKAEEAALKQKENAEKELEKQR-TFAEQIAQ 1868
Cdd:PRK10246 575 QALTQQWQ-AVCASLNITLQPQDDIQPWLDAQEEHERQLRLL-SQRHELQGQIAAHNQQIIQYQQQIEQRQqQLLTALAG 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1869 QKLS-----AEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQ--MKIQAEKVS- 1940
Cdd:PRK10246 653 YALTlpqedEEASWLATRQQEAQSWQQR---QNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDnwRQVHEQCLSl 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1941 --QSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKlaAINEATRLKTEAEVAL 2018
Cdd:PRK10246 730 hsQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLEN--QRQQAQTLVTQTAQAL 807
|
570 580
....*....|....*....|....
gi 1655220517 2019 KAKEAEN-ERLKRQAEDEAYQRKL 2041
Cdd:PRK10246 808 AQHQQHRpDGLDLTVTVEQIQQEL 831
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2416-2563 |
5.66e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.32 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEAARLSVEAEETARQ---RKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQA 2492
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKellLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2493 QEKAKKLLEDKQEIQQRLDKETQGFQK--SLEAERKRQ-----LEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQA 2563
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2503-2735 |
6.72e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2503 KQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLrvKELSSAQAKAEEEatrfKKQADEAKVRLQETEKQTTETVV 2582
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL--KQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2583 QKLETQRLqstrEADDLKKAIAELEK--EREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltekelllkrerdv 2660
Cdd:PRK09510 140 KAAAAAKA----KAEAEAKRAAAAAKkaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA-------------------- 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2661 edekkklqkhleDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQE 2735
Cdd:PRK09510 196 ------------AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2521-2754 |
7.06e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2521 LEAERKRQL-EISAEAEKLKlrvkelSSAQAKAEEEATRFKKQADEAKVRlQETEKQTTETVVQKLETQRlqstreaddl 2599
Cdd:COG2268 186 LDALGRRKIaEIIRDARIAE------AEAERETEIAIAQANREAEEAELE-QEREIETARIAEAEAELAK---------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2600 KKAIAELEKEREKLKRDAQelqnksketASAQQEQMEQQKAMLQQTFLTEKELLLKRERdvedEKKKLQKHLEDEVNKAK 2679
Cdd:COG2268 249 KKAEERREAETARAEAEAA---------YEIAEANAEREVQRQLEIAEREREIELQEKE----AEREEAELEADVRKPAE 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2680 ALKDEQQRQQKLmDEEKKKLQAIMdEAVKKQKEAEAEMKNKQkemEALEKKRLEQEKLLADENKKLREKLESLEV 2754
Cdd:COG2268 316 AEKQAAEAEAEA-EAEAIRAKGLA-EAEGKRALAEAWNKLGD---AAILLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1591-2046 |
7.31e-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: 49.19 E-value: 7.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1591 NLSEQEIRSKNQQLEEAQVSRRKLEEE----IHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQ 1666
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGEVetgiIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1667 VNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS 1746
Cdd:COG5185 210 SETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1747 FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEAlrlrlraeeeaqrKSLAQEEAEK 1826
Cdd:COG5185 290 QFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIE-------------QGQESLTENL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 QKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR-LKADFEHAEQQRGLLDNELQRLKNEV 1905
Cdd:COG5185 357 EAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAtLEDTLKAADRQIEELQRQIEQATSSN 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1906 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKqlLETEALKMKQLAEEAARLRSVAEE--AKKQRQL-- 1981
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSK--KEDLNEELTQIESRVSTLKATLEKlrAKLERQLeg 514
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1982 ---AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAK---EAENERLKRQAEDEAYQRKLLEDQA 2046
Cdd:COG5185 515 vrsKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKtdgQAANLRTAVIDELTQYLSTIESQQA 585
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1575-1744 |
7.44e-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: 48.30 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1575 AEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRK 1654
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1655 AAQE-----EAERLRKQvNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhkmqAEEAERrlKQAEEEKVRQIKV 1729
Cdd:TIGR02794 128 QAAEakakaEAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEA--KAKAEEAKAKAEA 200
|
170
....*....|....*
gi 1655220517 1730 VEEVAQKTAATQLQA 1744
Cdd:TIGR02794 201 AKAKAAAEAAAKAEA 215
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3622-3659 |
7.45e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 7.45e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 3622 LPLLEAQFATGGIIDPVSSHRVPNDVAIQRGYLSKQMV 3659
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
202-310 |
7.77e-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: 45.82 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 268
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655220517 269 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 310
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1676-1997 |
8.23e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1676 NAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLkQAEEEKVRQIKV---------VEEVAQKTAATQlQAMS 1746
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL-SALNRLLPRLNLladetladrVEEIREQLDEAE-EAKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1747 FSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKeletwrlkanealRLRLRAEEEAQRKSLAQEEAEK 1826
Cdd:PRK04863 912 FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQ-------------QAFALTEVVQRRAHFSYEDAAE 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1827 QKTEAerdakkkAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQ------- 1899
Cdd:PRK04863 979 MLAKN-------SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpad 1051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1900 ------------RLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmkiQAEKVsqsnTEKSKQLLE--TEALKMKQLAEEA 1965
Cdd:PRK04863 1052 sgaeerararrdELHARLSANRSRRNQLEKQLTFCEAEMDNLTK---KLRKL----ERDYHEMREqvVNAKAGWCAVLRL 1124
|
330 340 350
....*....|....*....|....*....|..
gi 1655220517 1966 ARLRSVaEEAKKQRQLAEDEAARQRAEAEKIL 1997
Cdd:PRK04863 1125 VKDNGV-ERRLHRRELAYLSADELRSMSDKAL 1155
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1586-1831 |
8.33e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1586 LTQLKNLSEQEIRSKNQQLEEAQVsRRKLEEEIHLIRI--QLQTTIKQKSTADDELQKLRDQaaEAEKVRKAAQEEAERL 1663
Cdd:PRK05771 22 LEALHELGVVHIEDLKEELSNERL-RKLRSLLTKLSEAldKLRSYLPKLNPLREEKKKVSVK--SLEELIKDVEEELEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1664 RKQVNEETQKKKNAEDELKRKsEAEKEAArQKQKALD-ELQK--------------HKMQAEEAERRLKQAEEEKVRQIK 1728
Cdd:PRK05771 99 EKEIKELEEEISELENEIKEL-EQEIERL-EPWGNFDlDLSLllgfkyvsvfvgtvPEDKLEELKLESDVENVEYISTDK 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1729 -------VVEEVAQKTAATQLQAMSFSEKTTKLEESLKkeqgtvlqlqEEAEKLRKQEEEANKAREQAEKELETWrlkAN 1801
Cdd:PRK05771 177 gyvyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPS----------ELIREIKEELEEIEKERESLLEELKEL---AK 243
|
250 260 270
....*....|....*....|....*....|
gi 1655220517 1802 EALRLRLRAEEEAqrkslaqeEAEKQKTEA 1831
Cdd:PRK05771 244 KYLEELLALYEYL--------EIELERAEA 265
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1404-1704 |
8.48e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.14 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1404 DSKALKEQLTQEKKLLEEIEKNKDQIENCQK----------DAKAYIDSLKDYE-------FQILAYRALQDPIASPLKK 1466
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQqlaqapaklrQAQAELEALKDDNdeetretLSTLSLRQLESRLAQTLDQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1467 pkMESASDNIIQ---EYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRM-AE---IQAQLETQKQL 1539
Cdd:PRK11281 137 --LQNAQNDLAEynsQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLqAEqalLNAQNDLQRKS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1540 AEGH--------------AKSVAKAELEAQEL-------KLKMKE----------DASQRQGLAVDAEKQKQNIQL---- 1584
Cdd:PRK11281 215 LEGNtqlqdllqkqrdylTARIQRLEHQLQLLqeainskRLTLSEktvqeaqsqdEAARIQANPLVAQELEINLQLsqrl 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1585 -ELTQLKN-LSEQEIRSKNQqLEEAQVSRRKLEEEIH-------LIRIQLQTtiKQKSTADDELQKLRDQAAEaekvrka 1655
Cdd:PRK11281 295 lKATEKLNtLTQQNLRVKNW-LDRLTQSERNIKEQISvlkgsllLSRILYQQ--QQALPSADLIEGLADRIAD------- 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 aqeeaerLRKQVNEETQKKknaeDELKRKSE-AEKEAARQKQKALDELQK 1704
Cdd:PRK11281 365 -------LRLEQFEINQQR----DALFQPDAyIDKLEAGHKSEVTDEVRD 403
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1389-1828 |
8.99e-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: 48.87 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1389 EARLRQEKIEAAPVWDSKALKEqLTQEKKLLEEIEKNKDQIENCQKDAKayidslKDYEFQILAYRALQDPIA---SPLK 1465
Cdd:pfam05701 50 EIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEELKLNLERAQTEEAQAK------QDSELAKLRVEEMEQGIAdeaSVAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1466 KPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDEKkRMAEIQAQLETQKQL------ 1539
Cdd:pfam05701 123 KAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEK-TVEELTIELIATKESlesaha 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1540 ----AEGHAKSVA---------------KAELEAQELK--------LKMKEDASQRQGLAVDAE---------KQKQNIQ 1583
Cdd:pfam05701 202 ahleAEEHRIGAAlareqdklnwekelkQAEEELQRLNqqllsakdLKSKLETASALLLDLKAElaaymesklKEEADGE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1584 LELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRI---QLQ----------TTIKQKSTA--------DDELQKL 1642
Cdd:pfam05701 282 GNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVaaaSLRselekekaelASLRQREGMasiavsslEAELNRT 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1643 RDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaedelkrksEAEkEAARQKQKALDELQKHKMQAEEAERRLKQAE-- 1720
Cdd:pfam05701 362 KSEIALVQAKEKEAREKMVELPKQLQQAAQ-------------EAE-EAKSLAQAAREELRKAKEEAEQAKAAASTVEsr 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1721 -EEKVRQIKVVEEvAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKAREQAEKELETW 1796
Cdd:pfam05701 428 lEAVLKEIEAAKA-SEKLALAAIKALQESESSAESTNQEDSPRGVTLSLEEYYElskRAHEAEELANKRVAEAVSQIEEA 506
|
490 500 510
....*....|....*....|....*....|....*.
gi 1655220517 1797 RLKANEAL-RLRLRAEEEAQRKS---LAQEEAEKQK 1828
Cdd:pfam05701 507 KESELRSLeKLEEVNREMEERKEalkIALEKAEKAK 542
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1512-1750 |
9.26e-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: 48.30 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1512 EKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksvaKAELEAQELKLKMKEDASQrqglavdAEKQKQNIQLEltqlkn 1591
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAE-------QARQKELEQRAAAEKAAKQ-------AEQAAKQAEEK------ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1592 lSEQEIRSKNQQLEEAqvsrrkleeeihliriqlqttiKQKSTADDELQKLRDQAAEAEKVRKA-----AQEEAERLRKQ 1666
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEA----------------------KAKAEAEAERKAKEEAAKQAEEEAKAkaaaeAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1667 VNEETQKKKNAE-----DELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQ 1741
Cdd:TIGR02794 175 AEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
....*....
gi 1655220517 1742 LQAMSFSEK 1750
Cdd:TIGR02794 255 AAAGSEVDK 263
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1544-2021 |
9.39e-05 |
|
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: 48.60 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1544 AKSVAKAELEAQELKLKMKEDASQRQGLAVdaekqkQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHL-IR 1622
Cdd:pfam09731 43 GEEVVLYALGEDPPLAPKPKTFRPLQPSVV------SAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAeAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1623 IQLQTTIKQKSTADDELQKlrDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDEL 1702
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLK--EAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1703 QKHKM-------------QAEEAERRLKQAEEEKVRQIKVVEEVAQKTA-ATQLQAMSFSEKTTKLEESLKKEQGTVLQL 1768
Cdd:pfam09731 195 LKEVInlakqseeeaappLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKlVDQYKELVASERIVFQQELVSIFPDIIPVL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1769 QE----EAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKslaQEEAEKQKTEAERDAkkkakaeea 1844
Cdd:pfam09731 275 KEdnllSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDK---LAEELSARLEEVRAA--------- 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1845 alkQKENAEKELEKQRTFAEQIAQQKLSAEQeyirlkadfehaEQQRGLLDnelQRLKNEV--NAAEKQRRQLEDELAKV 1922
Cdd:pfam09731 343 ---DEAQLRLEFEREREEIRESYEEKLRTEL------------ERQAEAHE---EHLKDVLveQEIELQREFLQDIKEKV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1923 RSE-------MDALLQMKIQAEKVSQSNTEkskqlLETEALKMKQLAEEAARLRSVAEEAKKQRQLA----EDEAARQRA 1991
Cdd:pfam09731 405 EEEragrllkLNELLANLKGLEKATSSHSE-----VEDENRKAQQLWLAVEALRSTLEDGSADSRPRplvrELKALKELA 479
|
490 500 510
....*....|....*....|....*....|.
gi 1655220517 1992 EAEKILKEKLAAINEATRLK-TEAEVALKAK 2021
Cdd:pfam09731 480 SDDEVVKAALASLPEEAYQRgVYTEAALRER 510
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2318-2763 |
9.46e-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: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2318 AEMAKHKKEAEQALKQKSQVEKEL----GLV---KLQLD--ETDKQKALMDEELQRVKAQ-------VNDAVKQKAQVEN 2381
Cdd:pfam05701 49 EEIPEYKKQSEAAEAAKAQVLEELestkRLIeelKLNLEraQTEEAQAKQDSELAKLRVEemeqgiaDEASVAAKAQLEV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2382 ELSKVKMQMDELLKLKvrieeENLRLMQKNKDntqkLLAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALA 2461
Cdd:pfam05701 129 AKARHAAAVAELKSVK-----EELESLRKEYA----SLVSERDIAIKRAEEAVSASKEIEKTVEE---LTIELIATKESL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2462 EKM----LKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLledKQEIQQRLDKETQgfqksLEAERKRQLEISAE-AE 2536
Cdd:pfam05701 197 ESAhaahLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRL---NQQLLSAKDLKSK-----LETASALLLDLKAElAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2537 KLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQET----EKQTTETVVQKLETQRLQStreaddlkkaiaELEKEREK 2612
Cdd:pfam05701 269 YMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVkaniEKAKDEVNCLRVAAASLRS------------ELEKEKAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2613 LKrDAQELQNKSKETASAQQEQMEQQKamlqqtflTEKELLLKRERDVEDEKKKLQKHLED---EVNKAKALKDEQQrqq 2689
Cdd:pfam05701 337 LA-SLRQREGMASIAVSSLEAELNRTK--------SEIALVQAKEKEAREKMVELPKQLQQaaqEAEEAKSLAQAAR--- 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2690 klmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEkkrlEQEKLLADENKKLREKLESLEVTSKQAASKT 2763
Cdd:pfam05701 405 ----EELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAK----ASEKLALAAIKALQESESSAESTNQEDSPRG 470
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1499-1691 |
9.47e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1499 KFILETQrrLEDDEKASEKLKEDEKKRMaeiqaqlETQKQlaeghaksvaKAELEAQELKLKMKEdasqrqglavDAEKQ 1578
Cdd:PRK12704 26 KKIAEAK--IKEAEEEAKRILEEAKKEA-------EAIKK----------EALLEAKEEIHKLRN----------EFEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1579 KQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKlrdQAAEAEKVRKAAQE 1658
Cdd:PRK12704 77 LRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERISGLTAE 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220517 1659 EA-ERLRKQVNEETQKKKNA---EDELKRKSEAEKEA 1691
Cdd:PRK12704 154 EAkEILLEKVEEEARHEAAVlikEIEEEAKEEADKKA 190
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2473-2645 |
9.54e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.10 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2473 QEATKLKAEAEELQKQ-KNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKR-QLEISAEAEKLKLRVKELssaqa 2550
Cdd:pfam01442 4 DSLDELSTYAEELQEQlGPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEElQAKLGQNVEELRQRLEPY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2551 kAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAE-LEKEREKLKRDAQELQNKSKETAS 2629
Cdd:pfam01442 79 -TEELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARLAPYAEELRQKLAErLEELKESLAPYAEEVQAQLSQRLQ 157
|
170
....*....|....*.
gi 1655220517 2630 AQQEQMEQQKAMLQQT 2645
Cdd:pfam01442 158 ELREKLEPQAEDLREK 173
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1621-1760 |
9.87e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1621 IRIQLQTTIKQKSTADDELQKLRDQAAEAEK-VRKAAQEEAERLRKQVneetQKKKNAEDELKRKSEAEKEAARQKQKAL 1699
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELRDEL----AELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1700 DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEE----------VAQKTA--ATQLQAmSFSEKTTKLEESLKK 1760
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteediaevVSRWTGipVGKLLE-GEREKLLNLEEELHE 549
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1926-2242 |
9.92e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.58 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1926 MDALLQMKIQAEKVSQSNTEKSKQLLETEalKMKQLAEEAARlrsvaeEAKKQRQLAEDEAARQRAeaekiLKEKLAAIN 2005
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2006 EATRLKTEAE-----VALKAKEAENERLKRQ--AEDEAYQRKL--LEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVE 2076
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEeiAMEISRMRELerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2077 ETLRQKKVVEEEIHIIRINFERASKEKsdlevelkklkgiADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIA 2156
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEER-------------AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2157 AAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELE-KQVILAKEAAQKSTAAEQKAQDVLSKNKEdllSQEKLRDE 2235
Cdd:pfam17380 485 DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEeRQKAIYEEERRREAEEERRKQQEMEERRR---IQEQMRKA 561
|
....*..
gi 1655220517 2236 FENAKKL 2242
Cdd:pfam17380 562 TEERSRL 568
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1630-1937 |
1.02e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1630 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQA 1709
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1710 EEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1789
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1790 EKELetwRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1869
Cdd:COG4372 191 EANR---NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1870 KLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAE 1937
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2594-2769 |
1.09e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 47.64 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2594 READDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqtfltekellLKRERDvedekkklqkHLED 2673
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQ----------LQKEKD----------QLQS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2674 EVNKAKALKD-------EQQRQQKLMDEEKKKLqaiMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLR 2746
Cdd:pfam09728 61 ELSKAILAKSkleklcrELQKQNKKLKEESKKL---AKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELR 137
|
170 180
....*....|....*....|....*....
gi 1655220517 2747 EKLESL----EVTSKQAAS--KTKEIEVQ 2769
Cdd:pfam09728 138 EKLKSLieqyELRELHFEKllKTKELEVQ 166
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1547-1791 |
1.09e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1547 VAKAELEAQELKLKMKEDASQR--------------------QGLAVDAEKQKQNIQ--LELTQLKNLSEQEIRSKNQQL 1604
Cdd:PRK05035 433 QAKAEIRAIEQEKKKAEEAKARfearqarlerekaarearhkKAAEARAAKDKDAVAaaLARVKAKKAAATQPIVIKAGA 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1605 EEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLrdQAAEAE-KVRKAAQEEAErlRKQVNEETQKKKNAEDEL-- 1681
Cdd:PRK05035 513 RPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAV--AAAIARaKAKKAAQQAAN--AEAEEEVDPKKAAVAAAIar 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1682 -KRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAAtqLQAMSFSEKTTkleeslKK 1760
Cdd:PRK05035 589 aKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA--VAAAIARAKAR------KA 660
|
250 260 270
....*....|....*....|....*....|.
gi 1655220517 1761 EQGTVLQLQEEAEKLRKQEEEANKAREQAEK 1791
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1770-1991 |
1.15e-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: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1770 EEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK 1849
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLE----QQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1850 ENAEKELEKQR-TFAEQIAQQKLSAEQEYIRLKADFEHAEQQRgllDNELQRLKNEVNAAEKQRRQLEDELAKVRSEmda 1928
Cdd:TIGR02794 126 AKQAAEAKAKAeAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1929 llQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRA 1991
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2416-2777 |
1.16e-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: 48.60 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEaaRLSVEAEETarqRKTAEAELAEQRALAEKMLKEKMQAIQEAtklkaeAEELQKQKNQAQEK 2495
Cdd:pfam09731 79 SKEPKEEKKQVKIPRQS--GVSSEVAEE---EKEATKDAAEAKAQLPKSEQEKEKALEEV------LKEAISKAESATAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2496 AKKLLEDKQE-IQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQAdeakvrLQETE 2574
Cdd:pfam09731 148 AKEAKDDAIQaVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDA------APETP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2575 KQTTETvvqklETQRLQSTREADDLKKAIAELEKEREKLKRD-AQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL 2653
Cdd:pfam09731 222 PKLPEH-----LDNVEEKVEKAQSLAKLVDQYKELVASERIVfQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREI 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2654 LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdeaVKKQKEAEAEMKNKQKEMEalEKKRLE 2733
Cdd:pfam09731 297 DQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADE-----AQLRLEFEREREEIRESYE--EKLRTE 369
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220517 2734 QEKLLADENKKLREKLESLEVTSKQAAskTKEIEvqtDKVPEEQ 2777
Cdd:pfam09731 370 LERQAEAHEEHLKDVLVEQEIELQREF--LQDIK---EKVEEER 408
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
208-298 |
1.20e-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: 44.60 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 208 KWVNKHLMKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 280
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1655220517 281 DDIADGNPKLTLGLIWTI 298
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2473-2765 |
1.22e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2473 QEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLdketqgfqKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKA 2552
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL--------KELAEKRD---ELNAQVKELREEAQELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2553 EEEATRFKKQADEAKVRLQETEKQTTEtvVQKLETQRLQSTREADDLKKAIAELEK--EREKLKRDAQ-ELQNKSKETAs 2629
Cdd:COG1340 70 NEKVKELKEERDELNEKLNELREELDE--LRKELAELNKAGGSIDKLRKEIERLEWrqQTEVLSPEEEkELVEKIKELE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2630 aqqEQMEQQKAMLQQtfltEKELllkreRDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAvkk 2709
Cdd:COG1340 147 ---KELEKAKKALEK----NEKL-----KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEA--- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2710 qKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKE 2765
Cdd:COG1340 212 -DELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2422-2636 |
1.22e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2422 EAEKMKSLAE---EAARLSVEAE-ETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKnQAQEKAK 2497
Cdd:COG2268 187 DALGRRKIAEiirDARIAEAEAErETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAE-TARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRldketqgfqksleaERKRQLEIsAEAEKlKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQt 2577
Cdd:COG2268 266 AAYEIAEANAER--------------EVQRQLEI-AERER-EIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE- 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2578 tetvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAqeLQNKSKETASAQQEQME 2636
Cdd:COG2268 329 -------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM--LIEKLPEIAEAAAKPLE 378
|
|
| valS |
PRK14900 |
valyl-tRNA synthetase; Provisional |
1639-1833 |
1.29e-04 |
|
valyl-tRNA synthetase; Provisional
Pssm-ID: 237855 [Multi-domain] Cd Length: 1052 Bit Score: 48.45 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1639 LQKLRDQAAEAEKVRK----AAQEEAERLRKQVNEETQKKknAEDELKRKSEAEKEAARQKqkaldelqKHKMQAEEAer 1714
Cdd:PRK14900 834 LAGVIDLAAETARVDKeigkVDQDLAVLERKLQNPSFVQN--APPAVVEKDRARAEELREK--------RGKLEAHRA-- 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1715 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEA--------EKLRKQEEEANK-- 1784
Cdd:PRK14900 902 MLSGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAatavasgiEKVAEAVRKTVRrs 981
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655220517 1785 AREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKqKTEAER 1833
Cdd:PRK14900 982 VKKAAATRAAMKKKVAKKAPAKKAAAKKAAAKKAAAKKKVAK-KAPAKK 1029
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2393-2567 |
1.32e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2393 LLKLKVRIEEENLRLmQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQrKTAEAELAEQRALAEKMLKEKMQAI 2472
Cdd:PRK00409 525 LEELERELEQKAEEA-EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ-AIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2473 QEATKlkaEAEELQKQKNQAQEKAKKLLEDKQEIQQRLD-----KETQGFQKS--LEAERKRQLEISAEAEKLKLRVKEL 2545
Cdd:PRK00409 603 SVKAH---ELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevKYLSLGQKGevLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
170 180
....*....|....*....|..
gi 1655220517 2546 SSAQAKAEEEATRFKKQADEAK 2567
Cdd:PRK00409 680 EKIQKPKKKKKKKPKTVKPKPR 701
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1417-2794 |
1.34e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1417 KLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQILAYRALQDPiasplkkpkmESASDNIIQEyvTLRTRYSElstlTSQ 1496
Cdd:TIGR01612 755 KILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYND----------QINIDNIKDE--DAKQNYDK----SKE 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1497 YIKFIletqrRLEDDEkaSEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQ------- 1569
Cdd:TIGR01612 819 YIKTI-----SIKEDE--IFKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKlndyekk 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1570 ---------GLAVDAEKQKQNIQ--------LELTQLKNLSEQEIRSKNQQLEEaqvsrrKLEEEIHLIRiqlQTTIKQK 1632
Cdd:TIGR01612 892 fndskslinEINKSIEEEYQNINtlkkvdeyIKICENTKESIEKFHNKQNILKE------ILNKNIDTIK---ESNLIEK 962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1633 STADDELQKLRDQAAEAEKVRKAAQEEAERLRKqvNEETQKKKNAEDEL-KRKSEAEKEAARQKQKALDELQKhkmQAEE 1711
Cdd:TIGR01612 963 SYKDKFDNTLIDKINELDKAFKDASLNDYEAKN--NELIKYFNDLKANLgKNKENMLYHQFDEKEKATNDIEQ---KIED 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1712 AERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSfsekttklEESLKKEQGTVLQLQEEAEKLR-------------KQ 1778
Cdd:TIGR01612 1038 ANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--------KEILEEAEINITNFNEIKEKLKhynfddfgkeeniKY 1109
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1779 EEEANKAREQAEkeletwrlKANEALRLRLRAEEEAQRKSlaqeeaekqkteaerdakkkakaeeaalkqkENAEKELEK 1858
Cdd:TIGR01612 1110 ADEINKIKDDIK--------NLDQKIDHHIKALEEIKKKS-------------------------------ENYIDEIKA 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1859 QRTFAEQIAQQKLSAE--------QEYIRLKADfehaeqQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRS------ 1924
Cdd:TIGR01612 1151 QINDLEDVADKAISNDdpeeiekkIENIVTKID------KKKNIYDEIKKLLNEIAEIEKDKTSLE----EVKGinlsyg 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 -EMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRaeaekilKEKLAA 2003
Cdd:TIGR01612 1221 kNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDK-------DHHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2004 INEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQaaQHKHDIQEKITQLQS-SSVSELDRQKNIVEETLRQK 2082
Cdd:TIGR01612 1294 KKHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQ--KHNSDINLYLNEIANiYNILKLNKIKKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2083 KVVEEEIHIIRINFERAS------KEKSDLE---------VELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRRE 2147
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSEklikkiKDDINLEeckskiestLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNEN 1451
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2148 AEEKVKKIAAAEEEAARQRKAAQD--------EVERLKQKAAEANKLKDKAE---KELEKQVILAKEAAQKSTAAEQKAQ 2216
Cdd:TIGR01612 1452 VLLLFKNIEMADNKSQHILKIKKDnatndhdfNINELKEHIDKSKGCKDEADknaKAIEKNKELFEQYKKDVTELLNKYS 1531
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2217 DVLSKNKEDLLSQ--EKLRDEFENAKKLAQAAETAKekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLrke 2294
Cdd:TIGR01612 1532 ALAIKNKFAKTKKdsEIIIKEIKDAHKKFILEAEKS----------EQKIKEIKKEKFRIEDDAAKNDKSNKAAIDI--- 1598
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2295 aeaeaakraaaeAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDET------DKQKALMD--EELQRVK 2366
Cdd:TIGR01612 1599 ------------QLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTelkengDNLNSLQEflESLKDQK 1666
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2367 AQVNDAVKQKAQVENELSKVKMQMDELLK-LKVRIEEENLRLMQKNK---DNTQKLLAEEAEKMKSLAEEAARLSVEAEE 2442
Cdd:TIGR01612 1667 KNIEDKKKELDELDSEIEKIEIDVDQHKKnYEIGIIEKIKEIAIANKeeiESIKELIEPTIENLISSFNTNDLEGIDPNE 1746
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2443 TARQRKTAEAELAEQ--------RALAEKMLKEKMQAIQ-EATKLKAEAEELqkqKN-QAQEKAKKLLEDKQ-------- 2504
Cdd:TIGR01612 1747 KLEEYNTEIGDIYEEfielyniiAGCLETVSKEPITYDEiKNTRINAQNEFL---KIiEIEKKSKSYLDDIEakefdrii 1823
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2505 -EIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELS---------------------SAQAKAEEEATRFKKQ 2562
Cdd:TIGR01612 1824 nHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKL 1903
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2563 ADEAKVRLQETE-----KQTTETVVQKLETqrlqstrEADDLKKAIAELEKERE---KLKRDAQELQNKSKETASAQQEQ 2634
Cdd:TIGR01612 1904 ANSINIQIQNNSgidlfDNINIAILSSLDS-------EKEDTLKFIPSPEKEPEiytKIRDSYDTLLDIFKKSQDLHKKE 1976
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2635 MEQQKAMLQQTFLTEK------------ELLLKRERDVEDekKKLQKHLEDEVNKAKA----------LKDEQQRQQKLM 2692
Cdd:TIGR01612 1977 QDTLNIIFENQQLYEKiqasnelkdtlsDLKYKKEKILND--VKLLLHKFDELNKLSCdsqnydtileLSKQDKIKEKID 2054
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2693 DEEKKKLQAIMDEAVKKQKEaeaEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDK 2772
Cdd:TIGR01612 2055 NYEKEKEKFGIDFDVKAMEE---KFDNDIKDIEKFENNYKHSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDK 2131
|
1530 1540 1550
....*....|....*....|....*....|....*...
gi 1655220517 2773 VPEE-----QLVSM----------TTVETTK-KVFNGS 2794
Cdd:TIGR01612 2132 IIEKndlidKLIEMrkecllfsyaTLVETLKsKVINHS 2169
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2560-2765 |
1.35e-04 |
|
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: 48.09 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2560 KKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLK-KAIAELEKEREKLKrdaQELQNKSKETASAQQEQMEQQ 2638
Cdd:NF033838 57 KEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKtEYLYELNVLKEKSE---AELTSKTKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2639 KAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALK-DEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEM 2717
Cdd:NF033838 134 TLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKV 213
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2718 KNKQKEMEALEKKRLEQEKllADENKKLREKLESLEVTSKQAASKTKE 2765
Cdd:NF033838 214 ESKKAEATRLEKIKTDREK--AEEEAKRRADAKLKEAVEKNVATSEQD 259
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2265-2417 |
1.39e-04 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.21 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2265 EEAEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAAL-KQKQEADAEMAKHKKEAEQA---LKQKSQVEKE 2340
Cdd:COG1193 521 EELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILeKAREEAEEILREARKEAEELireLREAQAEEEE 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2341 LGLVKLQLDETDKQkalMDEELQRVKA-----------QVNDAVK-----QKAQVENELSK--VKMQMDEllkLKVRIEE 2402
Cdd:COG1193 601 LKEARKKLEELKQE---LEEKLEKPKKkakpakppeelKVGDRVRvlslgQKGEVLEIPKGgeAEVQVGI---LKMTVKL 674
|
170
....*....|....*
gi 1655220517 2403 ENLRLMQKNKDNTQK 2417
Cdd:COG1193 675 SDLEKVEKKKPKKPK 689
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1661-1856 |
1.43e-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: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNEETQKKKNAEDELKRKSEaekEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEvaqktaat 1740
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQ---EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-------- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1741 QLQAMSFSEKTTKLEESLKKEQgtvlqLQEEaeklrkQEEEANKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLA 1820
Cdd:pfam05262 253 KQQEAKNLPKPADTSSPKEDKQ-----VAEN------QKREIEKAQIEIKK-------NDEEALKAKDHKAFDLKQESKA 314
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655220517 1821 QEEAEKQKT-EAERDAKKKAKAEEAALKQKENAEKEL 1856
Cdd:pfam05262 315 SEKEAEDKElEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1562-1804 |
1.51e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 47.92 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1562 KEDASQRqgLAVDAEKqkqnIQLELTQLKNLsEQEIRSKNQQLEEAQVSRR----KLEEEIHLIRIQLQTTIKQKstadd 1637
Cdd:pfam09726 393 KPDALVR--LEQDIKK----LKAELQASRQT-EQELRSQISSLTSLERSLKselgQLRQENDLLQTKLHNAVSAK----- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1638 elQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETqkkknaedelKRKSEAEKEAARQKQKALD------ELQKHKMQAEE 1711
Cdd:pfam09726 461 --QKDKQTVQQLEKRLKAEQEARASAEKQLAEEK----------KRKKEEEATAARAVALAAAsrgectESLKQRKRELE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1712 AERRLKQAE----EEKVRQIKV-VEEVAQ--------KTAATQLQAMsfSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQ 1778
Cdd:pfam09726 529 SEIKKLTHDiklkEEQIRELEIkVQELRKykesekdtEVLMSALSAM--QDKNQHLENSLSAETRIKLDLFSALGDAKRQ 606
|
250 260
....*....|....*....|....*.
gi 1655220517 1779 EEEANKAREQAEKELETWRLKANEAL 1804
Cdd:pfam09726 607 LEIAQGQIYQKDQEIKDLKQKIAEVM 632
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1750-1910 |
1.58e-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: 47.69 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1750 KTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEeeAQRKSLAQEEAEKQKT 1829
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1830 EAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKlsaeqeyirlkadfeHAEQQRGLLD--NELQRLKNEVNA 1907
Cdd:pfam05262 282 EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEA 346
|
...
gi 1655220517 1908 AEK 1910
Cdd:pfam05262 347 QPT 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1576-1711 |
1.70e-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: 46.46 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLELTQLKNL---SEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADD---------ELQKLR 1643
Cdd:COG1579 23 EHRLKELPAELAELEDElaaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkeyealqkEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1644 DQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1711
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1882-2730 |
1.71e-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: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1882 ADF-EHAEQQRGLLDNELQrLKNEVNAAEKQRRQLEDELAKVRSEMDALlqmkiqaekvsqsntEKSKQLLETE---ALK 1957
Cdd:COG3096 271 ADYmRHANERRELSERALE-LRRELFGARRQLAEEQYRLVEMARELEEL---------------SARESDLEQDyqaASD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1958 MKQLAEEAARlrsvAEEAKKQRQLAEDEAARQRAEAEKILKEklaaineATRLKTEAEVALKAKEAENERLKRQAEDeaY 2037
Cdd:COG3096 335 HLNLVQTALR----QQEKIERYQEDLEELTERLEEQEEVVEE-------AAEQLAEAEARLEAAEEEVDSLKSQLAD--Y 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2038 QRKLLEDQ--AAQHKHDIQ--EKITQLqsSSVSELDrQKNIvEETLRQKKVVEEEIHIIRINFER----ASKEKSDLEVE 2109
Cdd:COG3096 402 QQALDVQQtrAIQYQQAVQalEKARAL--CGLPDLT-PENA-EDYLAAFRAKEQQATEEVLELEQklsvADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2110 LKKLKGIADETQKSKAKAEEEAEKLKKlaaeeerkrreaeekvkkiaaaeeeaaRQRKAAQDEVERLKQKAAEANKLKDK 2189
Cdd:COG3096 478 YELVCKIAGEVERSQAWQTARELLRRY---------------------------RSQQALAQRLQQLRAQLAELEQRLRQ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2190 AEKELEKQVILAKEAAQKSTAAEQKaqdvlsknkEDLLS-QEKLRDEFENAKKLAQAAETAkekaekeaalLRQKAEEAE 2268
Cdd:COG3096 531 QQNAERLLEEFCQRIGQQLDAAEEL---------EELLAeLEAQLEELEEQAAEAVEQRSE----------LRQQLEQLR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2269 KLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakrAAAEAAALKQKQEADAEMAkhkkEAEQALKQKSQVEKELGLVKLQL 2348
Cdd:COG3096 592 ARIKELAARAPAWLAAQDALERL-----------REQSGEALADSQEVTAAMQ----QLLEREREATVERDELAARKQAL 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2349 DETDKQKAL----MDEELQRVKAQ--------------VNDAV--------KQKAQVENELSKVKMQMDEL--------- 2393
Cdd:COG3096 657 ESQIERLSQpggaEDPRLLALAERlggvllseiyddvtLEDAPyfsalygpARHAIVVPDLSAVKEQLAGLedcpedlyl 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2394 -------------------LKLKVRIEEENLR---------LMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETAR 2445
Cdd:COG3096 737 iegdpdsfddsvfdaeeleDAVVVKLSDRQWRysrfpevplFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQR 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2446 QRKTAEAELAEQRALA-----EKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK-------------LLEDkQEIQ 2507
Cdd:COG3096 814 LHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanLLAD-ETLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2508 QRLDKETQGFQKSLEAERkrqlEISAEAEKLKLRVKELSSAQAKAEEEAtRFKKQADEAKVRLQETEKQT--TETVVQKL 2585
Cdd:COG3096 893 DRLEELREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFE-QLQADYLQAKEQQRRLKQQIfaLSEVVQRR 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2586 ETqrlQSTREADDLKKAIAEL-EKEREKLkRDAQELQNKSKETASAQQEQMEQQKAMLQQ---TFLTEKELLlkreRDVE 2661
Cdd:COG3096 968 PH---FSYEDAVGLLGENSDLnEKLRARL-EQAEEARREAREQLRQAQAQYSQYNQVLASlksSRDAKQQTL----QELE 1039
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2662 DEKKKLQKHLEDE-VNKAKALKDE------QQRQQKlmDEEKKKLQAImdeavkkqkeaEAEMKNKQKEMEALEKK 2730
Cdd:COG3096 1040 QELEELGVQADAEaEERARIRRDElheelsQNRSRR--SQLEKQLTRC-----------EAEMDSLQKRLRKAERD 1102
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1767-1997 |
1.76e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1767 QLQEEAEKLRKQEEEANKAREQAEKELETwrlKANEALRLRlraEEEAQRksLAQEEAEKQKTEAERdakkkakaeeaal 1846
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQK---QAAEQERLK---QLEKER--LAAQEQKKQAEEAAK------------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1847 kQKENAEKELEKQRtfAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqleDELAKVRSEM 1926
Cdd:PRK09510 126 -QAALKQKQAEEAA--AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA-----EAEAAAKAAA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1927 DALLQMKIQAEKVSQSNTEKskqllETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIL 1997
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKK-----KAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2530-2753 |
1.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2530 EISAEAEKLKLRVKELSSAQAKAEEEatrfKKQAdEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKE 2609
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDA----REQI-ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2610 REKLKRDAQELQnksketasaqqEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ 2689
Cdd:COG4913 297 LEELRAELARLE-----------AELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2690 KLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREK---LESLE 2753
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELeaeIASLE 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1855-2494 |
1.79e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1855 ELEKQRTFAEQIAQQKLSAEQEYIRlKADFEHAEQQRGLLDNELQRLKNEVNAAEKQrrqLEDELAKVRSEMDALlqmKI 1934
Cdd:pfam12128 257 ELRLSHLHFGYKSDETLIASRQEER-QETSAELNQLLRTLDDQWKEKRDELNGELSA---ADAAVAKDRSELEAL---ED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1935 QAEKVSQSNTEKSKQLLETEALKMKQLAEEAARL-------RSVAEEAKKQRQLAEDEAARQRAEaekiLKEKLAAINEA 2007
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKLAKIREA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2008 -TRLKTEAEVALKAKEAEnerlkrqaedeayqrklLEDQAAQHKHDIQEKITQLQSSsVSELDRQKN---IVEETLRQKK 2083
Cdd:pfam12128 406 rDRQLAVAEDDLQALESE-----------------LREQLEAGKLEFNEEEYRLKSR-LGELKLRLNqatATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2084 VVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA 2163
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDW 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRK---------------------------------------------AAQDEVERLKQKAAEANKLKDKAEKELEKQV 2198
Cdd:pfam12128 548 EQSIgkvispellhrtdldpevwdgsvggelnlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2199 ILAKEAAQKSTAAEQKAQDVLSKNKEDLlsqEKLRDEFENAKklaqaaetakekaekeaallRQKAEEAEKLKKAAEDEA 2278
Cdd:pfam12128 628 VQANGELEKASREETFARTALKNARLDL---RRLFDEKQSEK--------------------DKKNKALAERKDSANERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2279 AKQAKAQKdaerlrkeaeaeaakraaaeaAALKQKQEADAEMAKHKKEAEQALKQKSQVEKElglvklqldETDKQKALM 2358
Cdd:pfam12128 685 NSLEAQLK---------------------QLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG---------ALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2359 DEELQrvkaqvndavKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKSlaeEAARLSV 2438
Cdd:pfam12128 735 KAAIA----------ARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI--ERIAVRRQ---EVLRYFD 799
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2439 EAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQE 2494
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1635-1929 |
1.80e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAER 1714
Cdd:COG4372 1 GDRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1715 RLKQAEEEkvrqikvVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELE 1794
Cdd:COG4372 81 ELEELNEQ-------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1795 TWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAE 1874
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 1875 QEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAL 1929
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1719-2060 |
1.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1719 AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRL 1798
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1799 KANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYI 1878
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1879 RLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKM 1958
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1959 KQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQ 2038
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 1655220517 2039 RKLLEDQAAQHKHDIQEKITQL 2060
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2470-2610 |
1.85e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 48.09 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2470 QAIQEATKLKAEAEElQKQKNQAQEKAKKLledKQEIQQRLDKetQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQ 2549
Cdd:PTZ00491 647 DSLQKSVQLAIEITT-KSQEAAARHQAELL---EQEARGRLER--QKMHDKAKAEEQRTKLLELQAESAAVESSGQSRAE 720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2550 AKAEEEATRFKKQA--DEAKVRLqETEKQTTETVVQKLETQR---LQSTREADDL----KKAIAELEKER 2610
Cdd:PTZ00491 721 ALAEAEARLIEAEAevEQAELRA-KALRIEAEAELEKLRKRQeleLEYEQAQNELeiakAKELADIEATK 789
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1948-2105 |
1.88e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1948 KQLLETEALKMKQLAE---EAARLRsvAEEAKKQRQL-AEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2023
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2024 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQS--SSVSELDRQ--KNIVEETLRqKKVVEEEIHIIRiNFERA 2099
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
....*.
gi 1655220517 2100 SKEKSD 2105
Cdd:PRK12704 182 AKEEAD 187
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1703-1876 |
1.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1703 QKHKMQAEEAERRLKQAEEEKvrqikvvEEVAQKTAATQlqamsfsekttkleESLKKEQGTVLQLQEEaeklRKQEEEA 1782
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQ--------------ERLKQLEKERLAAQEQ----KKQAEEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1783 NKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQrtf 1862
Cdd:PRK09510 124 AKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA--------------EAAKKAAAEAKKK--- 186
|
170
....*....|....
gi 1655220517 1863 AEQIAQQKLSAEQE 1876
Cdd:PRK09510 187 AEAEAAAKAAAEAK 200
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2261-2638 |
1.97e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2261 RQKaEEAEKLKKAAEDEAAKQAKAQKDAERLrkeaeaeaakraaaeaaalkQKQEADAEMAKHKKEAEQALKQK-SQVEK 2339
Cdd:PRK11281 77 RQK-EETEQLKQQLAQAPAKLRQAQAELEAL--------------------KDDNDEETRETLSTLSLRQLESRlAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2340 ELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKmqmdellklkvrIEEENLRLMQKNKDNT-QKL 2418
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGK------------VGGKALRPSQRVLLQAeQAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLAEEAARLSVEAEEtarQRktaeAELAEQRALAEKMLkekmQAIQEA--TKLKAEAEELQKQKNQAQEKA 2496
Cdd:PRK11281 204 LNAQNDLQRKSLEGNTQLQDLLQK---QR----DYLTARIQRLEHQL----QLLQEAinSKRLTLSEKTVQEAQSQDEAA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2497 K--------KLLEDKQEIQQRLDKETQG----FQKSLEAerKRQLEISAEAEK-LKLRVKELSSA---------QAKAEE 2554
Cdd:PRK11281 273 RiqanplvaQELEINLQLSQRLLKATEKlntlTQQNLRV--KNWLDRLTQSERnIKEQISVLKGSlllsrilyqQQQALP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EATRFKKQADE-AKVRLQ--ETEKQ-----TTETVVQKLETQrlQSTREADDLKKAIAELEKEREKLKRD---------- 2616
Cdd:PRK11281 351 SADLIEGLADRiADLRLEqfEINQQrdalfQPDAYIDKLEAG--HKSEVTDEVRDALLQLLDERRELLDQlnkqlnnqln 428
|
410 420
....*....|....*....|....*.
gi 1655220517 2617 -AQELQNKSKE---TASAQQEQMEQQ 2638
Cdd:PRK11281 429 lAINLQLNQQQllsVSDSLQSTLTQQ 454
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2929-2963 |
2.05e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.05e-04
10 20 30
....*....|....*....|....*....|....*
gi 1655220517 2929 LSAERAATGFKDPYTGAKISVFEAMQKGLIEKDLA 2963
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2279-2633 |
2.52e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2279 AKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALM 2358
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2359 DEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDnTQKLLAEEAEKMKSLAEEAARLSV 2438
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAE-LQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2439 EAEETARQRKTAEAELAEQrALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQ 2518
Cdd:COG4372 165 ELAALEQELQALSEAEAEQ-ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2519 KSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADD 2598
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330 340 350
....*....|....*....|....*....|....*
gi 1655220517 2599 LKKAIAELEKEREKLKRDAQELQNKSKETASAQQE 2633
Cdd:COG4372 324 LAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2494-2746 |
2.61e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2494 EKAKKLL-EDKQEIQQRLdketqgfqKSLEAERKRQLEISAEAEKLKlrvkelssaqakaeEEATRFKKQADEAKVRLQE 2572
Cdd:PRK00409 505 EEAKKLIgEDKEKLNELI--------ASLEELERELEQKAEEAEALL--------------KEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2573 TEKQttetVVQKLEtqrlqstREAddlKKAIAELEKEREKLKRDAQELQnksKETASAQQEQmeqqkamlqqtfltekel 2652
Cdd:PRK00409 563 EEDK----LLEEAE-------KEA---QQAIKEAKKEADEIIKELRQLQ---KGGYASVKAH------------------ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2653 llkrerDVEDEKKKLQKHLEdEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAE-------MKNKQKEME 2725
Cdd:PRK00409 608 ------ELIEARKRLNKANE-KKEKKKKKQKEKQEELKVGDEVKYLSLGQKGEVLSIPDDKEAIvqagimkMKVPLSDLE 680
|
250 260
....*....|....*....|.
gi 1655220517 2726 ALEKKRLEQEKLLADENKKLR 2746
Cdd:PRK00409 681 KIQKPKKKKKKKPKTVKPKPR 701
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3879-3914 |
2.64e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.64e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1655220517 3879 LNLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3914
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1721-1970 |
2.78e-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: 45.97 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1721 EEKVRQIKVVeeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKA 1800
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIREEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1801 NEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQK--ENAEKELEKQRTFAEQIAQQKLSAEQEYI 1878
Cdd:pfam17045 87 QEELSKLKRSYEKLQRKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKslEWEQQRLQYQQQVASLEAQRKALAEQSSL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1879 RLKADF----EHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMD--ALLQMKIQAEKvsqsntEKSKQLLE 1952
Cdd:pfam17045 167 IQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSelGDSNRKLLEEQ------QRLLEELR 240
|
250
....*....|....*...
gi 1655220517 1953 TEALKMKQLAEEAARLRS 1970
Cdd:pfam17045 241 MSQRQLQVLQNELMELKA 258
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
202-309 |
2.81e-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: 44.23 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNK---------HLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 268
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655220517 269 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 309
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2437-2690 |
2.82e-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: 47.52 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2437 SVEAEETARQRKTAEAELAEQRALAEKmlkekmqAIQEATKLKAEaeelQKQKNQAQEKAKKLLEDKQEIQQRLDKETQG 2516
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK-------ERAEADRQRLE----QEKQQQLAAISGSQSQLESTDQNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2517 FQKSLEAERKrqlEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQ-ADEAKVRLQETEKQTTETVVQKLETQRLQSTRE 2595
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDN 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2596 ADDLKKAIAELE---KEREKLKRDAQelQNKSKETASAQQEQMEqqkAMLQQTFLTEKEllLKRERDVEDEKKKLQKHLE 2672
Cdd:NF012221 1684 QQKVKDAVAKSEagvAQGEQNQANAE--QDIDDAKADAEKRKDD---ALAKQNEAQQAE--SDANAAANDAQSRGEQDAS 1756
|
250
....*....|....*....
gi 1655220517 2673 DEVNKA-KALKDEQQRQQK 2690
Cdd:NF012221 1757 AAENKAnQAQADAKGAKQD 1775
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2458-2750 |
2.82e-04 |
|
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: 46.45 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2458 RALAEKMLKEKMQAIQEATKLkaeaeelQKQKNQAQEKAKKLLEDKQEIQQRLDKEtqgfQKSLEAERKRQLEISAEAEK 2537
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIA-------EKKRIKAEEKEEERRLDEMMEEERERAL----EEEEEKEEERKEERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2538 LKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQttetvvqKLETQRLQSTREADDLKKAIAELEKEREKLKRDA 2617
Cdd:pfam13868 78 LEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQA-------EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2618 QELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELL------LKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKL 2691
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIarlraqQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2692 MDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLE 2750
Cdd:pfam13868 231 ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
306-416 |
2.89e-04 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 43.26 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 306 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQ-ENLEQAFSVA 384
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPvTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 385 ERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 416
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
2398-2738 |
2.93e-04 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 46.96 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2398 VRIEEENLRLMQKNKDNTQKLLAE-EAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAT 2476
Cdd:pfam14817 50 VRKIRGNLLWYGGLQDKGKAESRQsAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDEISDSRHRQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2477 KLKAeaeelqkQKNQAQEKAKKLLEDKQEIQQRLDketqgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKAEEEA 2556
Cdd:pfam14817 130 LLEA-------YDQQCEEARKILAEDHQRLQGQLQ-------------QLRDAARKAEKEVVFGDSKGSKSSVIALEPQV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2557 TRFKKQADEAKVR----LQETE-KQTTETVVQKLETQR----LQSTREADDLK-----------------KAIAELEKER 2610
Cdd:pfam14817 190 LRDVREACELRAQflqeLLESSlKAYEGSGIHMNRDQRraviQHWLSAVETLLtshppshllqalehlaaREKTAIQEET 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2611 EKL--KRDAQELQNK---------SKETASAQQEQ---MEQQKAMLQQtFLTEKELLLKRERdvedekkKLQKHLE---D 2673
Cdd:pfam14817 270 ESLdvRADAEALRFRyesnhlldvSSDESSDLPSVrqlLERQWAHVQQ-FLNELAETRSRCQ-------QLQARLQglkD 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2674 EVNK-----AKALKDEQQRQQKLMDE-----EKKKLQAIMDE------AVKKQKEAEAEMKNKQKEMEALEKKRLEQEKL 2737
Cdd:pfam14817 342 EAELeslgiGDTSQNDSLLRQVLELElqaagLAASRDTLRSEcqqlnkLARERQEALRSLQKKWQRILDFRQLVSELQEQ 421
|
.
gi 1655220517 2738 L 2738
Cdd:pfam14817 422 I 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2053-2509 |
2.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2053 IQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLkgiadETQKSKAKAEEEAE 2132
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2133 KLKKLAAEEERKRREAEEKVKKIaaaeEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAE 2212
Cdd:COG4717 136 ALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2213 QKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAERLR 2292
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2293 KEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKL--QLDETDKQKALMDEELQRVKA-QV 2369
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREAEELEEELQLEELeQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2370 NDAVKQKAQVENE--LSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEkmkSLAEEAARLSVEAEETARQR 2447
Cdd:COG4717 372 IAALLAEAGVEDEeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE---ELEEELEELEEELEELEEEL 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2448 KTAEAELAEQRALAEKMLKEK--MQAIQEATKLKAEAEELQKQKnQAQEKAKKLLEDKQEIQQR 2509
Cdd:COG4717 449 EELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEW-AALKLALELLEEAREEYRE 511
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2165-2376 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2165 QRKAAQDEVERLKQKAAEANKlKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLlsQEKLRDEFENAKKLAQ 2244
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEK-QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE--EAKAKQAAEAKAKAEA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2245 AAETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQ---AKAQKDAER-----LRKEAEAEAAKRAAaeaaalkqkQEA 2316
Cdd:TIGR02794 139 EAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAeaeAKAKAEAEAkakaeEAKAKAEAAKAKAA---------AEA 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2317 DAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQK------ALMDEELQRVKAQVNDAVKQK 2376
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAGSEVDKYAAIIQQAIQQN 275
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1648-1992 |
3.08e-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: 47.21 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1648 EAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKVRQI 1727
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1728 KVVEEVAQKTAAtqlQAMSFSEKTTKLEESLKKEQgtvlQLQEEAEK-LRKQEEEANKAREQAEKELETWRLKANEAlrl 1806
Cdd:pfam15964 431 SQLEEAQKQLAS---QEMDVTKVCGEMRYQLNQTK----MKKDEAEKeHREYRTKTGRQLEIKDQEIEKLGLELSES--- 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1807 RLRAEEEAQRKSLAQEEAEKQK---TEAERDAKKKAKaeeaalkqkenaEKElEKQRTFAEQIAQQKLSAEQEYIRLKAD 1883
Cdd:pfam15964 501 KQRLEQAQQDAARAREECLKLTellGESEHQLHLTRL------------EKE-SIQQSFSNEAKAQALQAQQREQELTQK 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1884 FEHAEQQRGLLDNELQRLKNEVNAAEKQRRQ--------LEDELAKVRSEMDALLQ----MKIQAEKVSQSNTEKSKQLL 1951
Cdd:pfam15964 568 MQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctlakkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCV 647
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1952 ------ETEALKMKQL-------AEEAARLRSVAEEAKKQRQLAEDEAARQRAE 1992
Cdd:pfam15964 648 qhgrmhERMKQRLRQLdkhcqatAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3254-3285 |
3.10e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.10e-04
10 20 30
....*....|....*....|....*....|..
gi 1655220517 3254 QLLSAERAVSGYKDPYTGKTVSLFEAMNKGLI 3285
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2548-2736 |
3.20e-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: 47.52 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2548 AQAKAEEEATRFKKQADEAKVRL-QE----------TEKQTTETVVQKLET----QRLQSTREADDLKKAIAELEKEREK 2612
Cdd:NF012221 1552 KQDDAAQNALADKERAEADRQRLeQEkqqqlaaisgSQSQLESTDQNALETngqaQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2613 LKRDAQ-------------------ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDV---EDEKKKLQKH 2670
Cdd:NF012221 1632 LDSQATyagesgdqwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVaqgEQNQANAEQD 1711
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 2671 LEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKK--QKEAEAEMKNKQKEMEALEKKRLEQEK 2736
Cdd:NF012221 1712 IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgeQDASAAENKANQAQADAKGAKQDESDK 1779
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2890-2923 |
3.41e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220517 2890 LLEAQAASGYIVDPVKNKLLTVDEAVKEELIGPE 2923
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1594-1704 |
3.46e-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: 43.58 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1594 EQEIRsknQQLEEAQVSRRKLEEeihliriqlqttikQKSTADDELQKLRdqaAEAEKVRKAAQEEAERLRKQVNEETQK 1673
Cdd:cd06503 32 EEKIA---ESLEEAEKAKEEAEE--------------LLAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKE 91
|
90 100 110
....*....|....*....|....*....|.
gi 1655220517 1674 KKNaedelKRKSEAEKEAARQKQKALDELQK 1704
Cdd:cd06503 92 EAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1798-2212 |
3.59e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1798 LKANEALRLRLRaEEEAQRKSLAQEEAEKQKTEAERDAKKKakaeeaalkQKENAEKELEKQRTF--AEQIAQQKLSAEQ 1875
Cdd:COG4717 70 LKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEA---------ELEELREELEKLEKLlqLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1876 EYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA 1955
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1956 LKMKQLAEEAARLRSVAEEAKKQRQLAEdEAARQRAEAEKILKEKLAAINEATRLKTEAEVAL-----------KAKEAE 2024
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2025 NERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKS 2104
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2105 DLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKK-IAAAEEEAARQRKAAQDEVERLKQKAAEA 2183
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAEL 458
|
410 420
....*....|....*....|....*....
gi 1655220517 2184 NKLKDKAEKELEKQVILAKEAAQKSTAAE 2212
Cdd:COG4717 459 EAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2567-2767 |
3.62e-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: 46.81 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2567 KVRLQETEKQTTEtVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQK--AMLQQ 2644
Cdd:pfam07888 33 QNRLEECLQERAE-LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKelSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2645 TFLTEKELLLkrerDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM 2724
Cdd:pfam07888 112 ELSEEKDALL----AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEEL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1655220517 2725 EALEKKRLEQEKLLADENK---KLREKLESLEVTSKQAASKTKEIE 2767
Cdd:pfam07888 188 RSLSKEFQELRNSLAQRDTqvlQLQDTITTLTQKLTTAHRKEAENE 233
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1767-2086 |
3.64e-04 |
|
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: 46.07 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1767 QLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAAL 1846
Cdd:pfam13868 37 EEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1847 KQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKV---- 1922
Cdd:pfam13868 117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQqeka 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1923 ---RSEMDALLQMKIQAEkvsqsNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlaEDEAARQRAEAEKILKE 1999
Cdd:pfam13868 197 qdeKAERDELRAKLYQEE-----QERKERQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2000 KlaaineatrlkteAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEEtl 2079
Cdd:pfam13868 270 Q-------------AEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE-- 334
|
....*..
gi 1655220517 2080 RQKKVVE 2086
Cdd:pfam13868 335 RQKKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1671-1872 |
3.65e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1671 TQKKKNAEDELKR-KSEAEKEAARQKQKALdelqkhkMQAEEAERRLKQAEEEKVRQIKvveevaqktaatqlqamsfsE 1749
Cdd:PRK12704 30 EAKIKEAEEEAKRiLEEAKKEAEAIKKEAL-------LEAKEEIHKLRNEFEKELRERR--------------------N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1750 KTTKLEESLK-KEQgtvlQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKS-LAQEEAEKQ 1827
Cdd:PRK12704 83 ELQKLEKRLLqKEE----NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgLTAEEAKEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1828 ---KTEAErdakkkAKAEEAALKQ------KENAEKELEK------QRTFAEQIAQQKLS 1872
Cdd:PRK12704 159 lleKVEEE------ARHEAAVLIKeieeeaKEEADKKAKEilaqaiQRCAADHVAETTVS 212
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1815-2034 |
3.67e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1815 QRKSLAQEEAEKQKTEAERdakkkakaeeaalkQKENAEKELEKQRTFaEQIAQQKLSAEQEYirlkadfEHAEQQRGll 1894
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQ--------------AEELQQKQAAEQERL-KQLEKERLAAQEQK-------KQAEEAAK-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1895 dnelQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQllETEALKMKQLAEEAARLRSVAEE 1974
Cdd:PRK09510 126 ----QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1975 AKKQRQLAEDEA---ARQRAEAEKilkeKLAAINEATRLKTEAEVALKAKEAENERLKRQAED 2034
Cdd:PRK09510 200 KKKAEAEAKKKAaaeAKKKAAAEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2426-2767 |
3.97e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 46.61 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2426 MKSLAEEAARLsveaeETARQRKTAEAELAEqRALAEKMLK--EKMQAIQEATKLKAEAEELQ------KQKNQAQEKAK 2497
Cdd:pfam05622 68 LEQLQEENFRL-----ETARDDYRIKCEELE-KEVLELQHRneELTSLAEEAQALKDEMDILRessdkvKKLEATVETYK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLED----KQEIQQRLDKETQGFQK--SLEAERKRQLEISAEAEKLKLRVKELssaQAKAEEEATRFKKQADEAKvRLQ 2571
Cdd:pfam05622 142 KKLEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK-KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2572 ETEKqttetVVQKlETQRLQSTReaDDLKKAIAELE----KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFL 2647
Cdd:pfam05622 218 EKLE-----ALQK-EKERLIIER--DTLRETNEELRcaqlQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2648 TEKELLLKRERDVEDEKKKLQKHLEDevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEM 2724
Cdd:pfam05622 290 ENKMLRLGQEGSYRERLTELQQLLED----ANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKL 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1655220517 2725 EALEKKRLEqeklLADENKKLREKLESLEVT-SKQAASKTKEIE 2767
Cdd:pfam05622 366 EEHLEKLHE----AQSELQKKKEQIEELEPKqDSNLAQKIDELQ 405
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1523-1984 |
3.99e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1523 KKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKlkmkedasqrQGLAVDAEKQKQNIQlELTQLKNLSEQEIRSKNQ 1602
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN----------AALNEMRQRYKEKTQ-QLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1603 qleEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKvrKAAQEEAERLRKQVNEETQKKKNAEDELK 1682
Cdd:PRK10246 494 ---EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV--KKLGEEGAALRGQLDALTKQLQRDESEAQ 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAEKEAARQKQKAL----------DELQKHKMQAEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQlqamSFSEKTT 1752
Cdd:PRK10246 569 SLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQ----QIEQRQQ 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1753 KLEESLKKEQGTVLQLQEEAEKLRKQEEEAN--KAREQAEKELETwRLKANEALRLRLRAEEEAQrkslaqEEAEKQKTE 1830
Cdd:PRK10246 645 QLLTALAGYALTLPQEDEEASWLATRQQEAQswQQRQNELTALQN-RIQQLTPLLETLPQSDDLP------HSEETVALD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1831 AER---DAKKKAKAEEAALKQKENAEKE--LEKQRTFAEQIAQQKLSAEQEYIRLKADfehaEQQRGLLDNELQRLKNEV 1905
Cdd:PRK10246 718 NWRqvhEQCLSLHSQLQTLQQQDVLEAQrlQKAQAQFDTALQASVFDDQQAFLAALLD----EETLTQLEQLKQNLENQR 793
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1906 NAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEA------LKMKQLAEEAARLRSVAEEAKKQR 1979
Cdd:PRK10246 794 QQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTrqgeirQQLKQDADNRQQQQALMQQIAQAT 873
|
....*
gi 1655220517 1980 QLAED 1984
Cdd:PRK10246 874 QQVED 878
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1790-2032 |
4.02e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.51 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1790 EKELETWRLKANEalrlrlRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQ 1869
Cdd:PRK07735 4 EKDLEDLKKEAAR------RAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1870 KLSAEQEYI---RLKADFEHAEQQRGlldnELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEK 1946
Cdd:PRK07735 78 KREGTEEVTeeeKAKAKAKAAAAAKA----KAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1947 SKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAED-------EAARQRAEAEKILKEKLAAI-----------NEAT 2008
Cdd:PRK07735 154 TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGteevteeEKAKAKAKAAAAAKAKAAALakqkasqgngdSGDE 233
|
250 260
....*....|....*....|....
gi 1655220517 2009 RLKTEAEVALKAKEAENERLKRQA 2032
Cdd:PRK07735 234 DAKAKAIAAAKAKAAAAARAKTKG 257
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1822-2119 |
4.06e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1822 EEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRL 1901
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1902 KNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEE-AKKQRQ 1980
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1981 LAEDEAARQR---AEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKI 2057
Cdd:COG4372 166 LAALEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2058 TQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2119
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4434-4467 |
4.12e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.12e-04
10 20 30
....*....|....*....|....*....|....
gi 1655220517 4434 EESGPVAGILDTDTLEKVSVTEAIHRNLVDNITG 4467
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1572-1725 |
4.18e-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: 46.56 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1572 AVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDELQKLRDQAAEAEK 1651
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIK----KLESSIKQVEEELEELKEQNEELEKQYK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1652 VRKA-------AQEEAERLRKQVNEETQKKKNAEDE-------LKRKSEAEKEAARQK----QKALDELQKHKMQAEEAE 1713
Cdd:pfam05667 388 VKKKtldllpdAEENIAKLQALVDASAQRLVELAGQwekhrvpLIEEYRALKEAKSNKedesQRKLEEIKELREKIKEVA 467
|
170
....*....|..
gi 1655220517 1714 RRLKQAEEEKVR 1725
Cdd:pfam05667 468 EEAKQKEELYKQ 479
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
203-268 |
4.22e-04 |
|
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: 42.65 E-value: 4.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 203 KKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 268
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1631-2070 |
4.38e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1631 QKSTADDELQKLRDQAAeaeKVRKAAQEEAERLRKQVNEETqkkknaeDELKRKSEAEKEAARQKQ--KALDELQKHKMQ 1708
Cdd:PRK10246 192 QHKSARTELEKLQAQAS---GVALLTPEQVQSLTASLQVLT-------DEEKQLLTAQQQQQQSLNwlTRLDELQQEASR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1709 AEEAERRLKQAEEEKVRQIKVVEeVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAE---KLRKQEEEANKA 1785
Cdd:PRK10246 262 RQQALQQALAAEEKAQPQLAALS-LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMAlraRIRHHAAKQSAE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1786 REQAEKELETWrLKANEALRLrLRAEEEAQRKSLAQEEAEKQKTEAERdakkkakAEEAALKQKENAEKELEKQRTFAEQ 1865
Cdd:PRK10246 341 LQAQQQSLNTW-LAEHDRFRQ-WNNELAGWRAQFSQQTSDREQLRQWQ-------QQLTHAEQKLNALPAITLTLTADEV 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1866 IAQQKLSAEQEYIR-----LKADFEHAEQQRGLLDNELQRLKNEV---NAAEKQRRQL----EDELAKVRS--------- 1924
Cdd:PRK10246 412 AAALAQHAEQRPLRqrlvaLHGQIVPQQKRLAQLQVAIQNVTQEQtqrNAALNEMRQRykekTQQLADVKTiceqearik 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1925 ---EMDALLQM----------------KIQAEKVSQSNTEKSKqlLETEalkMKQLAEEAARLRSVAEEAKKQRQLAEDE 1985
Cdd:PRK10246 492 dleAQRAQLQAgqpcplcgstshpaveAYQALEPGVNQSRLDA--LEKE---VKKLGEEGAALRGQLDALTKQLQRDESE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1986 AARQRAEaEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAeDEAYQRKLLEDQAAQHKHDI---QEKITQLQS 2062
Cdd:PRK10246 567 AQSLRQE-EQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQL-RLLSQRHELQGQIAAHNQQIiqyQQQIEQRQQ 644
|
....*...
gi 1655220517 2063 SSVSELDR 2070
Cdd:PRK10246 645 QLLTALAG 652
|
|
| I-BAR_IMD |
cd07605 |
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module ... |
2631-2774 |
4.40e-04 |
|
Inverse (I)-BAR, also known as the IRSp53/MIM homology Domain (IMD), a dimerization module that binds and bends membranes; Inverse (I)-BAR (or IMD) is a member of the Bin/Amphiphysin/Rvs (BAR) domain family. It is a dimerization and lipid-binding module that bends membranes and induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. IMD domains are found in Insulin Receptor tyrosine kinase Substrate p53 (IRSp53), Missing in Metastasis (MIM), and Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2-like (BAIAP2L) proteins. These are multi-domain proteins that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. Most members contain an N-terminal IMD, an SH3 domain, and a WASP homology 2 (WH2) actin-binding motif at the C-terminus, exccept for MIM which does not carry an SH3 domain. Some members contain additional domains and motifs. The IMD domain binds and bundles actin filaments, binds membranes and produces membrane protrusions, and interacts with the small GTPase Rac.
Pssm-ID: 153289 [Multi-domain] Cd Length: 223 Bit Score: 45.05 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2631 QQEQMEQQKAMLQQTFLteKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQR-QQKLMDEEKKKLQAIMDEAVKK 2709
Cdd:cd07605 76 THKSIEASLEQVAKAFH--GELILPLEKKLELDQKVINKFEKDYKKEYKQKREDLDKaRSELKKLQKKSQKSGTGKYQEK 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2710 QKEAEAEMKNKQKEMEALEKkrLEQEKLLADENKKLREKLESL-EVTSKQAASKTKEIEVQTDKVP 2774
Cdd:cd07605 154 LDQALEELNDKQKELEAFVS--QGLRDALLEERRRYCFLVDKHcSVAKHEIAYHAKAMTLLSTRLP 217
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1525-1698 |
4.46e-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: 45.30 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1525 RMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDAEKQKQNIQLELTQLknlsEQEIRSKNQQL 1604
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEV----EARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1605 EEAQVSRrkleeEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKrK 1684
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE-A 156
|
170
....*....|....
gi 1655220517 1685 SEAEKEAARQKQKA 1698
Cdd:COG1579 157 ELEELEAEREELAA 170
|
|
| MAP70 |
pfam07058 |
Microtubule-associated protein 70; This family represents a family of plant ... |
2477-2760 |
4.57e-04 |
|
Microtubule-associated protein 70; This family represents a family of plant microtubule-associated proteins of size 70 kDa. The proteins contain four predicted coiled-coil domains, and truncation studies identify a central domain that targets the proteins to microtubules. It has no predicted trans-membrane domains, and the region between the coils from approximately residues 240-483 is the targetting region.
Pssm-ID: 399798 [Multi-domain] Cd Length: 544 Bit Score: 46.35 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2477 KLKAEAEEL---QKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEIsaeaEKLKLRVKELSSAQAKAE 2553
Cdd:pfam07058 15 EVRDKDRELgeaLAEIKALRLSERLKEKAVEELTDELLKLDEKLKASENLLESKNLEI----KKINDEKKAALAAQFAAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2554 EEATRFKK-QADEAKVRLQETE-KQTTETVVQKLETQRLQSTREADD---LKKAIAELEKEREK--LKRDAQ---ELQNK 2623
Cdd:pfam07058 91 ATLRRVHAaQKDEDMPPIEAILaPLEAELKLARQEINKLQDDNKALDrltKSKEAALLEAERAVqiALAKASlvdDLQNK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2624 S----KETASAQQEQMEQQKAMLQQTFLTEKELLLKRErdvedekkkLQKHLEDEVNKAKALKDEQqRQQKLMDEEKKKL 2699
Cdd:pfam07058 171 NqelmKQIEICQEENKILDKAHRQKVAEVEKLSQTVRE---------LEEAVLAGGAAANAVRDYQ-RKVKEMNEERRTL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 2700 QAIMDEAVKKQKEAEAEMKNKQKE-----MEalEKKRLEQEKLLADENKKLREKLESLEVTSKQAA 2760
Cdd:pfam07058 241 ERELARAKVVANRVATVVANEWKDandkvMP--VKQWLEERRFLQGEMQQLRDKLAISERTAKAEA 304
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2595-2705 |
4.59e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2595 EADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLlkrerdveDEKKKLQKHLEDE 2674
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELI--------EEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|.
gi 1655220517 2675 VNKAKALKDEQQRQQKLMDEEKKKLQAIMDE 2705
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2311-2659 |
4.76e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.82 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2311 KQKQEADAEMAKHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEE------LQRVKAQVNDAVKQKAQVENELS 2384
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDdhnrasMQRDEAIAAIDNEQQTNSKDGEQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2385 KVKMQMDELLKLKVRIEEENLRLMQ-------------KNKDNTQK-------LLAEEAEKMKSLAEEAARLSVEAEETA 2444
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKNILLLNQarlqaledlekilTEKEALQGkinilemRLSETDARIKLAAQEKIHVEILEEQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2445 RQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKLLedkqeiqqRLDKETQGFQKSLeae 2524
Cdd:PLN02939 205 KLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVF--------KLEKERSLLDASL--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2525 rkRQLE---ISAEAEKLKLRVKELSSAQAKAEEEAT---RFKKQADEAKVRLQetEKQTTETVVQKLEtqrlQSTREADD 2598
Cdd:PLN02939 274 --RELEskfIVAQEDVSKLSPLQYDCWWEKVENLQDlldRATNQVEKAALVLD--QNQDLRDKVDKLE----ASLKEANV 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2599 LKKAIAELEKEREKLKRDAQELQNKSKETASaQQEQMEQQKAMLQQTFLTEKELLLKRERD 2659
Cdd:PLN02939 346 SKFSSYKVELLQQKLKLLEERLQASDHEIHS-YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1774-2029 |
5.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1774 KLRKQEEEANKAREQAEKEletwrlkanealrlrlrAEEEAQRKSL-AQEEAEKQKTEAERDAKkkakaeeaalkQKENA 1852
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKE-----------------AEAIKKEALLeAKEEIHKLRNEFEKELR-----------ERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1853 EKELEKqrtfaeqiaqqklsaeqeyiRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEdelaKVRSEMDALLQM 1932
Cdd:PRK12704 84 LQKLEK--------------------RLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1933 KIQA-EKVSQSNTEKSKQLLetealkMKQLAEEAarlrsvAEEAKKQRQLAEDEAarqRAEAEKILKEKLA-AIneaTRL 2010
Cdd:PRK12704 140 QLQElERISGLTAEEAKEIL------LEKVEEEA------RHEAAVLIKEIEEEA---KEEADKKAKEILAqAI---QRC 201
|
250 260
....*....|....*....|.
gi 1655220517 2011 KTE--AEVALKAKEAENERLK 2029
Cdd:PRK12704 202 AADhvAETTVSVVNLPNDEMK 222
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1503-1827 |
5.40e-04 |
|
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: 45.80 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDasqrqglavdaEKQKQNI 1582
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLE-----------RARQEAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1583 QLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIH---LIRIQLQTTIKQKSTAD----DELQKLRDQAAEAEKVRKA 1655
Cdd:pfam15558 120 QRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHkrqLKEREEQKKVQENNLSEllnhQARKVLVDCQAKAEELLRR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEdELKRKSEAEKEAARQKQ----KALDELQKHK-MQAEEAERRLKQAEEekvrqikVV 1730
Cdd:pfam15558 200 LSLEQSLQRSQENYEQLVEERHR-ELREKAQKEEEQFQRAKwraeEKEEERQEHKeALAELADRKIQQARQ-------VA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKTAATQLQAMSFSEKTTKLEEsLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALRLRLRA 1810
Cdd:pfam15558 272 HKTVQDKAQRARELNLEREKNHHILK-LKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKTARASFHMREKV 350
|
330
....*....|....*..
gi 1655220517 1811 EEEAQRKSLAQEEAEKQ 1827
Cdd:pfam15558 351 REETNNRTFDKMALEAQ 367
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2369-2664 |
5.54e-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: 46.29 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2369 VNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRK 2448
Cdd:pfam09731 109 TKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2449 TAEAELAEQRALAEKmlkekmqaIQEATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQ 2528
Cdd:pfam09731 189 EALAEKLKEVINLAK--------QSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQ 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2529 LE--------ISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTRE----- 2595
Cdd:pfam09731 261 QElvsifpdiIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARleevr 340
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2596 ADDLKKAIAELEKEREKLKRDAQ-----ELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEK 2664
Cdd:pfam09731 341 AADEAQLRLEFEREREEIRESYEeklrtELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLK 414
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2518-2851 |
6.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2518 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRL--QSTRE 2595
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEleSLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2596 ADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEV 2675
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2676 NKAKalKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVT 2755
Cdd:COG4372 190 KEAN--RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2756 SKQAASKTKEIEVQTDKVPEEQLVSMTTVETTKKVFNGSVEAVKKDGASPLAFEGIRESVPAERLLEIGVLTKKDVDKLK 2835
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330
....*....|....*.
gi 1655220517 2836 KGKVSAQDLSKADKVK 2851
Cdd:COG4372 348 VGLLDNDVLELLSKGA 363
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1864-2279 |
6.18e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.05 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1864 EQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSN 1943
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1944 TEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEA 2023
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2024 ENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 2103
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2104 SDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEA 2183
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2184 NKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAALLRQK 2263
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAA 512
|
410
....*....|....*.
gi 1655220517 2264 AEEAEKLKKAAEDEAA 2279
Cdd:COG5278 513 AEAALAAALAAALASA 528
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1516-1783 |
6.18e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.00 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1516 EKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLeltqLKNLSEQ 1595
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEA----LKAEVAS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1596 EIRSKNQQLEEA---QVSRRKLEEEIHLIRIQlqttikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQ 1672
Cdd:PLN03229 590 SGASSGDELDDDlkeKVEKMKKEIELELAGVL------KSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIE 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1673 KKKNAEDeLKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVRQIKvveevaQKTAATQLQAMSFSEKTT 1752
Cdd:PLN03229 664 RVIRSSD-LKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELK------EKFEELEAELAAARETAA 736
|
250 260 270
....*....|....*....|....*....|.
gi 1655220517 1753 KLEESLKKEqgtvlQLQEEAEKLRKQEEEAN 1783
Cdd:PLN03229 737 ESNGSLKND-----DDKEEDSKEDGSRVEVN 762
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
202-299 |
6.31e-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: 43.04 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVN---------KHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 268
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1655220517 269 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 299
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2263-2528 |
7.11e-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: 46.37 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2263 KAEEAEKLKKAAEDEAAKQA---KAQKDAERlrkeaeaeaakraaaeaAALKQ-KQEADAEMAKHKKEAE----QALKQK 2334
Cdd:NF012221 1541 SQQADAVSKHAKQDDAAQNAladKERAEADR-----------------QRLEQeKQQQLAAISGSQSQLEstdqNALETN 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2335 SQVEKELglVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENE-----LSKVKMQMDELlKLKVRIEEENLRlmQ 2409
Cdd:NF012221 1604 GQAQRDA--ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPfagglLDRVQEQLDDA-KKISGKQLADAK--Q 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2410 KNKDNTQKLlAEEAEKMKSLAEEAARLSVEAEETARQRKTaEAELAEQRALAEKmlkekmqaiQEATKLKAEAEELQKQK 2489
Cdd:NF012221 1679 RHVDNQQKV-KDAVAKSEAGVAQGEQNQANAEQDIDDAKA-DAEKRKDDALAKQ---------NEAQQAESDANAAANDA 1747
|
250 260 270
....*....|....*....|....*....|....*....
gi 1655220517 2490 NQAQEKAKKLLEDKQEIQQrldKETQGFQKSLEAERKRQ 2528
Cdd:NF012221 1748 QSRGEQDASAAENKANQAQ---ADAKGAKQDESDKPNRQ 1783
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1408-1723 |
7.23e-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: 45.66 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1408 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDY---------EFQILAYRALQDPIASPLKKPKMESASDNIIQ 1478
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQrrelesrvaELKEELRQSREKHEELEEKYKELSASSEELSE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1479 EYVTL-------RTRYSEL----STLTSQYIKFILETQRRLEDDEKASEKLKEDEKKRmaeiqAQLETQKQLAEGHAKSV 1547
Cdd:pfam07888 116 EKDALlaqraahEARIRELeediKTLTQRVLERETELERMKERAKKAGAQRKEEEAER-----KQLQAKLQQTEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1548 AKaelEAQELKLKMKEDASQRQGLAVDAEKQKQNI------QLELTQLK----------NLSEQEIRSKNQQLEEAQVSR 1611
Cdd:pfam07888 191 SK---EFQELRNSLAQRDTQVLQLQDTITTLTQKLttahrkEAENEALLeelrslqerlNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1612 RKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQ-AAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKE 1690
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
330 340 350
....*....|....*....|....*....|...
gi 1655220517 1691 AARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1723
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASLRVAQKEK 380
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2549-2769 |
7.37e-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: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2549 QAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQrlqstreaddlkkaIAELEKEREKLKRDAQELQNKSKETA 2628
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQR--------------AAEQARQKELEQRAAAEKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2629 SAQQEqmEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQ----KLMDEEKKKlqaimD 2704
Cdd:TIGR02794 111 AKQAE--EKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEeakkKAEAEAKAK-----A 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2705 EAVKKQKEAEAEMKNKQ--KEMEALEKKRLEQEKLLADENKKLReKLESLEVTSKQAASKTKEIEVQ 2769
Cdd:TIGR02794 184 EAEAKAKAEEAKAKAEAakAKAAAEAAAKAEAEAAAAAAAEAER-KADEAELGDIFGLASGSNAEKQ 249
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2515-2776 |
7.46e-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: 45.19 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2515 QGFQKSLEAERKRQLEISAEAEKL----KLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ-----TTETVVQKL 2585
Cdd:pfam15905 27 QRFRKQKAAESQPNLNNSKDASTPatarKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQdkrlqALEEELEKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2586 ETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAM-LQQTFLTEKELLLKRERDVEDEK 2664
Cdd:pfam15905 107 EAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSSLSMELMkLRNKLEAKMKEVMAKQEGMEGKL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2665 KKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEaEMKNKQKEMEALEKKRLEQEKLLADENKK 2744
Cdd:pfam15905 187 QVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSE-QVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270
....*....|....*....|....*....|..
gi 1655220517 2745 LREKLESLEVTSKQAASKTKEIEVQTDKVPEE 2776
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLRE 297
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2408-2640 |
7.73e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 45.36 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2408 MQKNKDnTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEAtklKAEAEELQK 2487
Cdd:PRK07735 1 MDPEKD-LEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAA---KAKAAALAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2488 QKNQAQEKAKKllEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEeatrFKKQADEAK 2567
Cdd:PRK07735 77 QKREGTEEVTE--EEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAA----LAKQKREGT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2568 VRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKA 2640
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKA 223
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2430-2693 |
8.45e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2430 AEEAARLSVEAE-----ETARQRKTAEAElaeqRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKakkLLEDKQ 2504
Cdd:PRK11281 29 AASNGDLPTEADvqaqlDALNKQKLLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAK---LRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2505 EIQQRLDKETQGFQKSLEAERKRQLEisaeaEKLKLRVKELSSAQAKAEEEAT----------RFKKQADEAKVRLQETE 2574
Cdd:PRK11281 102 ELEALKDDNDEETRETLSTLSLRQLE-----SRLAQTLDQLQNAQNDLAEYNSqlvslqtqpeRAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2575 KQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDA--QELQNKSKETASAQQEQMEQQKAMLQQtfltekel 2652
Cdd:PRK11281 177 NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlQDLLQKQRDYLTARIQRLEHQLQLLQE-------- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1655220517 2653 LLKRERDVEDEKKKLQKHLEDEVNKAKA---LKDEQQRQQKLMD 2693
Cdd:PRK11281 249 AINSKRLTLSEKTVQEAQSQDEAARIQAnplVAQELEINLQLSQ 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2601-2777 |
8.76e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2601 KAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELllkreRDVEDEKKKLQKHLedevnkaKA 2680
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAEL-------AE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2681 LKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKkRLEQEKLLADENKK----LREKLESLEVTS 2756
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREqaeeLRADLAELAALR 166
|
170 180
....*....|....*....|.
gi 1655220517 2757 KQAASKTKEIEVQTDKVPEEQ 2777
Cdd:COG4942 167 AELEAERAELEALLAELEEER 187
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1635-1786 |
9.08e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 45.80 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKhKMQAEEAER 1714
Cdd:PRK10811 625 DNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQAQQEA-KALNVEEQS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1715 RLKQAEEEKVRQI-----------KV-VEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEA 1782
Cdd:PRK10811 704 VQETEQEERVQQVqprrkqrqlnqKVrIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDEEN 783
|
....
gi 1655220517 1783 NKAR 1786
Cdd:PRK10811 784 NAEN 787
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1643-1831 |
9.31e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1643 RDQAAEAEKVRKAAQEEAErlrkqvnEETQKKKNAEDELKRKSEAEKEAARQKQKALD-------ELQKHKMQAEEAERR 1715
Cdd:PRK05035 464 REKAAREARHKKAAEARAA-------KDKDAVAAALARVKAKKAAATQPIVIKAGARPdnsaviaAREARKAQARARQAE 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1716 LKQAEEEKVRQIKVVEEVAQKTAATQLQAmsfsEKTTKLEESLKKEQGTVLQLQEEAeKLRKQEEEANKAREQAEKELET 1795
Cdd:PRK05035 537 KQAAAAADPKKAAVAAAIARAKAKKAAQQ----AANAEAEEEVDPKKAAVAAAIARA-KAKKAAQQAASAEPEEQVAEVD 611
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220517 1796 WRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEA 1831
Cdd:PRK05035 612 PKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1624-1907 |
9.78e-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: 45.60 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1624 QLQTTIKQKSTADDELQKLRDQA-AEAEKvRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKAL-DE 1701
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADR-QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESRAVtKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1702 LQKhKMQAEEAERRLKQAEEEKVRQ---------IKVVEEV---AQKTAATQLQAMS--FSEKTTKLEESLKKEQGTVLQ 1767
Cdd:NF012221 1622 LTT-LAQGLDALDSQATYAGESGDQwrnpfagglLDRVQEQlddAKKISGKQLADAKqrHVDNQQKVKDAVAKSEAGVAQ 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1768 lqeeAEKLRKQEEEA-NKAREQAEKeletwrlKANEALRLRLRAEEEAQRKSLAQEEAEKQ-KTEAERDAKKKAKAEEAA 1845
Cdd:NF012221 1701 ----GEQNQANAEQDiDDAKADAEK-------RKDDALAKQNEAQQAESDANAAANDAQSRgEQDASAAENKANQAQADA 1769
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1846 LKQKENAEKELEKQRTFAEQIAQQKLSAE---QEYIRLKADFEHAEQQR---GLLDNELQRLKNEVNA 1907
Cdd:NF012221 1770 KGAKQDESDKPNRQGAAGSGLSGKAYSVEgvaEPGSHINPDSPAAADGRfseGLTEQEQEALEGATNA 1837
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1498-1727 |
9.85e-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: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1498 IKFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEghaksVAKAELEAQELklkmkedasqRQGLAvDAEK 1577
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-----YSWDEIDVASA----------EREIA-ELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1578 QKQNIQLELTQLKNLSEQ------EIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEA-- 1649
Cdd:COG4913 676 ELERLDASSDDLAALEEQleeleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErf 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1650 --EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRK--------------SEAEKEAARQKQKALDELQKHKM--QAEE 1711
Cdd:COG4913 756 aaALGDAVERELRENLEERIDALRARLNRAEEELERAmrafnrewpaetadLDADLESLPEYLALLDRLEEDGLpeYEER 835
|
250
....*....|....*.
gi 1655220517 1712 AERRLKQAEEEKVRQI 1727
Cdd:COG4913 836 FKELLNENSIEFVADL 851
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1654-2048 |
9.91e-04 |
|
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: 45.40 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1654 KAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAarqKQKALDELQKHKMQAEEAERRLKQAEEEKvRQIKVVEEV 1733
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAA---KAQVLEELESTKRLIEELKLNLERAQTEE-AQAKQDSEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1734 AQktaaTQLQAMsfsekttklEESLKKEQGTVLQLQEEAEKLRKQE--EEANKAREqaekELETWRLKANEALRLRLRAE 1811
Cdd:pfam05701 103 AK----LRVEEM---------EQGIADEASVAAKAQLEVAKARHAAavAELKSVKE----ELESLRKEYASLVSERDIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1812 EEAQRKSLAQEEAEKQKTEAerdakkkakaeeaalKQKENAEKE-LEKQRTFAEQIAQQKLSA----EQEYIRLKADFEH 1886
Cdd:pfam05701 166 KRAEEAVSASKEIEKTVEEL---------------TIELIATKEsLESAHAAHLEAEEHRIGAalarEQDKLNWEKELKQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1887 AEQqrglldnELQRLKNEVNAAEKQRRQLE---DELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLL-ETEALKMKQLA 1962
Cdd:pfam05701 231 AEE-------ELQRLNQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIqAALASAKKELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1963 E----------EAARLRSVAE--EAKKQRQLAEDEAARQRAEAEKILKEKLAAinEATRLKTEAEVA-LKAKEAENERLK 2029
Cdd:pfam05701 304 EvkaniekakdEVNCLRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVqAKEKEAREKMVE 381
|
410 420
....*....|....*....|....
gi 1655220517 2030 -----RQAEDEAYQRKLLEdQAAQ 2048
Cdd:pfam05701 382 lpkqlQQAAQEAEEAKSLA-QAAR 404
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2465-2771 |
1.02e-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: 45.58 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2465 LKEKMQAI-QEATKLKAEAEELQ---KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEA-ERK---RQLEISAEAE 2536
Cdd:pfam10174 329 LKESLTAKeQRAAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVkERKinvLQKKIENLQE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2537 KLKLRVKELSSAQAKAEEEATRfKKQADEAKVRLQE--TEKqttETVVQKLETQRLQSTR----EADDLKKAIAELEKER 2610
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTD-SSNTDTALTTLEEalSEK---ERIIERLKEQREREDRerleELESLKKENKDLKEKV 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2611 EKLKRDAQELQ---NKSKETASAQQEQMEQQKAMLQQTfltEKELLLKRER--DVEDEKKKLQKHLEDE------VNKAK 2679
Cdd:pfam10174 485 SALQPELTEKEsslIDLKEHASSLASSGLKKDSKLKSL---EIAVEQKKEEcsKLENQLKKAHNAEEAVrtnpeiNDRIR 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2680 ALKDEQQRQQklmdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEKllaDENKKLREKLESLEVTSKQA 2759
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMK---EQNKKVANIKHGQQEMKKKG 634
|
330
....*....|..
gi 1655220517 2760 ASKTKEIEVQTD 2771
Cdd:pfam10174 635 AQLLEEARRRED 646
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1416-2081 |
1.02e-03 |
|
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: 45.81 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1416 KKLLEEIEKNKDQIENCQKDAKAYIDSLKDyefQILAYRALQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTS 1495
Cdd:TIGR01612 1121 KNLDQKIDHHIKALEEIKKKSENYIDEIKA---QINDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLN 1197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1496 QyIKFILETQRRLEDDEKASEKLKEDEKKRMAEiqaQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQrQGLAVDA 1575
Cdd:TIGR01612 1198 E-IAEIEKDKTSLEEVKGINLSYGKNLGKLFLE---KIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENE-MGIEMDI 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQLE---------LTQLKNLSEQEIRSKNQQLEEAQVSrrklEEEIHLIRIQLQTTIKQKSTADDELQKLRDQA 1646
Cdd:TIGR01612 1273 KAEMETFNIShdddkdhhiISKKHDENISDIREKSLKIIEDFSE----ESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1647 AEAEKVRK--AAQEEAERLRKQVNEETQKKKNAEDELkrkSEAEKEAARQKQKALDELQKHKMQA-------EEAERRLK 1717
Cdd:TIGR01612 1349 ANIYNILKlnKIKKIIDEVKEYTKEIEENNKNIKDEL---DKSEKLIKKIKDDINLEECKSKIEStlddkdiDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1718 Q------AEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGT------VLQLQEEAEKLRKQEEEANKA 1785
Cdd:TIGR01612 1426 ElknhilSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATndhdfnINELKEHIDKSKGCKDEADKN 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1786 REQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQkteaerdakkkakaeeaalkQKENAEKELEKQRTFAEQ 1865
Cdd:TIGR01612 1506 AKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSE--------------------IIIKEIKDAHKKFILEAE 1565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1866 IAQQKlsaeqeyirlkadfehaeqqrglldnelqrlkneVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKvsqsnte 1945
Cdd:TIGR01612 1566 KSEQK----------------------------------IKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLEN------- 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1946 kskqlLETEALKMKQLAEEAARLRSVAEEAKKqrQLAEDEAARQRAEaekiLKEKLAAINEatrLKTEAEvALKAKEAEN 2025
Cdd:TIGR01612 1605 -----FENKFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDTE----LKENGDNLNS---LQEFLE-SLKDQKKNI 1669
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2026 ERLKRQAEDEAYQRKLLEDQAAQHKHD----IQEKITQLQSSSVSELDRQKNIVEETLRQ 2081
Cdd:TIGR01612 1670 EDKKKELDELDSEIEKIEIDVDQHKKNyeigIIEKIKEIAIANKEEIESIKELIEPTIEN 1729
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2399-2583 |
1.03e-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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2399 RIEEENLRLMQKNKDNTQKLLAEEAEKMKslaEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKL 2478
Cdd:pfam15709 347 RLEVERKRREQEEQRRLQQEQLERAEKMR---EELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2479 KAEA---EELQKQKNQAQEKAKKLLEDKqeiQQRLDKETQgfqksLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEE 2555
Cdd:pfam15709 424 QQEEfrrKLQELQRKKQQEEAERAEAEK---QRQKELEMQ-----LAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*...
gi 1655220517 2556 ATRfKKQADEAKVRLQETEKQTTETVVQ 2583
Cdd:pfam15709 496 ERR-QKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1650-1807 |
1.04e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1650 EKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQkaldELQKHKMQAEEAERRLKQAEEEKVRQIkv 1729
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKE----ELEEKKEKLQEEEDKLLEEAEKEAQQA-- 578
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1730 VEEvAQKTAATQLQAMSFSEkttKLEESLKKEQgtvlQLQEEAEKLRKQEEEANKarEQAEKELETWRLKANEALRLR 1807
Cdd:PRK00409 579 IKE-AKKEADEIIKELRQLQ---KGGYASVKAH----ELIEARKRLNKANEKKEK--KKKKQKEKQEELKVGDEVKYL 646
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2318-2575 |
1.09e-03 |
|
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: 45.39 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2318 AEMAKHKKEAEQalKQKSQVEKEL--------GLVKLQLDETDKQKALMDEELQRVKAQV---NDAVKQ-KAQVENE--- 2382
Cdd:NF033838 142 AEATKKVEEAEK--KAKDQKEEDRrnyptntyKTLELEIAESDVEVKKAELELVKEEAKEprdEEKIKQaKAKVESKkae 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2383 ---LSKVKMQMDELL-KLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQR 2458
Cdd:NF033838 220 atrLEKIKTDREKAEeEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSSVGEETLPSPS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2459 ALAEKMLKEKMQAIQEATKlKAEAEELQKQKNQAQEKAKKL-LE------DKQEIQQRLDKETQgfQKSLEAERKRQLEI 2531
Cdd:NF033838 300 LKPEKKVAEAEKKVEEAKK-KAKDQKEEDRRNYPTNTYKTLeLEiaesdvKVKEAELELVKEEA--KEPRNEEKIKQAKA 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1655220517 2532 SAEAEKLK-LRVKELSSAQAKAEEEATRfkKQADEAKVRLQETEK 2575
Cdd:NF033838 377 KVESKKAEaTRLEKIKTDRKKAEEEAKR--KAAEEDKVKEKPAEQ 419
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1759-1922 |
1.09e-03 |
|
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: 44.84 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1759 KKEQGTVLQLQEEAEKL---RKQEEE----------ANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLA----- 1820
Cdd:TIGR02794 64 KKEQERQKKLEQQAEEAekqRAAEQArqkeleqraaAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAeaerk 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1821 -QEEAEKQKtEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRglldnelq 1899
Cdd:TIGR02794 144 aKEEAAKQA-EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAE-------- 214
|
170 180
....*....|....*....|...
gi 1655220517 1900 RLKNEVNAAEKQRRQLEDELAKV 1922
Cdd:TIGR02794 215 AEAAAAAAAEAERKADEAELGDI 237
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
2403-2776 |
1.10e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 45.05 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2403 ENLRLMQKNKDNTQKLLAEEA----EKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQA----IQE 2474
Cdd:pfam15070 4 ESLKQLQTERDQYAENLKEEGavwqQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPpagpSEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2475 ATKLKAEAEELQKQKNQAQEKAKKLLEDKQEIQqRLDKETQgfQKSLEAERkrQLEISAEAEKLKLRVkeLSSAQAkaeE 2554
Cdd:pfam15070 84 EQRLQEEAEQLQKELEALAGQLQAQVQDNEQLS-RLNQEQE--QRLLELER--AAERWGEQAEDRKQI--LEDMQS---D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EAT--RFKKQADEAKVRLQETEKQTTETVVQKLE-TQRLQSTREA-DDLKKAIAELEKEREKLKrdaQELQNKSKEtASA 2630
Cdd:pfam15070 154 RATisRALSQNRELKEQLAELQNGFVKLTNENMElTSALQSEQHVkKELAKKLGQLQEELGELK---ETLELKSQE-AQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2631 QQEQMEQQKAMLQQ------TFLTEKELLLKRERDVEDEKKKLQ-KHLEDEVNKAKALKDEQQRQQKL--MDEEKKKLQA 2701
Cdd:pfam15070 230 LQEQRDQYLAHLQQyvaayqQLASEKEELHKQYLLQTQLMDRLQhEEVQGKVAAEMARQELQETQERLeaLTQQNQQLQA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2702 -----------------IMDEAVKKQKEAEAEMKNKQKEMEA--------LEKKRLEQEKLLADENKKLREKLESLEVTS 2756
Cdd:pfam15070 310 qlsllanpgegdgleseEEEEEAPRPSLSIPEDFESREAMVAffnsalaqAEEERAELRRQLKEQKRRCRRLAQQAAPAQ 389
|
410 420
....*....|....*....|
gi 1655220517 2757 KQAASKTKEIEVQTDKVPEE 2776
Cdd:pfam15070 390 EEPEHEAHAPGTGGDSVPVE 409
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2164-2342 |
1.14e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKA-AEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKL 2242
Cdd:COG2268 199 RDARIAEAEAERETEIAiAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAERE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2243 AQAAETAKEKAEKEaallrqKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkeaeaeaakraaaeaAALKQKQEADAEMAK 2322
Cdd:COG2268 279 VQRQLEIAEREREI------ELQEKEAEREEAELEADVRKPAEAEKQA-----------------AEAEAEAEAEAIRAK 335
|
170 180
....*....|....*....|
gi 1655220517 2323 HKKEAEqALKQKSQVEKELG 2342
Cdd:COG2268 336 GLAEAE-GKRALAEAWNKLG 354
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1185-1776 |
1.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1185 QKTAEQMKVQSELEGLKKDLNSITEKTEEILASPQqsssapmlrseldvtlkkmdhvyglssvyldKLKTIDIVIRNTKD 1264
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEG-------------------------------SKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1265 AEDTVKSYESRLRDVSKVPAEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQL 1344
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1345 AGSLLERWQAVFAQIDLRQRELSLLGRhMNSYKQsyewliqwlREARLRQEKIEAAPVWDSKAlKEQLTQEkklLEEIEK 1424
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEE-LERLKK---------RLTGLTPEKLEKELEELEKA-KEEIEEE---ISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1425 NKDQIENCQKDAKAYIDSLK---------------DYEFQILA-YRALQDPIASPLKkpKMESASDNIIQEYVTLRTRYS 1488
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEeYTAELKRIEKELK--EIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1489 ELSTLTSQY--IKFILETQRRLE--DDEKASEKLKEDE--KKRMAEIQAQLETQKQLAEghaksvakaelEAQELKLKMK 1562
Cdd:PRK03918 491 KESELIKLKelAEQLKELEEKLKkyNLEELEKKAEEYEklKEKLIKLKGEIKSLKKELE-----------KLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1563 EDASQRQglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKSTADDELQKL 1642
Cdd:PRK03918 560 ELEKKLD----ELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1643 RDQAAEAEKVRKaaqeEAERLRKQVNEETQKKKNAE-----DELKRKSEAEKEAARQKQ---KALDELQKHKMQAEEAER 1714
Cdd:PRK03918 636 AETEKRLEELRK----ELEELEKKYSEEEYEELREEylelsRELAGLRAELEELEKRREeikKTLEKLKEELEEREKAKK 711
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 1715 RLKQAEEEKVRQIKVVEEVAQKTAATQLQAMS-FSEKTTKLEESLKKEQGTVLQLQEEAEKLR 1776
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSkVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
195-303 |
1.16e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 270
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1655220517 271 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 303
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
2498-2750 |
1.17e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.67 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRLDKETQgfqksleaeRKRQLEISAEAEKLKLRVKELSSAQAKA--EEEATRFKKQADEAKVRLQETEK 2575
Cdd:pfam15742 6 KLKYQQQEEVQQLRQNLQ---------RLQILCTSAEKELRYERGKNLDLKQHNSllQEENIKIKAELKQAQQKLLDSTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2576 QTT------ETVVQKLETQRLQSTREADDLKkAIAELEKEREKLKRDAQELQNKSKETasaqQEQMEQ-QKAMLQQTFLT 2648
Cdd:pfam15742 77 MCSsltaewKHCQQKIRELELEVLKQAQSIK-SQNSLQEKLAQEKSRVADAEEKILEL----QQKLEHaHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2649 EKELLLKRERDVEDEKKKLQKHLEdevnkakalkdEQQRQQKLMDEEKKKLQaiMDEAVKKQKEAEAEMKNKQ-----KE 2723
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQ-----------EEQQKRKLLDQNVNELQ--QQVRSLQDKEAQLEMTNSQqqlriQQ 218
|
250 260
....*....|....*....|....*..
gi 1655220517 2724 MEALEKKrLEQEKLLADENKKLREKLE 2750
Cdd:pfam15742 219 QEAQLKQ-LENEKRKSDEHLKSNQELS 244
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1518-1723 |
1.18e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 43.94 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1518 LKEDEKKRMAEIQAQ-LETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQE 1596
Cdd:pfam06008 33 SPENAHKIQIEILEKeLSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1597 IRSKNQQLEEAQVSRRKLEEEIhliriQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNeetQKKKN 1676
Cdd:pfam06008 113 FALPSSDLSRMLAEAQRMLGEI-----RSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALR---DSLAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655220517 1677 AEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEK 1723
Cdd:pfam06008 185 YEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQK 231
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1406-1791 |
1.18e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1406 KALKEQLTQEKKLLEEIEKNKDQIENCQKDakayidslkdyefqILAYRALQDPIASPLKKpKMESASDNiIQEYVTLrt 1485
Cdd:PRK04778 126 EELQELLESEEKNREEVEQLKDLYRELRKS--------------LLANRFSFGPALDELEK-QLENLEEE-FSQFVEL-- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1486 ryselsTLTSQYI---KFILETQRRLEDDEKASEKLKEDEKKRMAEIQAQLEtqkQLAEGHAKSVAKA--------ELEA 1554
Cdd:PRK04778 188 ------TESGDYVearEILDQLEEELAALEQIMEEIPELLKELQTELPDQLQ---ELKAGYRELVEEGyhldhldiEKEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1555 QELKLKMKEDASQRQGLAVD-AEKQKQNIQLELTQLKNLSEQEIRSKN----------QQLEEAQVSRRKLEEEIHLIR- 1622
Cdd:PRK04778 259 QDLKEQIDENLALLEELDLDeAEEKNEEIQERIDQLYDILEREVKARKyveknsdtlpDFLEHAKEQNKELKEEIDRVKq 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1623 --------IQLQTTI-KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVN--EETQKKKNaeDELK--RKSEAEk 1689
Cdd:PRK04778 339 sytlneseLESVRQLeKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEeiEKEQEKLS--EMLQglRKDELE- 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1690 eaARQKqkaLDELQ------KHKMQA--------------EEAERRLKQAEEEkVRQIKV-VEEVAQKTAATQLQAMSFS 1748
Cdd:PRK04778 416 --AREK---LERYRnklheiKRYLEKsnlpglpedylemfFEVSDEIEALAEE-LEEKPInMEAVNRLLEEATEDVETLE 489
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1655220517 1749 EKTTKLEESlkkeqgTVL--QLQEEAEKLRKQEEEANKAREQAEK 1791
Cdd:PRK04778 490 EETEELVEN------ATLteQLIQYANRYRSDNEEVAEALNEAER 528
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
337-418 |
1.22e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 41.52 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 337 RCDNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQ-AFSVAE--RELGVTRLLDPEdvDVAHPDEKSIITYV 413
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPE--DIVSGNPRLNLAFV 109
|
....*
gi 1655220517 414 SSLYD 418
Cdd:cd21218 110 ATLFN 114
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
255-299 |
1.24e-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: 41.66 E-value: 1.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1655220517 255 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 299
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1683-2036 |
1.25e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1683 RKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQ-AEEEKVRQIKvvEEVAQKTAATqLQAMSFSEKTTKLEESLKK- 1760
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSElALNEMIEKLK--KEIDLEYTEA-VIAMGLQERLENLREEFSKa 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1761 ---EQGTVLQLQEEAEKLrKQEEEANKAREQAEKELETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKK 1837
Cdd:PLN03229 499 nsqDQLMHPVLMEKIEKL-KDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIK 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1838 kakaeeaalkqkenaekelEKQRTFAEQIAQQKLSAEQEyirlkadfehaeqqrglLDNELqrlkneVNAAEKQRRQLED 1917
Cdd:PLN03229 578 -------------------EKMEALKAEVASSGASSGDE-----------------LDDDL------KEKVEKMKKEIEL 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1918 ELAKVRSEMDallqmkIQAEKVSQSNTEKSKQLLETE-ALKMKQLAEE----------AARLRSVAEEAKKQRQLA---E 1983
Cdd:PLN03229 616 ELAGVLKSMG------LEVIGVTKKNKDTAEQTPPPNlQEKIESLNEEinkkiervirSSDLKSKIELLKLEVAKAsktP 689
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 1984 DEAARQRAEA-EKILKEKLAAINEATRLKT-----EAEVALKAK--EAENERLKRQAEDEA 2036
Cdd:PLN03229 690 DVTEKEKIEAlEQQIKQKIAEALNSSELKEkfeelEAELAAAREtaAESNGSLKNDDDKEE 750
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1896-2059 |
1.32e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1896 NELQRlKNEVNAAEKQRRQledELAKVRSEMDalLQMKIQAEkvSQSNTEKSKQLLETEALKMKQLAEEAARLRSV---- 1971
Cdd:COG2268 206 AEAER-ETEIAIAQANREA---EEAELEQERE--IETARIAE--AEAELAKKKAEERREAETARAEAEAAYEIAEAnaer 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1972 -----AEEAKKQRQ--LAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEV-ALKAK---EAENERLKRQAEdEAYQRK 2040
Cdd:COG2268 278 evqrqLEIAEREREieLQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAeAIRAKglaEAEGKRALAEAW-NKLGDA 356
|
170
....*....|....*....
gi 1655220517 2041 LLEDQAAQHKHDIQEKITQ 2059
Cdd:COG2268 357 AILLMLIEKLPEIAEAAAK 375
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1555-1719 |
1.33e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1555 QELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKnlsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTTIKQKST 1634
Cdd:PRK00409 526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 AD------DELQKLRDQAAEAEKVRKAAQEEAERLR----------KQVNEETQKKKNAE--------------DELKRK 1684
Cdd:PRK00409 603 SVkaheliEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslGQKGEVLSIPDDKEaivqagimkmkvplSDLEKI 682
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1655220517 1685 SEAEKEAARQKQKALDELQK-------HKMQAEEAERRLKQA 1719
Cdd:PRK00409 683 QKPKKKKKKKPKTVKPKPRTvsleldlRGMRYEEALERLDKY 724
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1516-1831 |
1.40e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1516 EKLKEDEKKRMAEiQAQLETQKQLAEGHAKSVAKAELEAQElklkmKEDASQRQGlAVDAEKQKQniqleltqlknlseq 1595
Cdd:PRK07735 4 EKDLEDLKKEAAR-RAKEEARKRLVAKHGAEISKLEEENRE-----KEKALPKND-DMTIEEAKR--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1596 eiRSKNQQLEEAQVSRRKLEEEIhliriqlqttikqKSTADDELQKLRDQAAEAEKVRKAAqeeaerLRKQVNEETQKKK 1675
Cdd:PRK07735 62 --RAAAAAKAKAAALAKQKREGT-------------EEVTEEEKAKAKAKAAAAAKAKAAA------LAKQKREGTEEVT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1676 naEDELKRKSEAEKEAARQKQKALDElqkhkmQAEEAERRLKQAEEEKvrqikvVEEVAQKTAATQLQAMSFSEKTTKLE 1755
Cdd:PRK07735 121 --EEEKAAAKAKAAAAAKAKAAALAK------QKREGTEEVTEEEEET------DKEKAKAKAAAAAKAKAAALAKQKAA 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1756 ESlkkEQGTVLQLQEEAEKLRKQEEEANKAREQA-----------EKELETWRLKANEALRLRLRAEEEAQRKSLAQEEA 1824
Cdd:PRK07735 187 EA---GEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakqkasqgngDSGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKE 263
|
....*..
gi 1655220517 1825 EKQKTEA 1831
Cdd:PRK07735 264 EEPKQEE 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
2419-2546 |
1.41e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLAEEAARLSVEAEETARQRKtaEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKK 2498
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEE--EEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1655220517 2499 LLEDKQEIqQRLDKETQGFQKSLEAERKRQLEISAEAEKLK-LRVKELS 2546
Cdd:COG2433 460 EIRKDREI-SRLDREIERLERELEEERERIEELKRKLERLKeLWKLEHS 507
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
202-299 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 202 QKKTFTKWVNKHL---------MKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 267
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1655220517 268 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 299
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2419-2532 |
1.46e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.94 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAE---KMLKEKMQAIQEATkLKAEAEELQKQKNQAQEK 2495
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEekqQELEAQLEQLQEKA-AETSQERKQKRKEITDQA 225
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2496 AKKLLEDKQE----IQQRL-------DKETQGFQKSLEAERKRQLEIS 2532
Cdd:PRK11448 226 AKRLELSEEEtrilIDQQLrkagweaDSKTLRFSKGARPEKGRNLAIA 273
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1888-2486 |
1.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1888 EQQRGLLDN--------ELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLEtealkmk 1959
Cdd:PRK02224 183 SDQRGSLDQlkaqieekEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELET------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1960 qLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEklaaiNEATRLKTEAEvalkakEAENERLKRQAEDEAYQR 2039
Cdd:PRK02224 256 -LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEE-----RDDLLAEAGLD------DADAEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2040 KLLEDQAAQHKHDIQEKITQLqsssvseldrqkniveETLRqkkvveEEIHIIRINFERASKEKSDLEVELKKLKGIADE 2119
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEA----------------ESLR------EDADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2120 TQkskakaeeeaeklkKLAAEEERKRREAEEKVKKIAAAEEEAARQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVI 2199
Cdd:PRK02224 382 RR--------------EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2200 LAkeAAQKSTAAEQKAQD--VLSKNKEDLLSQEKLRDEFENAKklaqaaetakekaeKEAALLRQKAEEAEKLKKaAEDE 2277
Cdd:PRK02224 448 LL--EAGKCPECGQPVEGspHVETIEEDRERVEELEAELEDLE--------------EEVEEVEERLERAEDLVE-AEDR 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2278 AAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEqalKQKSQVEKELGLVKlqldETDKQKAL 2357
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA---EAEEEAEEAREEVA----ELNSKLAE 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2358 MDEELQRvkaqvndavkqkaqveneLSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK--LLAEEAEKMKSLAEEaar 2435
Cdd:PRK02224 584 LKERIES------------------LERIRTLLAAIADAEDEIERLREKREALAELNDERreRLAEKRERKRELEAE--- 642
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2436 LSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQ-EATKLKAEAEELQ 2486
Cdd:PRK02224 643 FDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQaEIGAVENELEELE 694
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
2527-2644 |
1.55e-03 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 44.68 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2527 RQLEISAEAEKLKlrvKELSSAQAKAEEEATRFKKQADEAKVrLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAEL 2606
Cdd:PTZ00186 537 RDSEQHAEADRVK---RELVEVRNNAETQLTTAERQLGEWKY-VSDAEKENVKTLVAELRKAMENPNVAKDDLAAATDKL 612
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220517 2607 EKE-----REKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ 2644
Cdd:PTZ00186 613 QKAvmecgRTEYQQAAAANSGSSSNSGEQQQQQQQQQQQNSEE 655
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2497-2736 |
1.60e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2497 KKLLEDKQEIQ--QRLDKetqgFQKSLEAERKRQL-----EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVR 2569
Cdd:PHA02562 153 RKLVEDLLDISvlSEMDK----LNKDKIRELNQQIqtldmKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2570 LQETEKQTTEtvvqkLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSK-----ETASAQQEQMEQQKAMLQ- 2643
Cdd:PHA02562 229 AKTIKAEIEE-----LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekgGVCPTCTQQISEGPDRITk 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2644 -QTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKALKD--EQQRQQ-KLMDEEKKKLQAIMDEAVKKQKEAEAEMKN 2719
Cdd:PHA02562 304 iKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNkiSTNKQSlITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
|
250
....*....|....*....
gi 1655220517 2720 KQKEMEALEKKR--LEQEK 2736
Cdd:PHA02562 384 LQDELDKIVKTKseLVKEK 402
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2187-2571 |
1.63e-03 |
|
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: 44.75 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2187 KDKAEKELEKQVILAKEAAQKSTAAEQKAQdvlSKNKEDLLSQEKLRDEFENAKKLAQAAETAKEKAEKEAallrQKAEE 2266
Cdd:pfam09731 78 ESKEPKEEKKQVKIPRQSGVSSEVAEEEKE---ATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESAT----AVAKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2267 AEKLKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQEADAEMAKHKKEAEQALKQKSQVEK---ELGL 2343
Cdd:pfam09731 151 AKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKlpeHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2344 VKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKV-----KMQMDELLKLkvrIEEENLRLMQKNKDNTQKL 2418
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVlkednLLSNDDLNSL---IAHAHREIDQLSKKLAELK 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLAEEAARLSVEAEETARQrktAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAeELQKQKNQAQEKAKK 2498
Cdd:pfam09731 308 KREEKHIERALEKQKEELDKLAEELSAR---LEEVRAADEAQLRLEFEREREEIRESYEEKLRT-ELERQAEAHEEHLKD 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2499 -LLEDKQEIQQRLDKEtqgFQKSLEAERKRQLEisaEAEKLKLRVKELssaqakaeEEATRFKKQADEAKVRLQ 2571
Cdd:pfam09731 384 vLVEQEIELQREFLQD---IKEKVEEERAGRLL---KLNELLANLKGL--------EKATSSHSEVEDENRKAQ 443
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1637-1705 |
1.69e-03 |
|
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: 42.08 E-value: 1.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1637 DELQKLRDQA----AEAEKVRKAAQEEAERLRKQVNEETQK-----KKNAEDELKR-KSEAEKEAARQKQKALDELQKH 1705
Cdd:COG0711 41 AEAERAKEEAeaalAEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELRAE 119
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1503-1722 |
1.70e-03 |
|
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: 44.07 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQL--AEGHAKSVAKAELEAQELKLKMKEDASQRQglAVDAEKQKQ 1580
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 niqlelTQLKNLSEQEirsknQQLEEAQVSRRKLEEeihliriqlqttIKQKSTADDELQKLRDQAAEAEKvrkaAQEEA 1660
Cdd:TIGR02794 146 ------EEAAKQAEEE-----AKAKAAAEAKKKAEE------------AKKKAEAEAKAKAEAEAKAKAEE----AKAKA 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 1661 ERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEE 1722
Cdd:TIGR02794 199 EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2260-2428 |
1.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2260 LRQKAEEAEKLKKAAEDEAAKQaKAQKDAERlrkeaeaeaakraaaeaaaLKQKQEADAEMAKHKKEAEQALKQKSQVEK 2339
Cdd:PRK00409 539 AEALLKEAEKLKEELEEKKEKL-QEEEDKLL-------------------EEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2340 ELGL-VKLQlDETDKQKALMD-----EELQRVKAQVNDAVK-----------QKAQVeneLSKVK-----MQMDeLLKLK 2397
Cdd:PRK00409 599 GGYAsVKAH-ELIEARKRLNKanekkEKKKKKQKEKQEELKvgdevkylslgQKGEV---LSIPDdkeaiVQAG-IMKMK 673
|
170 180 190
....*....|....*....|....*....|.
gi 1655220517 2398 VRIEEenLRLMQKNKDNTQKLLAEEAEKMKS 2428
Cdd:PRK00409 674 VPLSD--LEKIQKPKKKKKKKPKTVKPKPRT 702
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
197-305 |
1.71e-03 |
|
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: 41.51 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 197 ERDRVQKKTFTKWVNKhlMKAQRHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 267
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655220517 268 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 305
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1630-1704 |
1.77e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.91 E-value: 1.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 1630 KQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAedelkRKSEAEKEAARQKQKALDELQK 1704
Cdd:PRK07353 54 EAEKLEAQYEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAEAQA-----SKEKARREIEQQKQAALAQLEQ 123
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1731-1912 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1731 EEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRLRLRA 1810
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1811 E--------------------------------EEAQRKSL-----AQEEAEKQKTEAERDAKKKAKAEEAALKQKENAE 1853
Cdd:COG3883 95 LyrsggsvsyldvllgsesfsdfldrlsalskiADADADLLeelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1854 KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQR 1912
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2508-2667 |
1.88e-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: 43.37 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2508 QRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ----TTETVVQ 2583
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2584 KLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDE 2663
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
....
gi 1655220517 2664 KKKL 2667
Cdd:COG1579 173 PPEL 176
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2420-2739 |
1.92e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2420 AEEAEKMKSlAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAKKL 2499
Cdd:COG3064 1 AQEALEEKA-AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2500 LE---DKQEIQQRLDKETQgfQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQ 2576
Cdd:COG3064 80 AEaekAAAEAEKKAAAEKA--KAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2577 TTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKR 2656
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2657 ERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALEKKRLEQEK 2736
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
...
gi 1655220517 2737 LLA 2739
Cdd:COG3064 318 LAA 320
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1986-2226 |
1.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1986 AARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSv 2065
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2066 SELDRQKNIVEETLRqkkVVEEEIHIIRINFERASKEKSDLEVELKKLKGIADETQKSKAKAEEEAEKLKKLAAEEERKR 2145
Cdd:COG4942 97 AELEAQKEELAELLR---ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2146 REAEEKVKKIAAAEEEAARQRKAAQDEVERL-KQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKE 2224
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 1655220517 2225 DL 2226
Cdd:COG4942 254 KL 255
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1639-1834 |
1.97e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1639 LQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQkkknaeDELKRKSEAEKEAARQKQKALDelqkhkmqaeEAERRLKQ 1718
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAK------ELLLRERNQQRQEARREREELQ----------REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1719 AEEekvrqikvveevaqktaatQLQAMsfSEKTTKLEEslkkeqgtvlQLQEEAEKLRKQEEEANKAREQAEKEL-ETWR 1797
Cdd:PRK12705 89 KEE-------------------QLDAR--AEKLDNLEN----------QLEEREKALSARELELEELEKQLDNELyRVAG 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655220517 1798 LKANEALRL---RLRAEEEAQRKSLAQEEAEKQKTEAERD 1834
Cdd:PRK12705 138 LTPEQARKLllkLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1418-1722 |
2.18e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.54 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1418 LLEEIEKNKDQIEncqkdakAYIDS-----LKDYEFQILAYrALQDPIASPL---KKPKMESASDNIIQEyvtlRTRYSE 1489
Cdd:PLN03188 991 LLEEIQDLRSQLQ-------YYIDSslpsaRKRNSLLKLTY-SCEPSQAPPLntiPESTDESPEKKLEQE----RLRWTE 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1490 LStltSQYIKFILETQRRLEDDEKASEKLKE--DEKKRMAEiqaQLETQKQLA-EGHAKSVAK-AELEAQELKL-----K 1560
Cdd:PLN03188 1059 AE---SKWISLAEELRTELDASRALAEKQKHelDTEKRCAE---ELKEAMQMAmEGHARMLEQyADLEEKHIQLlarhrR 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1561 MKE------DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEirsknqqleeaqvsRRKLEEEIHLIRIQLQTTIKQKST 1634
Cdd:PLN03188 1133 IQEgiddvkKAAARAGVRGAESKFINALAAEISALKVEREKE--------------RRYLRDENKSLQAQLRDTAEAVQA 1198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1635 ADDELQKLRDQ---AAEAEKVRKAAQEEAERLRKQVNeetQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEE 1711
Cdd:PLN03188 1199 AGELLVRLKEAeeaLTVAQKRAMDAEQEAAEAYKQID---KLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCMAKYD 1275
|
330
....*....|.
gi 1655220517 1712 AERRLKQAEEE 1722
Cdd:PLN03188 1276 AGEPLSEGDQQ 1286
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1635-1711 |
2.19e-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: 2.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 1635 ADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNaedelKRKSEAEKEAARQKQKALDELQKHKMQAEE 1711
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE-----EILAEAKEEAERILEQAKAEIEQEKEKALA 113
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2322-2622 |
2.23e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.40 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2322 KHKKEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIE 2401
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2402 EENLRLMQKNKdntqKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQralaEKMLKEKMQAIQEATKLKAE 2481
Cdd:pfam09728 81 KQNKKLKEESK----KLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREE----NEELREKLKSLIEQYELREL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2482 -------AEELQKQKNQAqeKAKKLLEDKQEIQQ-----RLDKETQGFQKSLEAERKRQLEISAEAEKLKlrvkELSSAQ 2549
Cdd:pfam09728 153 hfekllkTKELEVQLAEA--KLQQATEEEEKKAQekevaKARELKAQVQTLSETEKELREQLNLYVEKFE----EFQDTL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2550 AKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQR--LQSTREADDLKKAIAELEKEREKLKRDAQELQN 2622
Cdd:pfam09728 227 NKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKalLEMAEERQKLKEELEKLQKKLEKLENLCRALQA 301
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1560-1817 |
2.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1560 KMKEDASQRQGLAVDAEKQKQNIQLELTqlknlsEQEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTTIKQKSTADDEL 1639
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEE------EEEIRRLEEQVERLEAEVEELEAELE----EKDERIERLERELSEA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1640 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQ---KALDELQKhkmqaeEAERRL 1716
Cdd:COG2433 454 RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELvpvKVVEKFTK------EAIRRL 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1717 KQAEEEKVRQIKVVEEV--AQKTAATQL-----QAMSFSEKT-TKLEESLKKEQGTVL-----QLQEEAEKLRKQEEEAN 1783
Cdd:COG2433 528 EEEYGLKEGDVVYLRDAsgAGRSTAELLaeagpRAVIVPGELsEAADEVLFEEGIPVLpaedvTIQEVDDLAVVDEEELE 607
|
250 260 270
....*....|....*....|....*....|....
gi 1655220517 1784 KAREQAEKELETWRLKANEALRLRLRAEEEAQRK 1817
Cdd:COG2433 608 AAIEDWEERAEERRREKKAEMLERLISEYRAERR 641
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1784-1945 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1784 KAREQAEKELETWR----LKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERdAKKKAKAEEAALKQKENAEKELEKQ 1859
Cdd:pfam05262 185 ALREDNEKGVNFRRdmtdLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADF-AQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1860 RTFAEQIAQQKLSAEQEYIRLKADFE---HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQA 1936
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEikkNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ-KTKP 342
|
....*....
gi 1655220517 1937 EKVSQSNTE 1945
Cdd:pfam05262 343 QVEAQPTSL 351
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
2425-2645 |
2.33e-03 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 44.18 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2425 KMKSLAEEAARLSVEAEETARQRKTAEAELAE-------QRALA--EKMLKEKMQAIQEATKLK---------AEAEELQ 2486
Cdd:PTZ00332 138 KMEKVEEELRRSQLDATQLAQVPTATLKNIEDimnvtqiQNALAstDDQIKTQLAQLEKTNEIQnvamhdgemQVAEEQM 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2487 KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKRQLEiSAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEA 2566
Cdd:PTZ00332 218 WTKVQLQERLIELVADKFRLIGKCEEENKSFSKIHEVQKQANQE-TSQMKDAKRRLKQRCETDLKHIHDAIQKADLEDAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2567 KVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKER-EKLKRDAQELQNKSKETASAQQ--EQMEQQKAMLQ 2643
Cdd:PTZ00332 297 AMKRYATNKEKSERFIRENEDRQEEAWNKIQDLERQLQRLGTERfEEVKRRIEENDREEKRRVEYQQflEVAGQHKKLLE 376
|
..
gi 1655220517 2644 QT 2645
Cdd:PTZ00332 377 LT 378
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1408-1638 |
2.34e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1408 LKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYidsLKDYEFQILAYRALQdpIASPLKKPKMEsaSDNIIQEYVTLRTRY 1487
Cdd:TIGR01612 1488 LKEHIDKSKGCKDEADKNAKAIEKNKELFEQY---KKDVTELLNKYSALA--IKNKFAKTKKD--SEIIIKEIKDAHKKF 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1488 SELSTLTSQYIKFILETQRRLEDDEKASEK-----------LKEDEKK--RMAEIQAQLETQKQLAEGHAKSVAKAELEA 1554
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKsnkaaidiqlsLENFENKflKISDIKKKINDCLKETESIEKKISSFSIDS 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1555 QELKLKMKEDASQR-QGLAVDAEKQKQNIQLELTQLKNLsEQEIRS---------KNQQL-------EEAQVSRRKLEEE 1617
Cdd:TIGR01612 1641 QDTELKENGDNLNSlQEFLESLKDQKKNIEDKKKELDEL-DSEIEKieidvdqhkKNYEIgiiekikEIAIANKEEIESI 1719
|
250 260
....*....|....*....|.
gi 1655220517 1618 IHLIRIQLQTTIKQKSTADDE 1638
Cdd:TIGR01612 1720 KELIEPTIENLISSFNTNDLE 1740
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1502-1728 |
2.36e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 44.05 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1502 LETQRRLEDDEKASE---KLKEDEKKRMAEIQ---------------AQLETQKQlaEGHAKSVAKAELEAQEL---KLK 1560
Cdd:pfam15066 304 FESLQPLEEDMALNEvlqKLKHTNRKQQMQIQdlqcsnlylekkvkeLQMKITKQ--QVFVDIINKLKENVEELiedKYN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1561 MKEDASqrqglavDAEKQKQNIQLELTQLKNLSEQEIRSKNQ-QLEEAQVsrrkleeEIHLIRIQLQ--TTIKQKStadd 1637
Cdd:pfam15066 382 VILEKN-------DINKTLQNLQEILANTQKHLQESRKEKETlQLELKKI-------KVNYVHLQERyiTEMQQKN---- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1638 elqKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRkseaEKEAARQKQKAL-DELQKHKMQAEEAERRL 1716
Cdd:pfam15066 444 ---KSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTSALDLLKR----EKETREQEFLSLqEEFQKHEKENLEERQKL 516
|
250
....*....|..
gi 1655220517 1717 KQAEEEKVRQIK 1728
Cdd:pfam15066 517 KSRLEKLVAQVK 528
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1646-2110 |
2.38e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1646 AAEAEKVRKAAQEEAERLRKQvneETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAEEEKVR 1725
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQA---EAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1726 QIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANEALR 1805
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1806 LRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFE 1885
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1886 HAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEA 1965
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1966 ARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKLLEDQ 2045
Cdd:COG3064 318 LAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 2046 AAQHKHDIQEKITQLQSSSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEKSDLEVEL 2110
Cdd:COG3064 398 GGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADAL 462
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2325-2701 |
2.40e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2325 KEAEQALKQKSQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVND--AVKQKAQVENELSkvkmQMDELLKLKVRIEE 2402
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDecWKKIKRKKNSALS----EALNGFKYEANFKS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2403 ENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEqrALAEKMLKeKMQAIQEATKLKAEA 2482
Cdd:pfam13166 165 RLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAE--ILIQKVIG-KSSAIEELIKNPDLA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2483 EELQkqknQAQEKAKKLLED----KQEIQQRL--------DKETQGFQKSLEaERKRQLE--ISAEAEKLKLRVKELSSA 2548
Cdd:pfam13166 242 DWVE----QGLELHKAHLDTcpfcGQPLPAERkaaleahfDDEFTEFQNRLQ-KLIEKVEsaISSLLAQLPAVSDLASLL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2549 QAkaeeeatrFKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADdLKKAIAELEKEREKLKRdAQELQNKSKETA 2628
Cdd:pfam13166 317 SA--------FELDVEDIESEAEVLNSQL-DGLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVAS-INELIAKHNEIT 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2629 SAQQEQMEQQKAMLQQTFLTEkellLKRERDVEDEKKKLqkhLEDEVNKAKALKDEQQRQQKLMDEEKKKLQA 2701
Cdd:pfam13166 386 DNFEEEKNKAKKKLRLHLVEE----FKSEIDEYKDKYAG---LEKAINSLEKEIKNLEAEIKKLREEIKELEA 451
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1865-2036 |
2.44e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1865 QIAQQKLSAEQEYIRlkadFEhAEQQRgLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDAllQMKIQAEKVSQSNT 1944
Cdd:PRK05035 440 AIEQEKKKAEEAKAR----FE-ARQAR-LEREKAAREARHKKAAEARAAKDKDAVAAALARVKA--KKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1945 EKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQlAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAE 2024
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK 590
|
170
....*....|..
gi 1655220517 2025 NERLKRQAEDEA 2036
Cdd:PRK05035 591 AKKAAQQAASAE 602
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1284-1442 |
2.46e-03 |
|
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: 42.82 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1284 AEEKEVEAHRSQLKAMRAEAEADQATFDRLQDELKAATSVSDKMTRLHSERDAELEHYRQlagSLLERWQAVFAQIDLRQ 1363
Cdd:cd00176 23 LSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLE---ELNQRWEELRELAEERR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1364 RELSLLGRHMNSYKQSYEwLIQWLREARLRQEKIEAAPvwDSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDS 1442
Cdd:cd00176 100 QRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEE 175
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3180-3217 |
2.49e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.49e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 3180 LQGTPSIAGLLNEPTKEKMSFYQAMKKELLSPEAAVNL 3217
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
2396-2639 |
2.50e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2396 LKVRIEEENLRLMQKNKDNTQKLLA---EEAEKMKSLAEEAARLSVEAEETARQRktAEAELAEqralAEKMLKEKMQAI 2472
Cdd:PRK05771 36 LKEELSNERLRKLRSLLTKLSEALDklrSYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEK----IEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2473 QEatkLKAEAEELQKQKNQAqEKAKKLledkqeiqqrldketqgfqkSLEAERKRQLE--------ISAEAEKLKLRVKE 2544
Cdd:PRK05771 110 SE---LENEIKELEQEIERL-EPWGNF--------------------DLDLSLLLGFKyvsvfvgtVPEDKLEELKLESD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 LSSAQAKAEEEATRF------KKQADEAKVRLQETEkqttetvVQKLETQRLQSTREA-DDLKKAIAELEKEREKLKRDA 2617
Cdd:PRK05771 166 VENVEYISTDKGYVYvvvvvlKELSDEVEEELKKLG-------FERLELEEEGTPSELiREIKEELEEIEKERESLLEEL 238
|
250 260
....*....|....*....|..
gi 1655220517 2618 QELQNKSKETASAQQEQMEQQK 2639
Cdd:PRK05771 239 KELAKKYLEELLALYEYLEIEL 260
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1516-1728 |
2.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1516 EKLKEDEKKRmAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAV------DAEKQKQNIQLELTQL 1589
Cdd:COG1340 57 EEAQELREKR-DELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeieRLEWRQQTEVLSPEEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1590 KNLSEQeIRSKNQQLEEAQVSRrKLEEEIHLIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNE 1669
Cdd:COG1340 136 KELVEK-IKELEKELEKAKKAL-EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADE 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1670 ETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQAE-EEKVRQIK 1728
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEElEEKAEEIF 273
|
|
| CortBP2 |
pfam09727 |
Cortactin-binding protein-2; This entry is the first approximately 250 residues of ... |
1564-1706 |
2.61e-03 |
|
Cortactin-binding protein-2; This entry is the first approximately 250 residues of cortactin-binding protein 2. In addition to being a positional candidate for autism this protein is expressed at highest levels in the brain in humans. The human protein has six associated ankyrin repeat domains pfam00023 towards the C-terminus which act as protein-protein interaction domains.
Pssm-ID: 462860 [Multi-domain] Cd Length: 187 Bit Score: 42.20 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1564 DASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKN---QQLEEAQVSRRKLEEEIhliriqlqttikqkstaDDELQ 1640
Cdd:pfam09727 57 DSELLRDQSQDEDVYEAMYEKPLAELEKLVEKQRETQRrmlEQLAAAEKRHRRVIREL-----------------EEEKR 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 1641 KLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSE-AEKEAARQKQKALDELQKHK 1706
Cdd:pfam09727 120 KHARDTAQGDDFTYLLEKERERLKQELEQEKAQQKRLEKELKKLLEkLEEELSKQKQIALLLVKERK 186
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1503-2098 |
2.69e-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: 44.04 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1503 ETQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAK--AELEAQELKLKMKEDASQRQGLAVDAEKQKQ 1580
Cdd:pfam10174 116 ENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKllEMLQSKGLPKKSGEEDWERTRRIAEAEMQLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1581 NIQLELTQLKnlseqeirSKNQQLEEAQVSRRKLEEEIHLIRiQLQTTIKQKSTADDELQK-LRDQAAEAEKVRKAA--- 1656
Cdd:pfam10174 196 HLEVLLDQKE--------KENIHLREELHRRNQLQPDPAKTK-ALQTVIEMKDTKISSLERnIRDLEDEVQMLKTNGllh 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1657 QEEAERLRKQV---NEETQKKKNAEDELKR---KSEAEKEAARQKQKALD----------ELQKHKMQAEEAERRLKQAE 1720
Cdd:pfam10174 267 TEDREEEIKQMevyKSHSKFMKNKIDQLKQelsKKESELLALQTKLETLTnqnsdckqhiEVLKESLTAKEQRAAILQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1721 EEKVRQIKVVEEVAQKTAATQLQAMSfSEKTT------KLEESLKKEQGTVLQLQEEAEKLRKQEEEANKARE---QAEK 1791
Cdd:pfam10174 347 VDALRLRLEEKESFLNKKTKQLQDLT-EEKSTlageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAglkERVK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1792 ELETWRLKANEAlrlrLRAEEEAqrksLAQEE--AEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTfaeqiaqQ 1869
Cdd:pfam10174 426 SLQTDSSNTDTA----LTTLEEA----LSEKEriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQP-------E 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1870 KLSAEQEYIRLKadfEHAEQQRGLLDNELQRLKnevnaaekqrrQLEDELAKVRSEMDALlqmkiQAEKVSQSNTEKSKQ 1949
Cdd:pfam10174 491 LTEKESSLIDLK---EHASSLASSGLKKDSKLK-----------SLEIAVEQKKEECSKL-----ENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1950 LLETEALKMKQLAEEAARLRSvaEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRL---KTEAEVALKAKEAENE 2026
Cdd:pfam10174 552 TNPEINDRIRLLEQEVARYKE--ESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLrqmKEQNKKVANIKHGQQE 629
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655220517 2027 RLKRQAEDEAYQRKLLEDQAAQHKHDIQEKITQLQSSSVSELDRQKNIVEETlrQKKVVEEEIHIIRINFER 2098
Cdd:pfam10174 630 MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSST--QQSLAEKDGHLTNLRAER 699
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2559-2743 |
2.72e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2559 FKKQADEAKVRLQETEKQTtETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQME-- 2636
Cdd:pfam04012 9 VRANIHEGLDKAEDPEKML-EQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2637 --QQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKhledevNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAE 2714
Cdd:pfam04012 88 alAEKKSLEKQAEALETQLAQQRSAVEQLRKQLAA------LETKIQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSS 161
|
170 180 190
....*....|....*....|....*....|....
gi 1655220517 2715 A-----EMKNKQKEMEALEKKRLEQEKLLADENK 2743
Cdd:pfam04012 162 AtdsfeRIEEKIEEREARADAAAELASAVDLDAK 195
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2402-2510 |
2.77e-03 |
|
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: 40.67 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2402 EENLRLMQKNKDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEKMQAIQEATKLKAE 2481
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1655220517 2482 AEELQKQKNQAQEKAKKLLEDKQEIQQRL 2510
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
2555-2753 |
2.78e-03 |
|
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: 42.43 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKETA---SAQ 2631
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2632 QEQMEQQKAMLQQtfltekeLLLKRERDVEDEKKKLQKHLEDEvnkaKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQK 2711
Cdd:cd00176 81 LEELNQRWEELRE-------LAEERRQRLEEALDLQQFFRDAD----DLEQWLEEKEAALASEDLGKDLESVEELLKKHK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655220517 2712 EAEAEMKNKQKEMEALEKKRLE-QEKLLADENKKLREKLESLE 2753
Cdd:cd00176 150 ELEEELEAHEPRLKSLNELAEElLEEGHPDADEEIEEKLEELN 192
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1549-2241 |
2.79e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1549 KAELEAQELKLKMKEDasqrqgLAVDAEKQKQNIQlelTQLKNLsEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQTT 1628
Cdd:TIGR04523 46 KNELKNKEKELKNLDK------NLNKDEEKINNSN---NKIKIL-EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1629 IKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKkknAEDELKRKSEAEKEaarqkqkaLDELQKHKMQ 1708
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK---YNDLKKQKEELENE--------LNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1709 AEEAERRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGtvlQLQEEAEKLRKQEEEANKAREQ 1788
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1789 AEKELETWRLKANEAlrlrlraeeEAQRKSLAQEEAEKQKTEAErdakkkakaeeaalKQKENAEKELEKQRTFAEQIAQ 1868
Cdd:TIGR04523 262 QNKIKKQLSEKQKEL---------EQNNKKIKELEKQLNQLKSE--------------ISDLNNQKEQDWNKELKSELKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1869 QklsaEQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDaLLQMKIQAEKVSQSNTEKSK 1948
Cdd:TIGR04523 319 Q----EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1949 QLLETEALKMKQLAEEaarlrsvaeeakKQRQLaedeaarQRAEAEKILKEKlaaineatrlkteaevalkakeaENERL 2028
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQ------------KDEQI-------KKLQQEKELLEK-----------------------EIERL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2029 KRQAEDEAYQRKLLEDQAAQHKHDIQ--EKITQLQSSSVSELDRQKNIVEETLRQKKvveEEIHIIRINFERASKEKSDL 2106
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESLETQLKVLSRSINKIKQNLEQKQ---KELKSKEKELKKLNEEKKEL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2107 EVELKKLKgiadetqKSKAKAEEEAEKLKKLAAEEERKRREAEEKVKKIAAAEEEAA--RQRKAAQDEVERLKQkaaEAN 2184
Cdd:TIGR04523 509 EEKVKDLT-------KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQ---TQK 578
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2185 KLKDKAEkelEKQVILAKEAAQKstaaeqkaQDVLSKNKEDLLSQEKLRDEFENAKK 2241
Cdd:TIGR04523 579 SLKKKQE---EKQELIDQKEKEK--------KDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2419-2598 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2419 LAEEAEKMKSLAEEAARL-SVEAEETARQRKTAEAElaeqralAEKMLKEKMQAIQEATKLKAEAEELQKQKNQAQEKAK 2497
Cdd:pfam05262 186 LREDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEE-------LDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KlLEDKQEIQQRLDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQT 2577
Cdd:pfam05262 259 N-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL 337
|
170 180
....*....|....*....|.
gi 1655220517 2578 TETVVQKletqRLQSTREADD 2598
Cdd:pfam05262 338 QKTKPQV----EAQPTSLNED 354
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1554-2039 |
2.87e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1554 AQELKLKMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEIHLIRIQLQttIKQKS 1633
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAE--AAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1634 TADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAE 1713
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1714 RRLKQAEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKEL 1793
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1794 ETWRLKANEALRLRLRAEEEAQRKSLAQEEAEKQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQQKLSA 1873
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1874 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLET 1953
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1954 EALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAE 2033
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 1655220517 2034 DEAYQR 2039
Cdd:COG3064 480 LLLLGG 485
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2351-2547 |
2.93e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2351 TDKQKALMDEELQrvkaqvndAVKQKAQVENELS--KVKMQMDELLKLKVrieEENLRLMQKNKdntqKLLAEEAEKMKS 2428
Cdd:smart00787 108 SPDVKLLMDKQFQ--------LVKTFARLEAKKMwyEWRMKLLEGLKEGL---DENLEGLKEDY----KLLMKELELLNS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2429 LAEEAARLSVEAEETARQRKTAEAEL-----AEQRALAEKMLKEKMQAIQEATKLkaeaEELQKQKNQAQEKAKKLLEDK 2503
Cdd:smart00787 173 IKPKLRDRKDALEEELRQLKQLEDELedcdpTELDRAKEKLKKLLQEIMIKVKKL----EELEEELQELESKIEDLTNKK 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655220517 2504 QEIQQRLDKETQGFQKSLEAERKrqleisaEAEKLKLRVKELSS 2547
Cdd:smart00787 249 SELNTEIAEAEKKLEQCRGFTFK-------EIEKLKEQLKLLQS 285
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
2339-2674 |
3.12e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2339 KELGLVKLQLDEtdKQKALMDEELQRVKAQVNDAVK-QKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNK--DNT 2415
Cdd:PTZ00108 983 KEFYLVRLDLYK--KRKEYLLGKLERELARLSNKVRfIKHVINGELVITNAKKKDLVKELKKLGYVRFKDIIKKKseKIT 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2416 QKLLAEEAEKMKSLAEEAARLSVEAEE------------TARQRKTAEAELAEQRALAEKMLK----------------- 2466
Cdd:PTZ00108 1061 AEEEEGAEEDDEADDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNttpkdmwledldkfeea 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2467 -EKMQAIQEATKLKAE---------AEELQKQKNQAQEKAKK-------------------LLEDKQEIQQRLDKETQGF 2517
Cdd:PTZ00108 1141 lEEQEEVEEKEIAKEQrlksktkgkASKLRKPKLKKKEKKKKkssadkskkasvvgnskrvDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2518 QKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2597
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGS 1300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2598 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQE--QMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDE 2674
Cdd:PTZ00108 1301 KPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKskTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDSEVDDSEDE 1379
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2312-2476 |
3.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2312 QKQEADAEMAKHKKEAEQALKQKSQVEKELglvklQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMD 2391
Cdd:PRK12705 31 LAKEAERILQEAQKEAEEKLEAALLEAKEL-----LLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2392 ELLKLKVRIEEENLRLMQKNKDNTQKLlaEEAEKMKS---LAEEAARLSVEAEETARQRKTAEAELA--EQRALAEKMLK 2466
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRVKKIEEEAdlEAERKAQNILA 183
|
170
....*....|
gi 1655220517 2467 EKMQAIQEAT 2476
Cdd:PRK12705 184 QAMQRIASET 193
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2167-2339 |
3.20e-03 |
|
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: 43.30 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2167 KAAQDEVERLKQKAAEANKLKDKAEKELEKQvilaKEAAQKSTAAEQKAQDVLSKNKEDllsqeklrdefENAKKLAQAA 2246
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ----AEEAEKQRAAEQARQKELEQRAAA-----------EKAAKQAEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2247 ETAKEKAEKEAALLRQKAEEAEKLKKAAEDEAAKQAKAQKDAErlrkeaeAEAAKRAAAEAAALKQKQEADAEM-AKHKK 2325
Cdd:TIGR02794 111 AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAE-------EEAKAKAAAEAKKKAEEAKKKAEAeAKAKA 183
|
170
....*....|....
gi 1655220517 2326 EAEQALKQKSQVEK 2339
Cdd:TIGR02794 184 EAEAKAKAEEAKAK 197
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1672-1795 |
3.22e-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: 40.70 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1672 QKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKMQAEEAERRLKQaeeekvrqikvvEEVAQKTAATQLQamsfsekt 1751
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNYER------------ELVLHAEDIKALQ-------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220517 1752 tKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELET 1795
Cdd:pfam07926 61 -ALREELNELKAEIAELKAEAESAKAELEESEESWEEQKKELEK 103
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1810-1927 |
3.28e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1810 AEEEAQRKSL-AQEEAEKQKTEAERDakkkakaEEAALKQKENAEKELEKQRTFAEQ--IAQQKL-SAEQEYIRLKADFE 1885
Cdd:COG1566 93 AAAEAQLARLeAELGAEAEIAAAEAQ-------LAAAQAQLDLAQRELERYQALYKKgaVSQQELdEARAALDAAQAQLE 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1886 HAEQQRGLL------DNELQRLKNEVNAAEKQRRQLEDELAK--VRSEMD 1927
Cdd:COG1566 166 AAQAQLAQAqaglreEEELAAAQAQVAQAEAALAQAELNLARttIRAPVD 215
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1465-1698 |
3.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1465 KKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIKFILETQRRLEDDEKASEKLKEDekkrMAEIQAQLETQKQLAEGHA 1544
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1545 KSVAKAELEAQELKL----KMKEDASQRQGLAVDAEKQKQNIQLELTQLKNLSEQEIRSKNQQLEEAQVSRRKLEEEihl 1620
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1621 iRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKA 1698
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1471-1713 |
3.47e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1471 SASDNIIQEYVTLRTRYSELSTLTSQyikfILETQRRLEDDEKASEKLKEDEKKRMAEIQaqlETQKQLAEghaksvAKA 1550
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAE------AEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1551 ELEAQELKLKMKEDASQRQGLAVDAEKQ---KQNIQLELTQLKNLSeQEIRSKNQQLEEAQVSRRKLEEeihliriqlqt 1627
Cdd:COG3883 80 EIEERREELGERARALYRSGGSVSYLDVllgSESFSDFLDRLSALS-KIADADADLLEELKADKAELEA----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1628 tikQKSTADDELQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDELKRKSEAEKEAARQKQKALDELQKHKM 1707
Cdd:COG3883 148 ---KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*.
gi 1655220517 1708 QAEEAE 1713
Cdd:COG3883 225 AAAAAA 230
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2500-2694 |
3.61e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.97 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2500 LEDKQEIQQR-LDKETQGFQKSLEAERKRQLEISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTT 2578
Cdd:pfam04012 16 GLDKAEDPEKmLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2579 ETVVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQNKSKeTASAqQEQMEQQKAMLQQTFLTEKELLLKRER 2658
Cdd:pfam04012 96 EKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK-AAKA-QEAVQTSLGSLSTSSATDSFERIEEKI 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1655220517 2659 DVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDE 2694
Cdd:pfam04012 174 EEREARADAAAELASAVDLDAKLEQAGIQMEVSEDV 209
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3291-3328 |
3.65e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.65e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655220517 3291 IRLLEAQLSTGGIIDPVKSYRVPQEVACKRGYFNEEMA 3328
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1214-1585 |
3.66e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1214 ILASPQQSSSAPMLRS-------ELDVTLKKMDHVYGLSSVYLDKLKtidiviRNTKDAEDTVKSYESRLRDVSKVPAEE 1286
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQELS------DASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1287 KEVEAHRSQLKAMRAEAEADQATFDRLQDELKAAtsvsdkmtrLHSERDAELEHYRQLAGSLLERWQAVFAQIDLRQREL 1366
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEED---------LHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1367 SLLGRHMNSYKQSYEWLIQWLREARlrQEKIEAAPVWDSKalKEQLTQEKKLLE-EIEKNKDQIENCQKDAKAYIDSLKD 1445
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQ--IKSIEKEIENLNgKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1446 YEFQILAYRAlqdpiasplKKPKMESASDNIIQEYVTLRTRYSELST---LTSQYIKFILETQRRLEDDEKAS---EKLK 1519
Cdd:TIGR02169 887 LKKERDELEA---------QLRELERKIEELEAQIEKKRKRLSELKAkleALEEELSEIEDPKGEDEEIPEEElslEDVQ 957
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 1520 EDEKKRMAEIQAqLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDAEKQKQNIQLE 1585
Cdd:TIGR02169 958 AELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3918-3952 |
3.69e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 3.69e-03
10 20 30
....*....|....*....|....*....|....*
gi 1655220517 3918 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLVPED 3952
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
686-779 |
3.84e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 39.62 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 686 LRYIQDLLGWVEENQRRVDDGEWGSDLPAVESQLGSHRGLHQSVEEFRSKIERAKADESQI---SPASKAAYRDYLAKLE 762
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*..
gi 1655220517 763 LQYDKLLHDSKARLRYL 779
Cdd:smart00150 84 ERWEELKELAEERRQKL 100
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1751-1875 |
3.88e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1751 TTKLEESLKKEQGTVLQLQEEAEKLRKQ-----EEEANKAREQAEKELETWRLKANEALRlRLRAEEEAQRKSLaqEEAE 1825
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKELRERRNELQKLEK-RLLQKEENLDRKL--ELLE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1826 KQKTEAERDAKKKAKAEEAALKQKENAEKELEKQRTFAEQIAQqkLSAEQ 1875
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2577-2758 |
3.93e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2577 TTETVVQKLETQRLQSTRE-------ADDLKkaiAELEKER---EKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQ-T 2645
Cdd:PLN03188 1041 TDESPEKKLEQERLRWTEAeskwislAEELR---TELDASRalaEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2646 FLTEKEL-LLKRERDVE---DEKKKL----------QKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMD---EAVK 2708
Cdd:PLN03188 1118 DLEEKHIqLLARHRRIQegiDDVKKAaaragvrgaeSKFINALAAEISALKVEREKERRYLRDENKSLQAQLRdtaEAVQ 1197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2709 KQKEAEAEMKNKQKEMEALEKKRLEQEKLLADENK---KLREKLESLEVTSKQ 2758
Cdd:PLN03188 1198 AAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAYKqidKLKRKHENEISTLNQ 1250
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
2607-2728 |
3.99e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2607 EKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQqTFLTEkelLLKRERDVEDEKKKLQKHLEDEV--NKAKALKDE 2684
Cdd:cd22656 109 DEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLT-DFENQ---TEKDQTALETLEKALKDLLTDEGgaIARKEIKDL 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655220517 2685 QQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEMEALE 2728
Cdd:cd22656 185 QKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLT 228
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2578-2778 |
4.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2578 TETVVQKLETQRLQ--STREADDLKKAIAElEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLK 2655
Cdd:PRK09510 57 PGAVVEQYNRQQQQqkSAKRAEEQRKKKEQ-QQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2656 RERDVEDEKKKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKKLQAimdEAvKKQKEAEAEMK-----NKQKEMEALEKK 2730
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA---EA-KKKAEAEAAAKaaaeaKKKAEAEAKKKA 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1655220517 2731 RLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIEVQTDKVPEEQL 2778
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
204-296 |
4.24e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.39 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 204 KTFTKWVNKHLMKAQrhITDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 273
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1655220517 274 KLVNIRNDDIADGNpKLTLGLIW 296
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1856-2058 |
4.40e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1856 LEKQRTFAEQIAQQKLSaeqeyiRLKADFEHAEQQrgllDNELQRLKNEvNAAEKQRRQLEDELAKVRSEM--------- 1926
Cdd:PRK11448 35 LIKLRQFGEALAKHIAA------LLGIYEPPCENQ----HDLLRRLGKE-GFLPDEILDVFHKLRKIGNKAvhefhgdhr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1927 DALLQMKIQ-------AEKVSQSNTEKSKQLLETE--ALKMKQLAEEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKIl 1997
Cdd:PRK11448 104 EALMGLKLAfrlavwfHRTYGKDWDFKPGPFVPPEdpENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655220517 1998 kEKLAAineatrlktEAEVALKAKEAENERLKRQAE----DEAYQRKLLEDQAAQhKHDIQEKIT 2058
Cdd:PRK11448 183 -EGLAA---------ELEEKQQELEAQLEQLQEKAAetsqERKQKRKEITDQAAK-RLELSEEET 236
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2448-2752 |
4.66e-03 |
|
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: 43.09 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2448 KTAEAELAEQRALAEKMLkEKMQaiQEATKLKAEAEELQKQKNQAQ---EKAKKLLEdkqEIQQRLDKetqgfqKSLEAE 2524
Cdd:pfam05701 27 KAHRIQTVERRKLVELEL-EKVQ--EEIPEYKKQSEAAEAAKAQVLeelESTKRLIE---ELKLNLER------AQTEEA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2525 RKRQleisaEAEKLKLRVKEL-------SSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREAD 2597
Cdd:pfam05701 95 QAKQ-----DSELAKLRVEEMeqgiadeASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2598 DLKKAIAELEKEREKLkrdAQELQN--KSKETASAQQEQMEQQK---AM-LQQTFLT-EKELllkreRDVEDEKKKLQkh 2670
Cdd:pfam05701 170 EAVSASKEIEKTVEEL---TIELIAtkESLESAHAAHLEAEEHRigaALaREQDKLNwEKEL-----KQAEEELQRLN-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2671 leDEVNKAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMK---NKQKEMEALEKKRLEQEKL----LADENK 2743
Cdd:pfam05701 240 --QQLLSAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKktsTSIQAALASAKKELEEVKAniekAKDEVN 317
|
....*....
gi 1655220517 2744 KLREKLESL 2752
Cdd:pfam05701 318 CLRVAAASL 326
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2259-2458 |
5.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2259 LLRQKAEEAEKLKKAAEDEAAKQAKAQKDaerlrkeaeaeaakraaaeaaalKQKQEADAEMAKHKKEAEQALKQKsqvE 2338
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKK-----------------------EALLEAKEEIHKLRNEFEKELRER---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2339 KELGlvklQLDETDKQK-ALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQK 2417
Cdd:PRK12704 82 NELQ----KLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1655220517 2418 LLAEEAEkmKSLAEEAARLSVEAEETARQRKTAEAE----LAEQR 2458
Cdd:PRK12704 158 ILLEKVE--EEARHEAAVLIKEIEEEAKEEADKKAKeilaQAIQR 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1286-1832 |
5.19e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1286 EKEVEAHRSQLKAMRAEAEADQATFD-------RLQDELKAAT-------SVSDKM----TRLHSERD---AELEHYRQL 1344
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEaleegkkRLQRELEALTqqleekaAAYDKLektkNRLQQELDdllVDLDHQRQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1345 AgSLLERWQAVFAQIDLRQRELSLlgrhmnsykQSYEWLIQWLREARlrqEKieaapvwDSKALkeQLTQEkklLEEIEK 1424
Cdd:pfam01576 596 V-SNLEKKQKKFDQMLAEEKAISA---------RYAEERDRAEAEAR---EK-------ETRAL--SLARA---LEEALE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1425 NKDQIENCQKDAKAYIDSL--------KDYEFQILAYRALQDPIASplKKPKMESASDNI-IQEYVTLRTRYSeLSTLTS 1495
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLvsskddvgKNVHELERSKRALEQQVEE--MKTQLEELEDELqATEDAKLRLEVN-MQALKA 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1496 QYikfiletQRRLEDDEKASEKLKEDEKKRMAEIQAQLETQKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQglavDA 1575
Cdd:pfam01576 728 QF-------ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGRE----EA 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1576 EKQKQNIQlelTQLKNLSeqeirsknQQLEEAQVSRRKleeeihlIRIQLQTTIKQKSTADDELQKLRDQAAEAEKVRKA 1655
Cdd:pfam01576 797 VKQLKKLQ---AQMKDLQ--------RELEEARASRDE-------ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQ 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1656 AQEEAERLRKQVNEETQKKKNAEDELKR------KSEAEKEAARQKQKALDE-LQKHKMQAEE------AERRLKQAEEE 1722
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEKRRleariaQLEEELEEEQSNTELLNDrLRKSTLQVEQlttelaAERSTSQKSES 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1723 KVRQIkvveEVAQKTAATQLQAMSFSEKtTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELETWRLKANE 1802
Cdd:pfam01576 939 ARQQL----ERQNKELKAKLQEMEGTVK-SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVED 1013
|
570 580 590
....*....|....*....|....*....|
gi 1655220517 1803 ALRLRLRAEEEAQRKSLAQEEAEKQKTEAE 1832
Cdd:pfam01576 1014 ERRHADQYKDQAEKGNSRMKQLKRQLEEAE 1043
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2169-2752 |
5.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2169 AQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAKKLAqaaet 2248
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL----- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2249 akekaekeaallRQKAEEAEKLKKAAEDEAAKQAKAQKdaERLRKEAEAEAAKRaaaeaaalkQKQEADAEMAKHKKEAE 2328
Cdd:COG4913 322 ------------REELDELEAQIRGNGGDRLEQLEREI--ERLERELEERERRR---------ARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2329 QAlkqksQVEKELGLVKLQLDETDKQKALMDEELQRVKAQVNDAVKQKAQVENELSKVK----------MQMDELLKLKV 2398
Cdd:COG4913 379 AE-----EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparlLALRDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2399 RIEEENLR----LMQ-KNKD-----------NTQK--LLAEEA--------------------EKMKSLAEEAARLSVEA 2440
Cdd:COG4913 454 GLDEAELPfvgeLIEvRPEEerwrgaiervlGGFAltLLVPPEhyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2441 EETARQ--------RKTAEAELAEQRALA----EKMLKEKMQAIQEA--TKLKAEAEELQKQKN---------QAQEKAK 2497
Cdd:COG4913 534 DSLAGKldfkphpfRAWLEAELGRRFDYVcvdsPEELRRHPRAITRAgqVKGNGTRHEKDDRRRirsryvlgfDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2498 KLLEDKQEIQQRLDkETQGFQKSLEAERKRQLEISAEAEKL-KLRVKELSSAQAKAE-EEATRFKKQADEAKVRLQETEK 2575
Cdd:COG4913 614 ALEAELAELEEELA-EAEERLEALEAELDALQERREALQRLaEYSWDEIDVASAEREiAELEAELERLDASSDDLAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2576 QttetvVQKLETQRLQSTREADDLKKAIAELEKEREKLKRDAQELQnksKETASAQQEQMEQQKAMLQQTFltEKELLLK 2655
Cdd:COG4913 693 Q-----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ---DRLEAAEDLARLELRALLEERF--AAALGDA 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2656 RERDVedekkklqkhledevnkAKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAEAEMknkQKEMEALEKKRLEQE 2735
Cdd:COG4913 763 VEREL-----------------RENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL---DADLESLPEYLALLD 822
|
650
....*....|....*..
gi 1655220517 2736 KLLADENKKLREKLESL 2752
Cdd:COG4913 823 RLEEDGLPEYEERFKEL 839
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
339-416 |
5.49e-03 |
|
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: 39.21 E-value: 5.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 339 DNFTSSWRDGKLFNAIIHKHRPALLDMSQVYRQSNQENLEQAFSvAERELGVTRLLDPEDVDVAHPDEKSIITYVSSL 416
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2607-2750 |
5.58e-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: 41.61 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2607 EKEREKLKRDAQElqnKSKETASAQQEQMEQQKAMLQQtfltEKElllKRERDVEDEKKKLQKHLEDEVNKaKALKDEQQ 2686
Cdd:pfam13904 43 KLEGLKLERQPLE---AYENWLAAKQRQRQKELQAQKE----ERE---KEEQEAELRKRLAKEKYQEWLQR-KARQQTKK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 2687 RQQKLMDEEKKKLQAIMDEAVKKQKEAEAemKNKQKEMEaLEKKRLEQEKLLADENKKLREKLE 2750
Cdd:pfam13904 112 REESHKQKAAESASKSLAKPERKVSQEEA--KEVLQEWE-RKKLEQQQRKREEEQREQLKKEEE 172
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3585-3621 |
5.80e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.80e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655220517 3585 KLLSAEKAVTGYKDPYTGNKISLFQAMTKELVLREHA 3621
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2633-2737 |
5.81e-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: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2633 EQMEQQKAMLQQTflTEKELLLkrERDVEDEKKKLQKHLEDEVNKAKAlkdeqQRQQKLMDEE-KKKLQAIMDEA-VKKQ 2710
Cdd:cd03406 169 EAMEAEKTKLLIA--EQHQKVV--EKEAETERKRAVIEAEKDAEVAKI-----QMQQKIMEKEaEKKISEIEDEMhLARE 239
|
90 100
....*....|....*....|....*...
gi 1655220517 2711 KE-AEAEMKNKQKEMEAlEKKRLEQEKL 2737
Cdd:cd03406 240 KArADAEYYRALREAEA-NKLKLTPEYL 266
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2164-2494 |
5.92e-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: 43.02 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEANKLKDKAEKELEKQVILAKEAAQKSTAAEQKAQDVLSKN--------KEDLLSQEKLRDE 2235
Cdd:COG5185 194 ELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSdkleklveQNTDLRLEKLGEN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2236 FENAKKLAQAAETAKEKAEKEAALLRQKAEEAEklKKAAEDEAAKQAKAQKDAERLRKEAEAEAAKRAAAEAAALKQKQE 2315
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSID--IKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2316 ADAEMAKHKKEAEQ--ALKQKSQVEKELGLVKLQLDET----DKQKALMDEELQRVKAQVNDAVK----QKAQVENELSK 2385
Cdd:COG5185 352 LTENLEAIKEEIENivGEVELSKSSEELDSFKDTIESTkeslDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQ 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2386 VKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMK-SLAEEAARLSVEAEETARQRKTAEAELAEQRALAEKM 2464
Cdd:COG5185 432 ATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQ 511
|
330 340 350
....*....|....*....|....*....|
gi 1655220517 2465 LKEKMQAIQEATKLKAEAEELQKQKNQAQE 2494
Cdd:COG5185 512 LEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2262-2528 |
5.93e-03 |
|
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: 42.53 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2262 QKAEEAEKLKKAAEDEAAKQAKAQKDAERlrkEAEAEAAKRAAAEAAALKQKQEADAEmaKHKKEAEQALKQKSQVEKEl 2341
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQKQ- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2342 glvklqldetdkqkalmDEELqrvKAQVNDAVKQKAQVENElskvkmqmdellklkvrieeenlrlmQKNKDNTQKllAE 2421
Cdd:TIGR02794 121 -----------------AEEA---KAKQAAEAKAKAEAEAE--------------------------RKAKEEAAK--QA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2422 EAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAekmlkEKMQAIQEATKLKAEAEelQKQKNQAQEKAKKLLE 2501
Cdd:TIGR02794 153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAE-AEAKAKA-----EEAKAKAEAAKAKAAAE--AAAKAEAEAAAAAAAE 224
|
250 260
....*....|....*....|....*..
gi 1655220517 2502 DKQEIQQRLDKETQGFQKSLEAERKRQ 2528
Cdd:TIGR02794 225 AERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1293-1536 |
6.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1293 RSQLKAMRAEAEAdqatfdrLQDELKAATSVSDKMTRLHSERDAELEHYRQLAgsllerwQAVFAQIDLR--QRELSLLG 1370
Cdd:COG4913 609 RAKLAALEAELAE-------LEEELAEAEERLEALEAELDALQERREALQRLA-------EYSWDEIDVAsaEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1371 RHMNSYKQSYEWLIQWLREARLRQEKIEAApvwdSKALKEQLTQEKKLLEEIEKNKDQIENCQKDAKAYIDSLKDYEFQI 1450
Cdd:COG4913 675 AELERLDASSDDLAALEEQLEELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1451 LAYRaLQDPIASPLKKPKMESASDNIIQEYVTLRTRYSELSTLTSQYIK-FILETQ----------------RRLEDD-- 1511
Cdd:COG4913 751 LEER-FAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETAdldadleslpeylallDRLEEDgl 829
|
250 260
....*....|....*....|....*....
gi 1655220517 1512 ----EKASEKLKEDEKKRMAEIQAQLETQ 1536
Cdd:COG4913 830 peyeERFKELLNENSIEFVADLLSKLRRA 858
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2345-2490 |
6.17e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2345 KLQLDETDkqkALMDEELQRVKAQVNDAVKQKAQVENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAE 2424
Cdd:smart00787 146 KEGLDENL---EGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMI 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2425 KMKSLAE---EAARLSVEAEETARQRKTAEAELAEQRalaEKMLKEKMQAIQEATKLKAEAEELQKQKN 2490
Cdd:smart00787 223 KVKKLEEleeELQELESKIEDLTNKKSELNTEIAEAE---KKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1557-1792 |
6.29e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1557 LKLKMKEDASQRQGLAVDAEKQKQNIQlelTQLKNLSEQEIRSKN--QQLEEAQVSRRKLEEEIHLIRIQLQTTIK---- 1630
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK---TYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELTDELLnlvm 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1631 -QKSTADDeLQKLRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKkNAEDELKRKSEAeKEAARQKQKALDELQKHkmQA 1709
Cdd:PHA02562 249 dIEDPSAA-LNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQ-QISEGPDRITKI-KDKLKELQHSLEKLDTA--ID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1710 EEAERrlkqaEEEKVRQIKVVEEVAQKTAATQLQAMSFSEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQA 1789
Cdd:PHA02562 324 ELEEI-----MDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1655220517 1790 EKE 1792
Cdd:PHA02562 399 VKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1848-2000 |
6.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1848 QKENAEKELEKQRTFAEQIAQQKLSAEQEYIRLKADFEHAEQQRGLLDN--ELQRLKNEVNAAEKQRRQLEDELAKVRSE 1925
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655220517 1926 MDALlqmkiqaEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRSVAEEAKKQRQ-LAEDEAARQRAEAEKILKEK 2000
Cdd:COG1579 119 IEEL-------EEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREeLAAKIPPELLALYERIRKRK 187
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
208-266 |
6.58e-03 |
|
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: 39.14 E-value: 6.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 208 KWVNKHLmkAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALD 266
Cdd:cd21184 8 EWVNSKI--PEYKVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPLENATKAMD 64
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1874-2122 |
6.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1874 EQEYIRLKADFEHAEQQRGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQmKIQAEKVSQSNTEKSKQLLET 1953
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1954 EALKMKQLAEEAARLRsvAEEAKKQRQLAEDEAARQRA----EAEKILkeklaaINEATRLKTEAEVALKAKEAENERLK 2029
Cdd:COG1340 93 ELDELRKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKEL------VEKIKELEKELEKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2030 RQAEDEAyqrklLEDQAAQHKHDIQEKITQLQS------SSVSELDRQKNIVEETLRQKKVVEEEIHIIRINFERASKEK 2103
Cdd:COG1340 165 LRAELKE-----LRKEAEEIHKKIKELAEEAQElheemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250
....*....|....*....
gi 1655220517 2104 SDLEVELKKLKGIADETQK 2122
Cdd:COG1340 240 RELRKELKKLRKKQRALKR 258
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1508-1792 |
6.66e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.92 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1508 LEDDEKASEKLKEDEKKRMAEIQAQLET-QKQLAEGHAKSVAKAELEAQELKLKMKEDASQRQGLAVDA---EKQKQNIQ 1583
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmglQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1584 LELTQLKnlseqeirSKNQQLEEAQVSR-RKLEEEIH--LIRIQLQTTIKQKstaddeLQKLRDqaAEAEKVRKAAQEEA 1660
Cdd:PLN03229 493 EEFSKAN--------SQDQLMHPVLMEKiEKLKDEFNkrLSRAPNYLSLKYK------LDMLNE--FSRAKALSEKKSKA 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1661 ERLRKQVNeetQKKKNAED--ELKRKSEAEK-EAARQKQKALDELQKHkmQAEEAERRLKQAEEEKVRQIKV----VEEV 1733
Cdd:PLN03229 557 EKLKAEIN---KKFKEVMDrpEIKEKMEALKaEVASSGASSGDELDDD--LKEKVEKMKKEIELELAGVLKSmgleVIGV 631
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655220517 1734 AQKTAATQLQAM--SFSEKTTKLEESLKKEQGTVLQ---LQEEAEKLRKQEEEANKAREQAEKE 1792
Cdd:PLN03229 632 TKKNKDTAEQTPppNLQEKIESLNEEINKKIERVIRssdLKSKIELLKLEVAKASKTPDVTEKE 695
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1575-1778 |
6.70e-03 |
|
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: 42.72 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1575 AEKQKQNIQLELTQLKNLSEQEIRS---KNQQLEEAQVSRRkleeeIHLIRIQlqttiKQKSTadDELQKLRDQaaeaek 1651
Cdd:pfam10168 522 ADKLSSPSPQECLQLLSRATQVFREeylKKHDLAREEIQKR-----VKLLKLQ-----KEQQL--QELQSLEEE------ 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1652 vRKAAQEEAERLRKQVNE--ETQKK---------KNAEDELKRKSEAEKEAARqkqkaldELQKHKMQAEEAERRLKQAE 1720
Cdd:pfam10168 584 -RKSLSERAEKLAEKYEEikDKQEKlmrrckkvlQRLNSQLPVLSDAEREMKK-------ELETINEQLKHLANAIKQAK 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 1721 EEKVRQIKvveEVAQKTAATQLQAMSFSEKTTK-LEESLKKEQGTVLQLQEEAEKLRKQ 1778
Cdd:pfam10168 656 KKMNYQRY---QIAKSQSIRKKSSLSLSEKQRKtIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
2592-2783 |
7.04e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2592 STREADDLKKAIAELEKEREKLKRDAQELQNKSkETASAQQEQMEQQKAMLQQ------TFLTEKElllKRERDVEDEKK 2665
Cdd:pfam17078 1 STKVIESLHDQIDALTKTNLQLTVQSQNLLSKL-EIAQQKESKFLENLASLKHendnlsSMLNRKE---RRLKDLEDQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2666 KLQKHLEDEVNKAKALKDE----QQRQQKLMdEEKKKLQAIMDEAVKKQKEAEAEMKNKQKEM-EALEKKRLEQEK---- 2736
Cdd:pfam17078 77 ELKNSYEELTESNKQLKKRlensSASETTLE-AELERLQIQYDALVDSQNEYKDHYQQEINTLqESLEDLKLENEKqlen 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2737 ---LLADENKKLREKLESLEVTSKQaaskTKEIEVQTDKVPEEQLVSMTT 2783
Cdd:pfam17078 156 yqqRISSNDKDIDTKLDSYNNKFKN----LDNIYVNKNNKLLTKLDSLAQ 201
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2530-2752 |
7.77e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2530 EISAEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTREA--DDLKKAIAELE 2607
Cdd:pfam19220 38 AILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAakEELRIELRDKT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2608 KEREKLKRDAQELQNKSKETASAQQEQMEQQKAMLQQTFLTEKELLLKRERD--VEDEKKKLQKHLEDEVNKA------- 2678
Cdd:pfam19220 118 AQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLalLEQENRRLQALSEEQAAELaeltrrl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2679 ----KALKDEQQR----QQKLMDE--EKKKLQAIMDEAVKKQKEAEAEMKNKqkeMEALEKKRLEQEKLLADENKKLREK 2748
Cdd:pfam19220 198 aeleTQLDATRARlralEGQLAAEqaERERAEAQLEEAVEAHRAERASLRMK---LEALTARAAATEQLLAEARNQLRDR 274
|
....
gi 1655220517 2749 LESL 2752
Cdd:pfam19220 275 DEAI 278
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2164-2467 |
7.87e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2164 RQRKAAQDEVERLKQKAAEAnKLK---DKAEKELEKQvilAKEAAQKSTAAEQKAQDVLSKNKEDLLSQEKLRDEFENAK 2240
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEA-KARfeaRQARLEREKA---AREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2241 KLAQAAETAKEKAEKEAALLRQKAEEAEKlKKAAEDEAAKQAKAQKDAERlrkeaeaeaakrAAAEAAALKQKQEADAEM 2320
Cdd:PRK05035 508 IKAGARPDNSAVIAAREARKAQARARQAE-KQAAAAADPKKAAVAAAIAR------------AKAKKAAQQAANAEAEEE 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2321 AKHKKEAEQALKQKSQVEKElglvklqldetdkQKALMDEELQRVKAQVNDavkQKAQVENELSKVKMQMDELLKLKVRI 2400
Cdd:PRK05035 575 VDPKKAAVAAAIARAKAKKA-------------AQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPE 638
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655220517 2401 EEEnlrlmqknkDNTQKLLAEEAEKMKSLAEEAARLSVEAEETARQRKTAEAElAEQRALAEKMLKE 2467
Cdd:PRK05035 639 EPV---------DPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAA-AIARAKAKKAAQQ 695
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1517-1726 |
8.04e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1517 KLKEDEKKRMAEIQAQLETQKQLAE---GHAKSVAKAELEAQELK-----LKMKEDASQRQGLAVDaekqKQNIQLElTQ 1588
Cdd:pfam19220 196 RLAELETQLDATRARLRALEGQLAAeqaERERAEAQLEEAVEAHRaerasLRMKLEALTARAAATE----QLLAEAR-NQ 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1589 LKNLSEqEIRSKNQQLEEAQVSRRKLEEEIHliriQLQTtikqkstaddELQKLRDQAAEAEKVRKAAQEEAERLRKQVN 1668
Cdd:pfam19220 271 LRDRDE-AIRAAERRLKEASIERDTLERRLA----GLEA----------DLERRTQQFQEMQRARAELEERAEMLTKALA 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655220517 1669 EETQKKKNAE----------DELKRKSEAEKEAARQKQKALDElqkhKMQAEEAERRLKQAEEEKVRQ 1726
Cdd:pfam19220 336 AKDAALERAEeriaslsdriAELTKRFEVERAALEQANRRLKE----ELQRERAERALAQGALEIARE 399
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
195-306 |
8.12e-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: 39.57 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 195 ADERDRVQKKTFTKWVNKHLMKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 270
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655220517 271 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 306
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1640-1740 |
8.15e-03 |
|
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: 40.16 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1640 QKLRDQAAEAEKVRKAAQEEAERLRKQVNEetqkkknAEDELKR-KSEAEKEAARQKQKALDELQkhkmqaEEAERRLKQ 1718
Cdd:COG0711 34 EKIADGLAEAERAKEEAEAALAEYEEKLAE-------ARAEAAEiIAEARKEAEAIAEEAKAEAE------AEAERIIAQ 100
|
90 100
....*....|....*....|...
gi 1655220517 1719 AEEEKVRQI-KVVEEVAQKTAAT 1740
Cdd:COG0711 101 AEAEIEQERaKALAELRAEVADL 123
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
2478-2598 |
8.28e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 42.31 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2478 LKAEAEELQKQKnqaQEKAKKLLEDKQEIQQRLDKETQGFQKSLEaerkrqleiSAEAEK--LKLRVKELSSAQAKAEEE 2555
Cdd:pfam09798 2 LRDKLELLQQEK---EKELEKLKNSYEELKSSHEEELEKLKQEVQ---------KLEDEKkfLLNELRSLSATSPASSQS 69
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1655220517 2556 ATRFKKQADEAKVRLQETEKQTTETVVQKLetQRLQSTREADD 2598
Cdd:pfam09798 70 HETDTDDSSSVSLKKRKIEESTAESLKQKY--IRLQNNRIVDE 110
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2380-2645 |
8.32e-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: 41.34 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2380 ENELSKVKMQMDELLKLKVRIEEENLRLMQKNKDNTQKLL--AEEAEKMKSLAEEAARLSVEAEETARQRKTAEAElaeq 2457
Cdd:pfam17045 5 EAELQELMKQIDIMVAHKKSEWEGQTRALETRLDIREEELlsARNTLERKHKEIGLLRQQLEELEKGKQELVAKYE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2458 ralaekmlkEKMQAIQEA-TKLKAEAEELQ-KQKNQAQEKAKKLLEDKQEIQQRLDKETQGFQKSLEAERKR---QLEIS 2532
Cdd:pfam17045 81 ---------QQLQKLQEElSKLKRSYEKLQrKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRlqyQQQVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2533 AEAEKLKLRVKELSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLETQRLQSTReaddLKKAIAELEKEREK 2612
Cdd:pfam17045 152 SLEAQRKALAEQSSLIQSAAYQVQLEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELER----LRMRVSELGDSNRK 227
|
250 260 270
....*....|....*....|....*....|...
gi 1655220517 2613 LKRDAQELQNKSKEtASAQQEQMEQQKAMLQQT 2645
Cdd:pfam17045 228 LLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2517-2676 |
8.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2517 FQKSLEAERKRQlEISAEAEKLKlrvkelSSAQAKAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLEtqrlQSTREA 2596
Cdd:PRK12705 29 QRLAKEAERILQ-EAQKEAEEKL------EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEE----QLDARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2597 DDLKKAIAELEKEREKLKRDAQELQNKSKetasaQQEQMEQQKAMLQQTFLteKELLLKR-ERDVEDEKKKLQKHLEDEV 2675
Cdd:PRK12705 98 EKLDNLENQLEEREKALSARELELEELEK-----QLDNELYRVAGLTPEQA--RKLLLKLlDAELEEEKAQRVKKIEEEA 170
|
.
gi 1655220517 2676 N 2676
Cdd:PRK12705 171 D 171
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1810-2066 |
9.04e-03 |
|
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: 42.51 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1810 AEEEAQRKSLAQEEAEKQKTEAERdakkkakaeEAALKQKENAEKELEKQRTFAEQIAQQKLSAEQEYIR--LKADFEHA 1887
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEADR---------QRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1888 EQQRGLLDNELQRLKNEVNAAEKQRRQLEDELA-----KVRSEMDallqmkiQAEKVSQSNTEKSKQLLETEALKMKqla 1962
Cdd:NF012221 1619 TKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglldRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVK--- 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1963 EEAARLRSVAEEAKKQRQLAEDEAARQRAEAEKILKEKLAAINEATRLKTEAEVALKAKEAENERLKRQAEDEAYQRKlL 2042
Cdd:NF012221 1689 DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQ-A 1767
|
250 260
....*....|....*....|....
gi 1655220517 2043 EDQAAQHKHDIQEKITQLQSSSVS 2066
Cdd:NF012221 1768 DAKGAKQDESDKPNRQGAAGSGLS 1791
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1737-1994 |
9.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1737 TAATQLQAMSfsEKTTKLEESLKKEQGTVLQLQEEAEKLRKQEEEANKAREQAEKELEtwrlKANEALRlRLRAEEEAQR 1816
Cdd:COG3883 13 FADPQIQAKQ--KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID----KLQAEIA-EAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1817 KSLAQEEAEKQKTEAERDAKKKAKaeeaalkqkeNAE--KELEKQRTFAEQIAQQKLSAEQEYIRLKADFEH----AEQQ 1890
Cdd:COG3883 86 EELGERARALYRSGGSVSYLDVLL----------GSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAkkaeLEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1891 RGLLDNELQRLKNEVNAAEKQRRQLEDELAKVRSEMDALLQMKIQAEKVSQSNTEKSKQLLETEALKMKQLAEEAARLRS 1970
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
250 260
....*....|....*....|....
gi 1655220517 1971 VAEEAKKQRQLAEDEAARQRAEAE 1994
Cdd:COG3883 236 AAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4440-4470 |
9.05e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.92 E-value: 9.05e-03
10 20 30
....*....|....*....|....*....|.
gi 1655220517 4440 AGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4470
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2310-2579 |
9.38e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2310 LKQKQEADAEMAKHKKEAEQALKQksqvekelglvklqldetdkqkalMDEELQRVKAQVNDAVKQKAQVENElSKVKMQ 2389
Cdd:pfam02029 65 LDRTAKREERRQKRLQEALERQKE------------------------FDPTIADEKESVAERKENNEEEENS-SWEKEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2390 MDELLKLKVRIEEENLRLMQKNKDNTQKLLAEEAEKMkslaEEAARLSVEAEETARQRKTAEaELAEQRALAEKMLKEKM 2469
Cdd:pfam02029 120 KRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEG----EEEEDKSEEAEEVPTENFAKE-EVKDEKIKKEKKVKYES 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2470 ----------------QAIQEATKLKAEAEELQKQKNQAQEK---AKKLLEDKQEI----QQRLDKETQGFQKSleaeRK 2526
Cdd:pfam02029 195 kvfldqkrghpevksqNGEEEVTKLKVTTKRRQGGLSQSQEReeeAEVFLEAEQKLeelrRRRQEKESEEFEKL----RQ 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1655220517 2527 RQLEISAEAEKLKLRVKELSSAQakaEEEATRFKKQADEAKVRLQETEKQTTE 2579
Cdd:pfam02029 271 KQQEAELELEELKKKREERRKLL---EEEEQRRKQEEAERKLREEEEKRRMKE 320
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2476-2681 |
9.53e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 40.80 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2476 TKLKAEAEELQKQKNQAQEKAKKLLEDKQE-IQQRLDKETQgfqkslEAERKRQLEISAEAEKLKLRVKElssaQAKAEE 2554
Cdd:pfam15665 7 TKNDEHEAEIQALKEAHEEEIQQILAETREkILQYKSKIGE------ELDLKRRIQTLEESLEQHERMKR----QALTEF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2555 EATRFKKQADEAKVRLQETEKQTT------------ETVVQKLETQRLQSTREAddlKKAIAELekeREKLKRDAQELQN 2622
Cdd:pfam15665 77 EQYKRRVEERELKAEAEHRQRVVElsreveeakrafEEKLESFEQLQAQFEQEK---RKALEEL---RAKHRQEIQELLT 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655220517 2623 KSKetasAQQEQMEQQKAMLQQTFLTEKELLLKRERDVEDEKKKLQKHLEDEVNKAKAL 2681
Cdd:pfam15665 151 TQR----AQSASSLAEQEKLEELHKAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAF 205
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2551-2724 |
9.71e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.16 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2551 KAEEEATRFKKQADEAKVRLQETEKQTTETVVQKLetqRLQSTREADDLKKAI-AELEKEREKLKRDAQELQNKS----- 2624
Cdd:PRK00106 39 NAEQEAVNLRGKAERDAEHIKKTAKRESKALKKEL---LLEAKEEARKYREEIeQEFKSERQELKQIESRLTERAtsldr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2625 KETASAQQEQMEQQKamlQQTFLTEKELLLKRERDVEdekkKLQKHLEDEVNKAKALKDEQQRQQKLMDEEKKklqaIMD 2704
Cdd:PRK00106 116 KDENLSSKEKTLESK---EQSLTDKSKHIDEREEQVE----KLEEQKKAELERVAALSQAEAREIILAETENK----LTH 184
|
170 180
....*....|....*....|
gi 1655220517 2705 EAVKKQKEAEAEMKNKQKEM 2724
Cdd:PRK00106 185 EIATRIREAEREVKDRSDKM 204
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
1642-1722 |
9.76e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 40.70 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 1642 LRDQAAEAEKVRKAAQEEAERLRKQVNEETQKKKNAEDElKRKSEAEKEAARQKQKALDELQKHKMQAEEA--ERRLKQA 1719
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILE-KAEREAEREKRRIISSAELEARKELLEAKEEliEEVFEEA 90
|
...
gi 1655220517 1720 EEE 1722
Cdd:COG1390 91 LEK 93
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2598-2764 |
9.90e-03 |
|
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: 41.75 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2598 DLKKAIAELEKEREKLKRDAQELQNKSKETASAQQEQMEQQKAmlqqtfltEKELLLKRERDVEDEKKKLQkhlEDEVNK 2677
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA--------EQARQKELEQRAAAEKAAKQ---AEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2678 AKALKDEQQRQQKLMDEEKKKLQAIMDEAVKKQKEAE--AEMKNKQKEMEALEKKRLEQEKLLADENKK---LREKLESL 2752
Cdd:TIGR02794 113 QAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAkaeAEAKAKAE 192
|
170
....*....|..
gi 1655220517 2753 EVTSKQAASKTK 2764
Cdd:TIGR02794 193 EAKAKAEAAKAK 204
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2397-2767 |
9.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2397 KVRIEEENLRLMQKNKDNTQKLLAEE-----AEKMKSlAEEAARLSVEAEETARQRKTAEAELAEQRALAEKMLKEkMQA 2471
Cdd:PRK04863 241 ENRMTLEAIRVTQSDRDLFKHLITEStnyvaADYMRH-ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARE-LAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2472 IQEA-----TKLKAEAEELQKQKN--QAQEKAKKLLEDKQEIQQRLDKetqgfqksleaerkrQLEISAEAEKLKLRVKE 2544
Cdd:PRK04863 319 LNEAesdleQDYQAASDHLNLVQTalRQQEKIERYQADLEELEERLEE---------------QNEVVEEADEQQEENEA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2545 LSSAqakAEEEATRFKKQ-ADeakvrlqetekqttetVVQKLEtqrLQSTReADDLKKAIAELEKereklkrdAQELQNK 2623
Cdd:PRK04863 384 RAEA---AEEEVDELKSQlAD----------------YQQALD---VQQTR-AIQYQQAVQALER--------AKQLCGL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655220517 2624 SKETASAQQEQMEQQKAMLQQtfLTEKELLLKRERDVEDEKK-------KLQKHLEDEVNKAKAlkdEQQRQQKLMDEEK 2696
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQE--ATEELLSLEQKLSVAQAAHsqfeqayQLVRKIAGEVSRSEA---WDVARELLRRLRE 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655220517 2697 KKLQAimdeavkkqkEAEAEMKNKQKEMEALEKKRLEQEKLLADENKKLREKLESLEVTSKQAASKTKEIE 2767
Cdd:PRK04863 508 QRHLA----------EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE 568
|
|
| |
