|
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 ... |
43-147 |
1.58e-74 |
|
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: 243.85 E-value: 1.58e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 43 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1655274923 123 RNDDIADGNPKLTLGLIWTIILHFQ 147
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
40-158 |
3.62e-72 |
|
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: 237.62 E-value: 3.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKL 119
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSE 158
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
36-156 |
1.49e-69 |
|
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: 230.64 E-value: 1.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 36 DGRKDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHR 115
Cdd:cd21236 8 ERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRR 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655274923 116 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 156
Cdd:cd21236 88 QVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
160-265 |
1.59e-64 |
|
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: 215.27 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1655274923 240 PEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
161-265 |
5.58e-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: 213.41 E-value: 5.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1655274923 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
40-157 |
1.78e-60 |
|
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: 204.11 E-value: 1.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKL 119
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274923 120 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 157
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
161-265 |
1.50e-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: 195.21 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1655274923 241 EDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
159-265 |
8.02e-50 |
|
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: 173.30 E-value: 8.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 159 DMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLL 238
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1655274923 239 DPEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
45-148 |
1.01e-49 |
|
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: 172.95 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1655274923 124 NDDIADGNPKLTLGLIWTIILHFQI 148
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 ... |
40-144 |
7.90e-47 |
|
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: 164.85 E-value: 7.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1655274923 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
161-261 |
1.25e-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: 163.74 E-value: 1.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1655274923 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
161-261 |
5.26e-45 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 159.10 E-value: 5.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655274923 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
41-148 |
3.88e-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: 157.15 E-value: 3.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHRQ 116
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1655274923 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
39-144 |
7.24e-43 |
|
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: 153.61 E-value: 7.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 39 KDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLrHRQV 117
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1655274923 118 KLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
41-148 |
1.15e-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: 150.03 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM--RFHKLQNVQIALDFLRHRQ 116
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKlsQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1655274923 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
44-261 |
4.83e-41 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 163.57 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvngQSEDMSAKEKLLLWSQRMTDGYQ-GIRCDNFTTSWRDGKLFNAVI 199
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 200 HKNYPRLIDMGKVYRQTNLE--NLEQAFNVAEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLY 261
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
895-972 |
9.11e-41 |
|
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: 146.21 E-value: 9.11e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 895 LSWQYLMKDFTLIRSWNITMLKTMKPEEYRLILRNLELHYQDFMRDSQDSQLFGPDDRMQIEGDYTKSTQHFDSLLRS 972
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
40-144 |
1.91e-40 |
|
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: 147.48 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 1655274923 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
27-144 |
1.08e-39 |
|
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: 145.20 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 27 FYQGMLKATdgrKDERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNV 105
Cdd:cd21317 16 FERSRIKAL---ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENV 92
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 106 QIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21317 93 DKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
157-261 |
1.53e-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: 143.99 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 157 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 236
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1655274923 237 LLDPEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
160-265 |
1.89e-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: 143.61 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1655274923 240 PEDVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
148-263 |
5.38e-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: 142.50 E-value: 5.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 148 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 227
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274923 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
160-261 |
1.36e-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: 138.46 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1655274923 240 PEDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
41-148 |
1.78e-37 |
|
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: 138.04 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSQ--RHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1655274923 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
45-146 |
5.46e-37 |
|
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: 136.38 E-value: 5.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1655274923 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
157-269 |
1.15e-36 |
|
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: 135.96 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 157 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 236
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100 110
....*....|....*....|....*....|...
gi 1655274923 237 LLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 269
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYYHYFSKMKA 113
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
43-144 |
1.89e-36 |
|
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: 134.82 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 43 DRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVKLVN 121
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1655274923 122 IRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1276-2133 |
2.99e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.99 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1276 YIDIIKDYELQLVAYKAQVEPLTSPLKKTKL-DSASDNIIQEYVTLRTRYSELMTLTSQYIKF-ITDTQRRLEDEEKAAE 1353
Cdd:PTZ00121 1017 TIDFNQNFNIEKIEELTEYGNNDDVLKEKDIiDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFdFDAKEDNRADEATEEA 1096
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1354 KLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEkeaqelKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQ 1433
Cdd:PTZ00121 1097 FGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAE------EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEAR 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1434 IKDKSQQVDEALKSrlrieEEIHliriqlettvkqksnaedelkqlrdradAAEKLRKlaqeeAEKLRKqvseeTQKKRL 1513
Cdd:PTZ00121 1171 KAEDAKKAEAARKA-----EEVR----------------------------KAEELRK-----AEDARK-----AEAARK 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1514 AEEElkHKSEAERKAANEKQ-KALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSK 1592
Cdd:PTZ00121 1208 AEEE--RKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK 1285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1593 LEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEaerelekwRQKANEALRlrlqAEEEAHKKSLAQEEAEKQKEEADR 1672
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA--------KKKAEEAKK----KADAAKKKAEEAKKAAEAAKAEAE 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1673 EAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQqrsLLEDELYRLKNEVIAAQQERK 1752
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE---LKKAAAAKKKADEAKKKAEEK 1430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1753 QLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE--DAARQRA 1830
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKK 1510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1831 EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILE-DQANQHKLEIEEKIVLLKKSSDAEMER 1909
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAE 1590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1910 QKAIVDdtlkQRRVVEEEIRILKLNFEKASSGKLDLElELNKLKNIAEETQQSKLRAEEEAEKlrrlvlEEEMRRKEAED 1989
Cdd:PTZ00121 1591 EARIEE----VMKLYEEEKKMKAEEAKKAEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKK------AEELKKAEEEN 1659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1990 KVKKIAAAEEEAARQRKAaqEELdrlqKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQN 2069
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKA--EEA----KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2070 KLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKD 2133
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1305-2105 |
9.55e-36 |
|
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: 150.59 E-value: 9.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1305 KLDSASDNIIQEYVTLRTRYSELMTLTSQY---IKFitdtqRRLEDEEKAAEKL-----KAEEQKKMAEMQAELDKQKQL 1376
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAekaERY-----KELKAELRELELAllvlrLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1377 AEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLELHELKNLseqqIKDKSQQVDEALKSRLRIEEEIH 1456
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYALANE----ISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1457 LIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELkhksEAERKAANEKQKAL 1536
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL----ETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1537 EDLENlrmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRK 1616
Cdd:TIGR02168 396 ASLNN---EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1617 QQEDAENAREEAERELEkwRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADRE----AKKRSKAEESALKQR--DM 1690
Cdd:TIGR02168 473 AEQALDAAERELAQLQA--RLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSElisvDEGYEAAIEAALGGRlqAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1691 AENELERQRRLAESTAQQKL--AAEQELIRLRADFDNAEQQRSLLEDELYR--LKNEVIAAQQERKQLEDELSKVR---- 1762
Cdd:TIGR02168 551 VVENLNAAKKAIAFLKQNELgrVTFLPLDSIKGTEIQGNDREILKNIEGFLgvAKDLVKFDPKLRKALSYLLGGVLvvdd 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1763 --SEMDILIQLKSR--------------------AEKETMSNTEKSKQLLEAEAtKLRDLAEEASKLRAIAEEAKHQRQL 1820
Cdd:TIGR02168 631 ldNALELAKKLRPGyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEE 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1821 AEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEdQANQHKLEIEEKIVLLk 1900
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEEL- 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1901 kssDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEE 1980
Cdd:TIGR02168 788 ---EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1981 EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ 2060
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1655274923 2061 QKEDSMMqnklkeEYEKAKALARDAEAAKERAEREAALLRQQAEE 2105
Cdd:TIGR02168 945 LSEEYSL------TLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1770-2573 |
1.01e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.45 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 QLKSRAEKETmsnTEKSKQLLEAEATKLRDLAEEASKLRAI---AEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDA 1846
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1847 TRLKTEAEIALKEKEAENERLRRQAED--EAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSDA----EMERQKAIVDDT 1917
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDArkaEAARKAEEERKAEEARKAEDAkkaeAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1918 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKlkniAEETQQS-KLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAA 1996
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1997 AEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvlAQQKEDSMmqNKLKEEYE 2076
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE--AKKKADAA--KKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2077 KAKALARDAEAAKERAE--REAALLRQQAEEAERQKVAAEQEAANQAKAQD--DAERLRKDAEFEAAKLAQAEAAALKQK 2152
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADelKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2153 QQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL 2232
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2233 MKL-KVRIEEEnqrlmkkdkdntqkflVEEAENMKKLAEDAARLSIEAQEAarlrqiaeddlnqqRTLAEKMLKEKMQAI 2311
Cdd:PTZ00121 1552 KKAeELKKAEE----------------KKKAEEAKKAEEDKNMALRKAEEA--------------KKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2312 QEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEyQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKA 2391
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2392 EEEAKKFKKQADTIAARLHEteiatKEQMTEVKKMEFEKLntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMada 2471
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEE-----AKKAEELKKKEAEEK---KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA--- 1749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2472 qqKQIEREMTVLQQTFLTEkemllkkEKLIEDEKKKLESQFEEEIKKakalKDEQDRqrqqMEEEKlKLKATMDAALNKQ 2551
Cdd:PTZ00121 1750 --KKDEEEKKKIAHLKKEE-------EKKAEEIRKEKEAVIEEELDE----EDEKRR----MEVDK-KIKDIFDNFANII 1811
|
810 820
....*....|....*....|....
gi 1655274923 2552 KEAEKD--ILNKQKEMQELERKRL 2573
Cdd:PTZ00121 1812 EGGKEGnlVINDSKEMEDSAIKEV 1835
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
145-269 |
2.12e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.87 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 145 HFQISDIQVNGQSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQA 224
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1655274923 225 FNVAEKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDAMPRTDA 269
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFYHYFSKMKA 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1339-2572 |
4.18e-35 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 148.82 E-value: 4.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1339 TDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELdkqkqlaeaHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEkqkqn 1418
Cdd:NF041483 90 ADAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAE----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1419 iqlelhELKNLSEQQIK---DKSQQVDEALKSRLRIEEEihliRIQLETTVKQKSNAEDElkqlrdRADAAEKLRKlAQE 1495
Cdd:NF041483 156 ------QLRARTESQARrllDESRAEAEQALAAARAEAE----RLAEEARQRLGSEAESA------RAEAEAILRR-ARK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1496 EAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQaeEAERQVKQAEVEKERQIQVA-HVAAQQS 1574
Cdd:NF041483 219 DAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAkEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1575 AAAELRSKQMSFA--ENVSKL-------EESLKQEHGTVLQ-LQQDAERLRKQqedaenareeaerelekwrqkANEALR 1644
Cdd:NF041483 297 ASAESANEQRTRTakEEIARLvgeatkeAEALKAEAEQALAdARAEAEKLVAE---------------------AAEKAR 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1645 lRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSK-AEESALKQRDMAENELERQRRLAESTAQQ-KLAA---------- 1712
Cdd:NF041483 356 -TVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRaAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAkddtkeyrak 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1713 ----EQELIRLRADfdnAEQQRSLLEDELYRLKNE-----VIAAQQERKQLEDELSKVRSEMDiliqlksraEKETMSNT 1783
Cdd:NF041483 435 tvelQEEARRLRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADAD---------ELRSTATA 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1784 EKSKQLLEA--EATKLRDLAE--------EASKLRAIAEE-AKHQRQLAEEDAARQRAEAERILKEKLA-AISDATRLKT 1851
Cdd:NF041483 503 ESERVRTEAieRATTLRRQAEetlertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHT 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1852 EAE-------IALKEKEAENERLRRQAEDEayqrkiledqANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVV 1924
Cdd:NF041483 583 EAEerltaaeEALADARAEAERIRREAAEE----------TERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAE 652
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1925 EEEIRIlKLNFEKASsgkldlelELNKLKNIAEETQQsKLRAE----------EEAEKLRRLVLEEEMRRKEAEDkvkKI 1994
Cdd:NF041483 653 GENVAV-RLRSEAAA--------EAERLKSEAQESAD-RVRAEaaaaaervgtEAAEALAAAQEEAARRRREAEE---TL 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1995 AAAEEEAARQRKAAQEELDRLQKKAdevRKQKEEADKEAEKQIVAAQQAALK-CNMAEQQVQSVlaqqkedsmmqnklke 2073
Cdd:NF041483 720 GSARAEADQERERAREQSEELLASA---RKRVEEAQAEAQRLVEEADRRATElVSAAEQTAQQV---------------- 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2074 eyekakalaRDAEAA-KERAEREAALLRQQAEE-AERQKvaaeqeaanqAKAQDDAERLRKDAefeAAKLAQAEAAALKQ 2151
Cdd:NF041483 781 ---------RDSVAGlQEQAEEEIAGLRSAAEHaAERTR----------TEAQEEADRVRSDA---YAERERASEDANRL 838
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2152 KQQADEEMAKHKKLAEQTlkqkfqveqeltkVKLQLEETDKQKSLLDDELQRLKDEVD--------DAMRQKASVEEELF 2223
Cdd:NF041483 839 RREAQEETEAAKALAERT-------------VSEAIAEAERLRSDASEYAQRVRTEASdtlasaeqDAARTRADAREDAN 905
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2224 KVK----IQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMK-KLAEDAARLSIEAQ-EAARLRQIAEDDLNQQR 2297
Cdd:NF041483 906 RIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQ 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2298 TLAEKMLKekmqaiqEASRLKAEAEM-LQRQKDLAQEQAQKLLEDKQlmqqrldeETEEYQRSLEAERKRQLEIIAEAEK 2376
Cdd:NF041483 986 QHAERIRT-------EAERVKAEAAAeAERLRTEAREEADRTLDEAR--------KDANKRRSEAAEQADTLITEAAAEA 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2377 LKLqvsqLSEAQAKAEEEAKKFKKQADTI--AARLHETEI---ATKEQMTEVKKmefeklnTSKEADDL-------RKAI 2444
Cdd:NF041483 1051 DQL----TAKAQEEALRTTTEAEAQADTMvgAARKEAERIvaeATVEGNSLVEK-------ARTDADELlvgarrdATAI 1119
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2445 TELEKE-KARLKKEAEE-HQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKAL 2522
Cdd:NF041483 1120 RERAEElRDRITGEIEElHERARRESAEQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAAVKKAEGL 1199
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2523 KDEQDRQRQQMEEEKLKLKATMDAalnkqkEAEKDILNKQKEMQELERKR 2572
Cdd:NF041483 1200 LKEAEQKKAELVREAEKIKAEAEA------EAKRTVEEGKRELDVLVRRR 1243
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
40-148 |
7.24e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 130.43 E-value: 7.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1655274923 119 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
161-261 |
3.68e-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: 128.29 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1655274923 241 EDVDVPHPDEKSIITYVSSLY 261
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
164-265 |
4.52e-34 |
|
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: 127.93 E-value: 4.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 242
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655274923 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1442-2359 |
2.03e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 143.74 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1442 DEALKSRLRIEEEI---HLIRIQLETTVKQK-----SNAEDELKQLRD-RADAAEKLRKLAQEEAEKLRKQVSEETQKKr 1512
Cdd:PTZ00121 1039 DDVLKEKDIIDEDIdgnHEGKAEAKAHVGQDeglkpSYKDFDFDAKEDnRADEATEEAFGKAEEAKKTETGKAEEARKA- 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1513 laEEELKHKSEAERKAANEKQKALEDLENLRmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELR-SKQMSFAENVS 1591
Cdd:PTZ00121 1118 --EEAKKKAEDARKAEEARKAEDARKAEEAR-KAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARkAEEVRKAEELR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1592 KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAD 1671
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRS---KAEESAlKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyRLKNEVIAAQ 1748
Cdd:PTZ00121 1275 EEARKADelkKAEEKK-KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEA--KKAAEAAKAE 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1749 QERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQlleaEATKLRDLAEEASKLRAIAEEAKhqrqlaEEDAARQ 1828
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAA---EKKKEEAKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELK------KAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1829 RAEAeriLKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEME 1908
Cdd:PTZ00121 1419 KADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1909 RQKAivdDTLKQRRVVEEEIRILKLNFEKASSgkldlelelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAE 1988
Cdd:PTZ00121 1496 KKKA---DEAKKAAEAKKKADEAKKAEEAKKA---------DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1989 DKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCnmaeQQVQSVLAQQKEDSMMQ 2068
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA----EELKKAEEEKKKVEQLK 1639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2069 NKLKEEYEKAKALARDAEAAKERAEREAallrQQAEEAERQKVAAEQEAANQAKAqddAERLRKDAEfeaaklaqAEAAA 2148
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEA----KKAEEDKKKAEEAKKAEEDEKKA---AEALKKEAE--------EAKKA 1704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2149 LKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKlqlEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQ 2228
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE---EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2229 MEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAArlrqiaeDDLNQQRTLAEKMLKEKM 2308
Cdd:PTZ00121 1782 EEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVA-------DSKNMQLEEADAFEKHKF 1854
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2309 QAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKqlMQQRLDEETEEYQRS 2359
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEEEIEEAD--EIEKIDKDDIEREIP 1903
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1343-2079 |
3.53e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 142.97 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLE 1422
Cdd:PTZ00121 1176 KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1423 LHELKNLSEQQIKDKSQQVDEALKS-------------RLRIEEEIHLIRiQLETTVKQKSNAEDELKQLRDRADAAEKL 1489
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKAdelkkaeekkkadEAKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1490 RKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKAledlENLRMQAEE---AERQVKQAEVEKERQIQV 1566
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----DAAKKKAEEkkkADEAKKKAEEDKKKADEL 1410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1567 AHVAAQQSAAAELRSKqmsfAENVSKLEESLK--QEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKwrQKANEAlr 1644
Cdd:PTZ00121 1411 KKAAAAKKKADEAKKK----AEEKKKADEAKKkaEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAK--KKAEEA-- 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1645 lrlQAEEEAHKKSlaqeeaeKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 1724
Cdd:PTZ00121 1483 ---KKADEAKKKA-------EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1725 NAEQQRSlledelyrlKNEVIAAQQERKQLEDELSKVRsEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEA 1804
Cdd:PTZ00121 1553 KAEELKK---------AEEKKKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1805 SKLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEialkEKEAENERLRRQAEDEayqrkilEDQ 1884
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKAE----EDKKKAEEAKKAEEDE-------KKA 1690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1885 ANQHKLEIEEKivllkkssdaemerQKAivddtlKQRRVVEEEirilklnfEKASSGKLDLELELNKLKniaeeTQQSKL 1964
Cdd:PTZ00121 1691 AEALKKEAEEA--------------KKA------EELKKKEAE--------EKKKAEELKKAEEENKIK-----AEEAKK 1737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1965 RAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRL-QKKADEVRKQKEEADKEAEKQIVAAQQA 2043
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEdEKRRMEVDKKIKDIFDNFANIIEGGKEG 1817
|
730 740 750
....*....|....*....|....*....|....*.
gi 1655274923 2044 ALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 2079
Cdd:PTZ00121 1818 NLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
160-258 |
1.06e-32 |
|
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: 124.07 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1655274923 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
40-144 |
4.15e-32 |
|
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: 124.39 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHRQVK 118
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1655274923 119 LVNIRNDDIADGNPKLTLGLIWTIIL 144
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
45-148 |
1.79e-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: 120.88 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQR-HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1655274923 124 NDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
45-148 |
2.72e-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: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR--EKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1655274923 123 RNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
44-149 |
3.07e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 120.63 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQ-VKLV 120
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
160-258 |
3.11e-31 |
|
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: 119.94 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1655274923 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1343-1922 |
1.45e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 133.52 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEK---LKAEEQKKMAEMQA-ELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQN 1418
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEAELLLlKLRELEAELEELEAELEELEAELEEL----EAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1419 IQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE 1498
Cdd:COG1196 279 LELELEEAQ----AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1499 KLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 1578
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1579 LRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSL 1658
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1659 AQEEAEKQKEEADREAKKRSKAE------ESALKQRDMAENElERQRRLAESTAQQKL--AAEQELIRLRADFDNAEQQR 1730
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEaaleaaLAAALQNIVVEDD-EVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1731 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRsemdILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 1810
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGR----TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1811 AEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQAnqhkL 1890
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE----E 745
|
570 580 590
....*....|....*....|....*....|..
gi 1655274923 1891 EIEEKIVLLKKSSDAEMERQKAIVDDtLKQRR 1922
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELER-LEREI 776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1951-2598 |
1.58e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 134.11 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQ--------RKAAQEELDRLQKKADEV 2022
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkaeeaRKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2023 RKQKEEADKEAEKQIVAAQQAaLKCNMAEQQVQSVLAQQKEDSmmqnKLKEEYEKAKALARDAEAAKERAEREAALLRQQ 2102
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKA-EEVRKAEELRKAEDARKAEAA----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2103 AEEAER-QKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELT 2181
Cdd:PTZ00121 1239 AEEAKKaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2182 KVKLQLEETDKQKSLLDD--ELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMK--LKVRIEEENQRLMKKDKDNTQKF 2257
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeAKKKADAAKKKAEEKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2258 LVEE----AENMKKlAEDAARLSIEAQEAARLRQIAEDdlnqqrtlaekmLKEKMQAIQEASRLKAEAEmlqrQKDLAQE 2333
Cdd:PTZ00121 1399 KAEEdkkkADELKK-AAAAKKKADEAKKKAEEKKKADE------------AKKKAEEAKKADEAKKKAE----EAKKAEE 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2334 QAQKLLEDKQlmQQRLDEETEEYQRSLEAERKrqleiiaeAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETE 2413
Cdd:PTZ00121 1462 AKKKAEEAKK--ADEAKKKAEEAKKADEAKKK--------AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2414 IATKEQmtEVKKM-EFEKLNTSKEADDLRKAiteLEKEKARLKKEAEEHQN----KSKEMADAQQKQIEREMTVLQQTFL 2488
Cdd:PTZ00121 1532 EAKKAD--EAKKAeEKKKADELKKAEELKKA---EEKKKAEEAKKAEEDKNmalrKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2489 TEKEMLLKKE---------KLIEDEKKKLES---QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN-KQKEAE 2555
Cdd:PTZ00121 1607 MKAEEAKKAEeakikaeelKKAEEEKKKVEQlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEED 1686
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1655274923 2556 KDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 2598
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1315-1894 |
2.85e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 132.37 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1315 QEYVTLRTRYSELmtLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEmQAELDKQKQLAEAHAKAIAKAEKEAQEL 1394
Cdd:COG1196 213 ERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1395 KLRMQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAED 1474
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 ELKQL-RDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLrmQAEEAERQV 1553
Cdd:COG1196 366 ALLEAeAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1554 KQAEVEKERQIQVAHVAAQQSaAAELRSKQMSFAENVSKLEESLKQEHgTVLQLQQDAERLRKQQEDAENAREEAERELE 1633
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLEL-LAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1634 KWRQKaneALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAE 1713
Cdd:COG1196 522 LAGAV---AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1714 QELIRLRADFDNAEQQRSLLEDELY---RLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtmsnTEKSKQLL 1790
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAAL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1791 EAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQ 1870
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE 754
|
570 580
....*....|....*....|....
gi 1655274923 1871 AEDEAYQRKILEDQANQHKLEIEE 1894
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEA 778
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
148-263 |
4.86e-30 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 116.86 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 148 ISDIQvngqSEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 227
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274923 228 AEKDLGVTRLLDPEDV-DVPHPDEKSIITYVSSLYDA 263
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1860-2629 |
6.44e-30 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 132.19 E-value: 6.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1860 KEAENERLRRQAEDEAYQ--RKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVE----EEIRILKL 1933
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEarkaEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1934 NFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIaaaeeeaarqRKAAQEELD 2013
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA----------RKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2014 RLQKKADEVRKQKEEAdKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAlardAEAAKERAE 2093
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEA-KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA----DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2094 REAALLRQQAEEAERqkvaaeqeaanqakaqddAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQK 2173
Cdd:PTZ00121 1302 KKADEAKKKAEEAKK------------------ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2174 FQVEQEltkvKLQLEETDKQKslldDELQRLKDEVDDAMRQKASVEEElfkvKIQMEELMKL---KVRIEEENQRLMKKD 2250
Cdd:PTZ00121 1364 EKAEAA----EKKKEEAKKKA----DAAKKKAEEKKKADEAKKKAEED----KKKADELKKAaaaKKKADEAKKKAEEKK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2251 KDNTQKFLVEEaenmKKLAEDAARLSIEAQEAARLRQIAEddlnQQRTLAEkmLKEKMQAIQEASRLKAEAEMLQRQKD- 2329
Cdd:PTZ00121 1432 KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAE----EAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADe 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2330 --LAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAA 2407
Cdd:PTZ00121 1502 akKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2408 RLHETEIATKEQMTEVKKMEFEKlnTSKEADDLRKAitELEKEKARLKKEAEEHQNKSKEMADAQQKQIERemtvlqqtf 2487
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEE--KKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK--------- 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2488 lteKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQE 2567
Cdd:PTZ00121 1649 ---AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2568 LERK-RLEQERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVEKR 2629
Cdd:PTZ00121 1726 EENKiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
41-150 |
8.30e-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: 116.14 E-value: 8.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSQR--HVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHRQ 116
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1655274923 117 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 150
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
164-266 |
8.66e-30 |
|
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: 116.18 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLDPE 241
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1655274923 242 DVDVPHPDEKSIITYVSSLYDAMPR 266
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1450-2042 |
1.42e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.06 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1450 RIEEEIHLIRIQLETTVKQKSNAE--DELKQLRDRADAAEKLRKL--AQEEAEKLRKQVSEETQKKRLAEEELKHKsEAE 1525
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAEL-EAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1526 RKAANEKQKALEDLENlRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVL 1605
Cdd:COG1196 269 LEELRLELEELELELE-EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1606 QLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESAL 1685
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDElskvrsem 1765
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-------- 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1766 diliqlksRAEKETMSNTEKSKQLLEAEATKLRDLAEEAS--KLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAI 1843
Cdd:COG1196 500 --------EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1844 SDATRLkteAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRV 1923
Cdd:COG1196 572 GRATFL---PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1924 VEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAAR 2003
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
570 580 590
....*....|....*....|....*....|....*....
gi 1655274923 2004 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 2042
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
44-146 |
3.88e-29 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 114.12 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
164-265 |
8.37e-29 |
|
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: 113.13 E-value: 8.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLL-WSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 242
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1655274923 243 VDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1519-2109 |
1.36e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1519 KHKSEAERKAANEKQKALED--------LENLRMQAEEAER--QVKQAEVEKERQIQVAH-------VAAQQSAAAELRS 1581
Cdd:COG1196 174 KEEAERKLEATEENLERLEDilgelerqLEPLERQAEKAERyrELKEELKELEAELLLLKlreleaeLEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1582 KQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQE 1661
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1662 EAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLK 1741
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1742 NEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLA 1821
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1822 EEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKK 1901
Cdd:COG1196 494 LLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1902 SSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE 1981
Cdd:COG1196 574 ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAlkcnmAEQQVQSVLAQQ 2061
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER-----LEEELEEEALEE 728
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1655274923 2062 KEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAAlLRQQAEEAERQ 2109
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEE-LERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1521-2355 |
2.61e-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: 126.32 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1521 KSEAERK--AANEKQKALED--------LENLRMQAEEAER--QVKQAEVEKERQIQVAHVaaqQSAAAELRSKQMSFAE 1588
Cdd:TIGR02168 174 RKETERKleRTRENLDRLEDilnelerqLKSLERQAEKAERykELKAELRELELALLVLRL---EELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1589 NVSKLEESLKQEHgtvlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA-LRLRLQAEEEAHKKSlAQEEAEKQK 1667
Cdd:TIGR02168 251 AEEELEELTAELQ----ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLER-QLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1668 eeadreakkrskaeESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAA 1747
Cdd:TIGR02168 326 --------------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1748 QQERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAEatkLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR 1827
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLE---RLEDRRERLQQEIEELLKKLEEAE---LKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1828 QRAEAERILKEKLAAISDATRLKTEAEIAlkekeaenERLRRQAEDEAYQRKILEDQANQ---------HKLEIEEK--- 1895
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSL--------ERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGyea 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1896 ---IVLLKKSSDAEMERQKAIVD--DTLKQ-----------RRVVEEEIRILKLNFEKASSGKLDLELELNKLK------ 1953
Cdd:TIGR02168 538 aieAALGGRLQAVVVENLNAAKKaiAFLKQnelgrvtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1954 ------------NIAEETQQSKLRAEEE-------------------AEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAA 2002
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEVRKQKEeadkEAEKQIVAAQQAALKcnmAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALA 2082
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELE----ELSRQISALRKDLAR---LEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2083 RDAEAAKERAEREAALLRQQAEEAERQKvaaEQEAANQAKAQDDAERLRKDAefeaaklaqaeAAALKQKQQADEEMAKH 2162
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEEL---KALREALDELRAELTLLNEEA-----------ANLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2163 KKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEE 2242
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2243 NQRLMKKDKD---NTQKFLVEEAENMKKLAEDAarlSIEAQEAARLRQIAEDDLNQQR---TLAEKMLKE----KMQAIQ 2312
Cdd:TIGR02168 917 LEELREKLAQlelRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARrrlKRLENKIKElgpvNLAAIE 993
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1655274923 2313 EASRLKAEAEMLQRQKDLAQEQAQKLLEdkqlMQQRLDEETEE 2355
Cdd:TIGR02168 994 EYEELKERYDFLTAQKEDLTEAKETLEE----AIEEIDREARE 1032
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1350-2232 |
2.83e-28 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 126.48 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1350 KAAEKLKAEEQKKMAEMQAELDkqKQLAEAHAKA-----------IAKAEKEAQELKLRMQEEVSKRETAAVD------- 1411
Cdd:NF041483 323 KEAEALKAEAEQALADARAEAE--KLVAEAAEKArtvaaedtaaqLAKAARTAEEVLTKASEDAKATTRAAAEeaerirr 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1412 -AEKQKQNIQLELHELKNLSEQQIKDKSQQV--------DEALKSR-----LRIEEEIHLIRIQLET---TVKQKSNAED 1474
Cdd:NF041483 401 eAEAEADRLRGEAADQAEQLKGAAKDDTKEYraktvelqEEARRLRgeaeqLRAEAVAEGERIRGEArreAVQQIEEAAR 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 ELKQLRDRADA-AEKLRKLAQEEAEKLRKQVSEE-TQKKRLAEEELKH-KSEAERKAAnekqKALEDLENLRMQAEEAER 1551
Cdd:NF041483 481 TAEELLTKAKAdADELRSTATAESERVRTEAIERaTTLRRQAEETLERtRAEAERLRA----EAEEQAEEVRAAAERAAR 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1552 QVKQaevEKERQIQvahvAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDA----ERLR----------KQ 1617
Cdd:NF041483 557 ELRE---ETERAIA----ARQAEAAEELTRLHTEAEERLTAAEEALADARAEAERIRREAaeetERLRteaaerirtlQA 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1618 QEDAENAREEAERELEKWRQKA---NEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKR---------SKAEESAL 1685
Cdd:NF041483 630 QAEQEAERLRTEAAADASAARAegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaaealAAAQEEAA 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRDMAENELERQRRLAESTAQQKLAAEQELI---RLRADFDNAEQQRsLLEDELYRLKNEVIAAQQERKQLEDELSKVR 1762
Cdd:NF041483 710 RRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLQ 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1763 SEMDILIQ-LKSRAE---KETMSNTEKSKQLLEAEATKLRDLA-EEASKLRAIA-EEAKHQRQLAEEDAARQRAEAERIL 1836
Cdd:NF041483 789 EQAEEEIAgLRSAAEhaaERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLR 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1837 KEklaAISDATRLKTEAEIALKEKEAENERLRRQAEDEAyqRKILEDQANQHKLEIEEkivllkKSSDAEMERQKAIVDD 1916
Cdd:NF041483 869 SD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGE------ATSEAERLTAEARAEA 937
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1917 TLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSklrAEEEAEKLRRlvlEEEMRRKEAEdkvkkiaa 1996
Cdd:NF041483 938 ERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGS---AQQHAERIRT---EAERVKAEAA-------- 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1997 aeEEAARQRKAAQEELDRL------------QKKADEVRKQKEEADKEAEKQIVAAQQAALKCNM-AEQQVQS-VLAQQK 2062
Cdd:NF041483 1004 --AEAERLRTEAREEADRTldearkdankrrSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTeAEAQADTmVGAARK 1081
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2063 EDSMMQNKLKEE----YEKAKAlarDAEAAKERAEREAALLRQQAEEAeRQKVAAEQEAANQAKAQDDAERLRKDAEFEA 2138
Cdd:NF041483 1082 EAERIVAEATVEgnslVEKART---DADELLVGARRDATAIRERAEEL-RDRITGEIEELHERARRESAEQMKSAGERCD 1157
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2139 AKLAQAEAAALKQKQQADEEMAKHK-----------KLAEQTLKQKFQVEQELTKvklqleETDKQKSLLDDELQRL--- 2204
Cdd:NF041483 1158 ALVKAAEEQLAEAEAKAKELVSDANseaskvriaavKKAEGLLKEAEQKKAELVR------EAEKIKAEAEAEAKRTvee 1231
|
970 980
....*....|....*....|....*....
gi 1655274923 2205 -KDEVDDAMRQKASVEEELFKVKIQMEEL 2232
Cdd:NF041483 1232 gKRELDVLVRRREDINAEISRVQDVLEAL 1260
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
166-261 |
4.53e-28 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 110.90 E-value: 4.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 244
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1655274923 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1486-2472 |
1.15e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 124.55 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1486 AEKLRKLAQEEAEKLRKQVSEETQKKRlAEEELKHKSEAERKAanekqkaledlenlRMQAE---EA--ERQVKQAEVEK 1560
Cdd:NF041483 74 AEQLLRNAQIQADQLRADAERELRDAR-AQTQRILQEHAEHQA--------------RLQAElhtEAvqRRQQLDQELAE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1561 ERQIQVAHVAAQQSAAAELRSKQMSFAENVskLEESLKQEHGTVLQLQQDAERLRKQ--QEDAENAREEAERELEKWRQK 1638
Cdd:NF041483 139 RRQTVESHVNENVAWAEQLRARTESQARRL--LDESRAEAEQALAAARAEAERLAEEarQRLGSEAESARAEAEAILRRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1639 ANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQR-DMAENELERQRRLAEST-AQQKLAAEQEL 1716
Cdd:NF041483 217 RKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRmQEAEEALREARAEAEKVvAEAKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1717 IrlRADFDNaEQQRSLLEDELYRLKNEVIA-AQQERKQLEDELSKVRSEMDILI-----QLKSRAEKETMSNTEKSKQLL 1790
Cdd:NF041483 297 A--SAESAN-EQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVaeaaeKARTVAAEDTAAQLAKAARTA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1791 EAEATKLRDLAEEASklRAIAEEAKHQRQLAEEDAARQRAEAERILKE-KLAAISD--------------ATRLKTEAEI 1855
Cdd:NF041483 374 EEVLTKASEDAKATT--RAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDtkeyraktvelqeeARRLRGEAEQ 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1856 ALKEKEAENERLRRQAEDEAYQRkiLEDQANQhkleIEEkiVLLKKSSDAEMERQKAIVDdtlkQRRVVEEEIrilklnf 1935
Cdd:NF041483 452 LRAEAVAEGERIRGEARREAVQQ--IEEAART----AEE--LLTKAKADADELRSTATAE----SERVRTEAI------- 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1936 EKASSgkldlelelnkLKNIAEETQQsklRAEEEAEKLRRLVLEE-EMRRKEAEDKVKKIAAAEEEAARQRKA-AQEELD 2013
Cdd:NF041483 513 ERATT-----------LRRQAEETLE---RTRAEAERLRAEAEEQaEEVRAAAERAARELREETERAIAARQAeAAEELT 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2014 RLQKKADEVRKQKEEADKEAEKQIV-----AAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEyekakaLARDAEAA 2088
Cdd:NF041483 579 RLHTEAEERLTAAEEALADARAEAErirreAAEETERLRTEAAERIRTLQAQAEQEA---ERLRTE------AAADASAA 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2089 KERAEREAALLRQQA-EEAERQKvaaeqeaanqAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQqadEEMAKHKKLAE 2167
Cdd:NF041483 650 RAEGENVAVRLRSEAaAEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQ---EEAARRRREAE 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2168 QTL-KQKFQVEQELTKVKLQLEE----TDKQKSLLDDELQRLKDEVD-------DAMRQKA-SVEEELFKVKIQM-EELM 2233
Cdd:NF041483 717 ETLgSARAEADQERERAREQSEEllasARKRVEEAQAEAQRLVEEADrratelvSAAEQTAqQVRDSVAGLQEQAeEEIA 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2234 KLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQ-------------------EAARLRQIAEDDLN 2294
Cdd:NF041483 797 GLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQeeteaakalaertvseaiaEAERLRSDASEYAQ 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2295 QQRTLAEKMLKekmQAIQEASRLKAEA-EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAE-----RKRQL 2368
Cdd:NF041483 877 RVRTEASDTLA---SAEQDAARTRADArEDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEaraeaERVRA 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2369 EIIAEAEKLKLQVS----QLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEK-LNTSKEADDLRKA 2443
Cdd:NF041483 954 DAAAQAEQLIAEATgeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRtLDEARKDANKRRS 1033
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1655274923 2444 ---------ITELEKEKARLKKEAEEHQNKSKEMADAQ 2472
Cdd:NF041483 1034 eaaeqadtlITEAAAEADQLTAKAQEEALRTTTEAEAQ 1071
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1974-2605 |
1.92e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.12 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1974 RRLVLEE-------EMRRKEAEdkvkkiaaaeeeaaRQRKAAQEELDRLQKKADEVRKQKEEADKEAEK----QIVAAQQ 2042
Cdd:COG1196 157 RRAIIEEaagiskyKERKEEAE--------------RKLEATEENLERLEDILGELERQLEPLERQAEKaeryRELKEEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2043 AALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK 2122
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2123 AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQ 2202
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2203 RLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmkkdKDNTQKFLVEEAENMKKLAEDAARLSIEAQEA 2282
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2283 ARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQ------------------- 2343
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLrglagavavligveaayea 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2344 --------LMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQA-DTIAARLHETEI 2414
Cdd:COG1196 539 aleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAsDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2415 ATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQtfltEKEML 2494
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA----EEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2495 LKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQElERKRLE 2574
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER-ELERLE 773
|
650 660 670
....*....|....*....|....*....|....*....
gi 1655274923 2575 QER-------VLA-DENQKLREKLQQMEEaQKSTLITEK 2605
Cdd:COG1196 774 REIealgpvnLLAiEEYEELEERYDFLSE-QREDLEEAR 811
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
148-263 |
2.61e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 109.40 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 148 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 227
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274923 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
146-263 |
3.63e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 109.02 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 146 FQISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAF 225
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 226 NVAEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1342-2268 |
1.27e-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: 120.85 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAE----KLKAEEQKKMAEMQAELDKQ---KQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEK 1414
Cdd:pfam02463 153 ERRLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1415 QKQNIQLELHELKNLSEQQIKDKSQQVDEAlksrlRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQ 1494
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1495 EEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQS 1574
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1575 AAAELRSKQMSFAENVSKLEESLKQEhgtvLQLQQDAERLRKQQEDAenareeaerelekwrqKANEALRLRLQAEEEAH 1654
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLEL----ARQLEDLLKEEKKEELE----------------ILEEEEESIELKQGKLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1655 KKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLE 1734
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1735 DELYRLKnEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEA 1814
Cdd:pfam02463 528 HGRLGDL-GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1815 KHQRQLAEEDAARQRAeAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEE 1894
Cdd:pfam02463 607 QLDKATLEADEDDKRA-KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1895 KIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFekassgkldLELELNKLKNIAEETQQSKLRAEEEAEKLR 1974
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR---------VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1975 RLVLEEEMRRKEAEDKVKKIAAAEEEAARQrKAAQEELDRLQKKADEVRKQKEEADKEAEKQivaaQQAALKCNMAEQQV 2054
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKL-KVEEEKEEKLKAQEEELRALEEELKEEAELL----EEEQLLIEQEEKIK 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2055 QSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDA 2134
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2135 EFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKF-----QVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVD 2209
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEennkeEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2210 DAMRQKASVEEElfKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKL 2268
Cdd:pfam02463 992 KDELEKERLEEE--KKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1672-2560 |
3.63e-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: 119.31 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQER 1751
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1752 KQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLA-EEASKLRAIAEEAKHQRQLAEEDAARQRA 1830
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLkLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1831 EAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK--------ILEDQANQHKLEIEEKIVLLKKS 1902
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEserlssaaKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1903 SDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKniAEETQQSKLRAEEEAEKLRRLVLEEEM 1982
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE--LELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1983 RRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQK 2062
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2063 EDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLA 2142
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2143 QAEAAALKQKQQADEEMAKHKK--LAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddamrqkasvee 2220
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKelLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE------------- 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2221 elfKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLA 2300
Cdd:pfam02463 719 ---AEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEASRLKAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEaeKLKLQ 2380
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK--EELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2381 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEK-ARLKKEAE 2459
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLlEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2460 EHQNKSKEMADAQQKQIERE-------MTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQ 2532
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEelgkvnlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
890 900
....*....|....*....|....*...
gi 1655274923 2533 MEEEKLKLKATMDAALNKQKEAEKDILN 2560
Cdd:pfam02463 1031 KGWNKVFFYLELGGSAELRLEDPDDPFS 1058
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
44-146 |
4.00e-26 |
|
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: 105.65 E-value: 4.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
44-149 |
4.27e-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: 106.27 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1788-2598 |
6.34e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.62 E-value: 6.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1788 QLLEAEATKLRDLAEEA---SKLRAIAEEAkhQRQLAEEDAARQRAEAerILKEKLAAISdatRLKTEAEIALKEKEAEN 1864
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAagiSKYKERRKET--ERKLERTRENLDRLED--ILNELERQLK---SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1865 ERlrrqaedEAYQRKILEDQANQHKLEIEEKivllkKSSDAEMERQKAIVDDTLKqrrVVEEEIRILKLNFEKASSGKLD 1944
Cdd:TIGR02168 221 EL-------RELELALLVLRLEELREELEEL-----QEELKEAEEELEELTAELQ---ELEEKLEELRLEVSELEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1945 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 2024
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIVAAQQAALKCNMAEQQvqsvlaqqkedsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAE 2104
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQ--------------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2105 EAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQE----L 2180
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkaL 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2181 TKVKLQLE----------ETDKQKSL-----LDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQR 2245
Cdd:TIGR02168 512 LKNQSGLSgilgvlseliSVDEGYEAaieaaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2246 LMKKDKDNTQKFLVEEAENMKKLA----------------EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQ 2309
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2310 AI---QEASRLKAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSE 2386
Cdd:TIGR02168 672 ILerrREIEELEEKIEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2387 AQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKsK 2466
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-L 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2467 EMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 2546
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE-ELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2547 ALNKQKEAEKDILNKQKEMQELERkRLEQERVLADENQ-KLREKLQQMEEAQK 2598
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQeRLSEEYSLTLEEAE 957
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
39-148 |
9.14e-26 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 105.23 E-value: 9.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 39 KDERDRVQKKTFTKWVNKHLIKSQRHV--TDLYEDLRDGHNLISLLEVLSGDTLPR-EKGRMRFHKLQNVQIALDFLRHR 115
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 1655274923 116 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
148-263 |
3.51e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 103.27 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 148 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 227
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274923 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
164-263 |
3.59e-25 |
|
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: 102.75 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED- 242
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1655274923 243 VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
794-860 |
5.25e-25 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 100.80 E-value: 5.25e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 794 QLKPRNptTPIKGNLPVQAVCDFKQVEITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPSVCFLVP 860
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
48-145 |
1.71e-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: 100.47 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 48 KTFTKWVNKHLIKS-QRHVTDLYEDLRDGHNLISLLEVLSGDTLPREK---GRMRFHKLQNVQIALDFLRHRQVKLVNIR 123
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1655274923 124 NDDIADGnPKLTLGLIWTIILH 145
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
161-261 |
2.01e-24 |
|
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: 100.58 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1655274923 241 EDV---DVphPDEKSIITYVSSLY 261
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
160-266 |
3.12e-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: 100.05 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 160 MSAKEKLLLWSQRMTDGY-QGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY--RQTNLENLEQAFNVAEKDLGVTR 236
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1655274923 237 -LLDPEDVDvpHPDEKSIITYVSSLYDAMPR 266
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1787-2376 |
4.28e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1787 KQLLEAEATKLRDLaeeasKLRAIAEEAKHQRQLAEEDAARQraeaerilkeklaaisdatrlktEAEIALKEKEAENER 1866
Cdd:COG1196 222 LKELEAELLLLKLR-----ELEAELEELEAELEELEAELEEL-----------------------EAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1867 LRRQAEDEAYQRKILEDQANQHKLE--IEEKIVLLKKSSDAEMERQKAivddtlkqrrvvEEEIRILKLNFEKASSGKLD 1944
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELArlEQDIARLEERRRELEERLEEL------------EEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1945 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 2024
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAE 2104
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2105 EAErQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKfqveqELTKVK 2184
Cdd:COG1196 502 DYE-GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA-----KAGRAT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2185 LQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEN 2264
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2265 MKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQL 2344
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570 580 590
....*....|....*....|....*....|..
gi 1655274923 2345 MQQRLDEETEEYQRSLEAERKRQLEIIAEAEK 2376
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
166-261 |
7.45e-24 |
|
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: 98.76 E-value: 7.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 166 LLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED-VD 244
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1655274923 245 VPHPDEKSIITYVSSLY 261
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
148-263 |
8.94e-24 |
|
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: 99.38 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 148 ISDIQVngqsEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNV 227
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1655274923 228 AEKDLGVTRLLDPED-VDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1315-2211 |
1.41e-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: 110.83 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1315 QEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 1394
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1395 KLrmqeevSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEeihliRIQLETTVKQKSNAED 1474
Cdd:pfam02463 246 LR------DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-----KSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 ELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVK 1554
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1555 QAEVEKERQIQvahvaaQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQdaERLRKQQEDAENAREEAERELEK 1634
Cdd:pfam02463 395 EELELKSEEEK------EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ--GKLTEEKEELEKQELKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1635 WRQKANEALRLRLQAEEEAHKK----SLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKL 1710
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELllsrQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1711 AAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVrsEMDILIQLKSRAEKETMSNTEKSKQLL 1790
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL--EIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1791 EAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKlaaisdaTRLKTEAEIALKEKEAENERLRRQ 1870
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTK-------ELLEIQELQEKAESELAKEEILRR 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1871 AEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRilklnfEKASSGKLDLELELN 1950
Cdd:pfam02463 698 QLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------LKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEAD 2030
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2031 KEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAErqk 2110
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAE--- 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2111 vaAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMaKHKKLAEQTLKQKFQVEQELTKVKLQLEET 2190
Cdd:pfam02463 929 --ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV-NLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
890 900
....*....|....*....|.
gi 1655274923 2191 DKQKSLLDDELQRLKDEVDDA 2211
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELF 1026
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
164-264 |
1.80e-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: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPEDV 243
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1655274923 244 DVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1676-2460 |
1.93e-23 |
|
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: 110.53 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1676 KRSKAEESALkQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLE 1755
Cdd:TIGR02168 216 KELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1756 DELSKVrsEMDILIQLKSRAEKETmSNTEKSKQLLEAEAtKLRDLAEEASKLRAIAEEAKHQRQLAEED---AARQRAEA 1832
Cdd:TIGR02168 295 NEISRL--EQQKQILRERLANLER-QLEELEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAEleeLEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1833 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKA 1912
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1913 IVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE----------- 1981
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlse 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 ------------------------MRRKEA---------EDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKE- 2027
Cdd:TIGR02168 528 lisvdegyeaaieaalggrlqavvVENLNAakkaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDl 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2028 -EADKEAEK---------------QIVAAQQAALKCNM-------------------AEQQVQSVLAQQKEDSmmqnKLK 2072
Cdd:TIGR02168 608 vKFDPKLRKalsyllggvlvvddlDNALELAKKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIE----ELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2073 EEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQK 2152
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2153 QQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL 2232
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2233 MKLKVRIEEENQRLmkkdkdntqkflveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 2312
Cdd:TIGR02168 844 EEQIEELSEDIESL---------------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2313 EASRLKAEAEMLQRQKDLAQEQAQKLledKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQakae 2392
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI---- 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2393 eeakkfkkqadtiaARLHETEIATKEQMTEVKKmEFEKLNTSKEadDLRKAITELEKEKARLKKEAEE 2460
Cdd:TIGR02168 982 --------------KELGPVNLAAIEEYEELKE-RYDFLTAQKE--DLTEAKETLEEAIEEIDREARE 1032
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
45-148 |
3.03e-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: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQRH--VTDLYEDLRDGHNLISLLEVLSGDTLP-REKGRMRFHKLQNVQIALDFLRHRQ-VKLV 120
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
162-265 |
6.82e-23 |
|
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: 96.01 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 162 AKEKLLLWSQRMTDGYqGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 241
Cdd:cd21245 4 AIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEPE 82
|
90 100
....*....|....*....|....
gi 1655274923 242 DVDVPHPDEKSIITYVSSLYDAMP 265
Cdd:cd21245 83 DVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1696-2581 |
1.48e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 107.60 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1696 ERQRRLAESTAQQKLA-AEQELIRLRAdfdnaEQQRSLLE--DELYRLKNEVIA-AQQERKQLEDELSKVRSEMDILI-- 1769
Cdd:NF041483 75 EQLLRNAQIQADQLRAdAERELRDARA-----QTQRILQEhaEHQARLQAELHTeAVQRRQQLDQELAERRQTVESHVne 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 ------QLKSRAEK-------ETMSNTEKSKQLLEAEATKLrdlAEEASklRAIAEEAKHQRQLAEEDAARQRAEAERIL 1836
Cdd:NF041483 150 nvawaeQLRARTESqarrlldESRAEAEQALAAARAEAERL---AEEAR--QRLGSEAESARAEAEAILRRARKDAERLL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1837 K-------------EKL----AAISDATRLK------------TEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQ 1887
Cdd:NF041483 225 NaastqaqeatdhaEQLrsstAAESDQARRQaaelsraaeqrmQEAEEALREARAEAEKVVAEAKEAAAKQLASAESANE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1888 HKLEI-EEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEeiRILKLNFEKA-SSGKLDLELELNKLKNIAEE------- 1958
Cdd:NF041483 305 QRTRTaKEEIARLVGEATKEAEALKAEAEQALADARAEAE--KLVAEAAEKArTVAAEDTAAQLAKAARTAEEvltkase 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1959 -TQQSKLRAEEEAEKLRRLVLEEEMR-RKEAEDKVKKIAAAEEEAARQRKAA----QEELDRLQKKADEVR--------K 2024
Cdd:NF041483 383 dAKATTRAAAEEAERIRREAEAEADRlRGEAADQAEQLKGAAKDDTKEYRAKtvelQEEARRLRGEAEQLRaeavaegeR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIV-AAQQAALKCNMAEQQVQSVLAQQKEDSmmQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQA 2103
Cdd:NF041483 463 IRGEARREAVQQIEeAARTAEELLTKAKADADELRSTATAES--ERVRTEAIERATTLRRQAEETLERTRAEAERLRAEA 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2104 EE-AERQKvaaeqeaanqAKAQDDAERLRKDAEfeaaklaqaeAAALKQKQQADEEMAKHKKLAEQTLKQkfqVEQELTK 2182
Cdd:NF041483 541 EEqAEEVR----------AAAERAARELREETE----------RAIAARQAEAAEELTRLHTEAEERLTA---AEEALAD 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2183 VKLQ--------LEETDKQK-----------SLLDDELQRLKDE-VDDAMRQKAsvEEELFKVKIQME---ELMKLKVRI 2239
Cdd:NF041483 598 ARAEaerirreaAEETERLRteaaerirtlqAQAEQEAERLRTEaAADASAARA--EGENVAVRLRSEaaaEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2240 EEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEA-ARLRQIAEDDLNQQRTLAEKML----KEKMQAIQEA 2314
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETlGSARAEADQERERAREQSEELLasarKRVEEAQAEA 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2315 SRLKAEAEmlQRQKDL---AQEQAQKLLEDKQLMQQRLDEETEEYQRSLE--AERKRQlEIIAEAEKLK----LQVSQLS 2385
Cdd:NF041483 756 QRLVEEAD--RRATELvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEhaAERTRT-EAQEEADRVRsdayAERERAS 832
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2386 EAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTskEADDlrkAITELEKEKARLKKEAEEHQNKS 2465
Cdd:NF041483 833 EDANRLRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRT--EASD---TLASAEQDAARTRADAREDANRI 907
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2466 KEMADAQQKQIEREMTVlqqtfltekemllKKEKLIEDEKKKLESQFEEEIKKAkalkdEQDRQRQQMEEEKLKLKATMD 2545
Cdd:NF041483 908 RSDAAAQADRLIGEATS-------------EAERLTAEARAEAERLRDEARAEA-----ERVRADAAAQAEQLIAEATGE 969
|
970 980 990
....*....|....*....|....*....|....*.
gi 1655274923 2546 AALNKQKEAEkdilNKQKEMQELERKRLEQERVLAD 2581
Cdd:NF041483 970 AERLRAEAAE----TVGSAQQHAERIRTEAERVKAE 1001
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1942-2545 |
1.55e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1942 KLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEmrrkEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE 2021
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2022 VRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQ 2101
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2102 QAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELT 2181
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2182 KVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqkasveEELFKVKIQMEELMKLKVRIEeenqrlmKKDKDNTQKFLVEE 2261
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEA--------AARLLLLLEAEADYEGFLEGV-------KAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2262 AENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKM--QAIQEASRLKAEAEMLQRQKDLAQEQAQKLL 2339
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2340 EDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQ 2419
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2420 MTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEK 2499
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2500 LiEDEKKKLESQFE----------EEIKKAKALKDEQDRQRQQMEEEKLKLKATMD 2545
Cdd:COG1196 765 L-ERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIE 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1245-1843 |
1.59e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1245 LKEQLAKEKKLLEEIEKNKDKVDEcqkyakayidiikdYELQLVAYKAQVEPLTspLKKTKLDSASDNIIQEYVTLRTRY 1324
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEE--------------LEAELAELEAELEELR--LELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1325 SELmtltSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK 1404
Cdd:COG1196 298 ARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1405 RETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETtvkqksnAEDELKQLRDRAD 1484
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAE-------LEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1485 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELkhksEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQI 1564
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAAL----AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1565 QVAHVAAQQSAAAELRskqmsfAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAenareeaerelekwRQKANEALR 1644
Cdd:COG1196 522 LAGAVAVLIGVEAAYE------AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG--------------RATFLPLDK 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1645 LRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 1724
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1725 NAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEA 1804
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
570 580 590
....*....|....*....|....*....|....*....
gi 1655274923 1805 SKLRAIAEEAKHQRQLAEEDAARQRAEAERiLKEKLAAI 1843
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEELERELER-LEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1342-1855 |
3.65e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.76 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELKlRMQEEVSKRETAAVDAEKQKQniql 1421
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE-------EDKKKADELK-KAAAAKKKADEAKKKAEEKKK---- 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1422 elhelknlsEQQIKDKSQQVDEALKSRLRIEEeihliriqlettvkqKSNAEdELKQLRDRADAAEKLRKLAQEeaeklr 1501
Cdd:PTZ00121 1433 ---------ADEAKKKAEEAKKADEAKKKAEE---------------AKKAE-EAKKKAEEAKKADEAKKKAEE------ 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1502 KQVSEETQKKrlaEEELKHKSEAERKAANEKQKAledlENLRmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELR- 1580
Cdd:PTZ00121 1482 AKKADEAKKK---AEEAKKKADEAKKAAEAKKKA----DEAK-KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1581 SKQMSFAENVSKLEESLKQEHGTVLQLQQdAERLRKQQEDAENAREEAERELEKwrQKANEAlrlrlQAEEEAHKKSlaq 1660
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLYEEEKK--MKAEEA-----KKAEEAKIKA--- 1622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1661 eeaekqkeeadREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyRL 1740
Cdd:PTZ00121 1623 -----------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KK 1689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1741 KNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKlrdlAEEASKLRAIAEEAKHQRQL 1820
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKE 1765
|
490 500 510
....*....|....*....|....*....|....*
gi 1655274923 1821 AEEDAARQRAEAERILKEKLAAISDATRLKTEAEI 1855
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1338-2384 |
1.61e-21 |
|
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: 104.10 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1338 ITDTQRRLEDEEKAAEKLKAE---------------------------EQKKMAEMQAELDKQKQLAEAHAKAIAKAEKE 1390
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEkvtteakikkleedillledqnsklskERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1391 AQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKS 1470
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQ----EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKN 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1471 NAEDELKQLRDR-ADAAEKL--RKLAQEEAEKLRKQVSEE----------TQKKRLAEEELKHKSEAErkaANEKQKALE 1537
Cdd:pfam01576 261 NALKKIRELEAQiSELQEDLesERAARNKAEKQRRDLGEElealkteledTLDTTAAQQELRSKREQE---VTELKKALE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1538 DlENLRMQAEEAERQVKQAEVEKERQIQVAHvaAQQSAAAELRSKQMSFAENvskleESLKQEHGTVLQLQQDAERLRKQ 1617
Cdd:pfam01576 338 E-ETRSHEAQLQEMRQKHTQALEELTEQLEQ--AKRNKANLEKAKQALESEN-----AELQAELRTLQQAKQDSEHKRKK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1618 QEDAENAREEaerelekwrqKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELER 1697
Cdd:pfam01576 410 LEGQLQELQA----------RLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1698 QRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKnevIAAQQERKQLEDELSKVRSEMDILIQLKSRAEK 1777
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQ---AQLSDMKKKLEEDAGTLEALEEGKKRLQRELEA 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1778 ETMSNTEKSKQLLEAEATKLRdLAEEaskLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEIAL 1857
Cdd:pfam01576 557 LTQQLEEKAAAYDKLEKTKNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEA 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1858 KEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivlLKKSSDA------EMERQKAIVDDTLKQRRVVEEEiriL 1931
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMED----LVSSKDDvgknvhELERSKRALEQQVEEMKTQLEE---L 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1932 KLNFEKASSGKLDLELELNKLKNIAEETQQSKlraEEEAEKLRRLvLEEEMRRKEAEdkvkkiaaaeeeaarqrkaaqEE 2011
Cdd:pfam01576 705 EDELQATEDAKLRLEVNMQALKAQFERDLQAR---DEQGEEKRRQ-LVKQVRELEAE---------------------LE 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2012 LDRLQKKADEVRKQKEEAD-KEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEaaKE 2090
Cdd:pfam01576 760 DERKQRAQAVAAKKKLELDlKELEAQIDAANKGR---EEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE--KK 834
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2091 RAEREAALLRQQAEEAErqkvaaeqeaanqakaqddAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAKHKKLAEQTL 2170
Cdd:pfam01576 835 LKNLEAELLQLQEDLAA-------------------SERARRQAQ--------------QERDELADEIASGASGKSALQ 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2171 KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKA---SVEEELFKVKIQMEELMK-LKVRIEEENQRL 2246
Cdd:pfam01576 882 DEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAaerSTSQKSESARQQLERQNKeLKAKLQEMEGTV 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2247 MKKDKDNTQKFlveEAenmkKLAEDAARLSIEAQEaarlRQIAEDDLNQqrtlAEKMLKEKMqaiqeasrLKAEAEmlQR 2326
Cdd:pfam01576 962 KSKFKSSIAAL---EA----KIAQLEEQLEQESRE----RQAANKLVRR----TEKKLKEVL--------LQVEDE--RR 1016
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2327 QKDLAQEQAQKL-LEDKQLMQQrLDEETEEYQRSLEAERK--RQLEIIAE-AEKLKLQVSQL 2384
Cdd:pfam01576 1017 HADQYKDQAEKGnSRMKQLKRQ-LEEAEEEASRANAARRKlqRELDDATEsNESMNREVSTL 1077
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
161-261 |
1.81e-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: 92.02 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1655274923 241 EDVDV--PHPDEKSIITYVSSLY 261
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1241-2226 |
2.17e-21 |
|
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: 103.72 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1241 DSKTLKEQLAKEKKLLEEI--------EKNKDKVDECQKYAKAYIDIIKDYELQLVA-----YKAQVEPLTSPLKKTK-- 1305
Cdd:pfam01576 58 EAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQLEKVTTEAKIKKle 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1306 -----LDSASDNIIQEYVTLRTRYSELMT--------------LTSQYIKFITDTQRRLEDEEKA---AEKLKAEEQKKM 1363
Cdd:pfam01576 138 edillLEDQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1364 AEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAavdaekQKQNIQLELHelknLSEQQ--IKDKSQQV 1441
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA------LKKIRELEAQ----ISELQedLESERAAR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1442 DEALKSRLRIEEEIHLIRIQLETTVkQKSNAEDELKQLRDRAdaAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHK 1521
Cdd:pfam01576 288 NKAEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQE--VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1522 SEAER--KAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQ 1599
Cdd:pfam01576 365 LEQAKrnKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1600 EHGTVLQLQQDAERLRKQ-QEDAENAREEAERELEKWRQKANEALRLRlQAEEEahKKSLAQEEaekqkeeaDREAKKRS 1678
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDvSSLESQLQDTQELLQEETRQKLNLSTRLR-QLEDE--RNSLQEQL--------EEEEEAKR 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1679 KAEesalKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLkneviaaQQERKQLEDEL 1758
Cdd:pfam01576 514 NVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------EKTKNRLQQEL 582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1759 SKVRSEMDILIQLKSRAEKETmsntEKSKQLLEAEATKLRDLAEEASKLRAIAEEaKHQRQL----AEEDAARQRAEAER 1834
Cdd:pfam01576 583 DDLLVDLDHQRQLVSNLEKKQ----KKFDQMLAEEKAISARYAEERDRAEAEARE-KETRALslarALEEALEAKEELER 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1835 ILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSDAEM---- 1907
Cdd:pfam01576 658 TNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDElqaTEDAKLRLEVNMQALKAQFERDLqard 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ----ERQKAIVddtlKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEET---------QQSKLRAE------- 1967
Cdd:pfam01576 738 eqgeEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAAnkgreeavkQLKKLQAQmkdlqre 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1968 -EEAEKLRRLVL----EEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK-ADEVRKQKEEADkeaEKQIVAAQ 2041
Cdd:pfam01576 814 lEEARASRDEILaqskESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEiASGASGKSALQD---EKRRLEAR 890
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2042 QAALKCNMAEQQ--VQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAE-----RQKVAAE 2114
Cdd:pfam01576 891 IAQLEEELEEEQsnTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEgtvksKFKSSIA 970
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2115 QEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQK 2194
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE----RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
1050 1060 1070
....*....|....*....|....*....|..
gi 1655274923 2195 SLLDDELQRLKDEVDDAMRQKASVEEELFKVK 2226
Cdd:pfam01576 1047 SRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1672-2485 |
2.68e-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: 103.21 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAENELERQRRLAEstAQQKLAaeQELIRLRADFDNAEQQRSL-----LEDELYRLKNEVIA 1746
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLE--RQAEKA--ERYKELKAELRELELALLVlrleeLREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1747 AQQERKQLEDELSKVRSEMDILIQLKSRAEKEtmsntekskqlLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAA 1826
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1827 RQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQanqhkleieekivllkkssDAE 1906
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL-------------------EEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1907 MERQKAIVDDTLKQRRVVEEEIRILKlnfekasSGKLDLELELNKLKNIAEETQQSKLRAE-----EEAEKLRRLVLEEE 1981
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLE-------ARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELEELQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEkqivaaqqaALKCNMAEQQVQSVLAQQ 2061
Cdd:TIGR02168 454 EELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE---------GVKALLKNQSGLSGILGV 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2062 KEDSMmqnKLKEEYEKA--KALARDAEAA----KERAEREAALLRQqaEEAERQKVAAEQEAANQAKAQDDAERLRKDAE 2135
Cdd:TIGR02168 525 LSELI---SVDEGYEAAieAALGGRLQAVvvenLNAAKKAIAFLKQ--NELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2136 FEAAKLAQAEAAALKQK------------QQADEEMAKHKKL-----------------------AEQTLKQKFQVEQEL 2180
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKalsyllggvlvvDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2181 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmKKDKDNTQKFLVE 2260
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTE 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2261 EAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAemlqRQKDLAQEQAQKLLE 2340
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIA 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2341 DKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEiatkeqm 2420
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE------- 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2421 TEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQ 2485
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
44-149 |
2.86e-21 |
|
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: 92.45 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
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 ... |
44-149 |
4.37e-21 |
|
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: 92.07 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 44 RVQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR---EKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1139-2018 |
5.98e-21 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 102.36 E-value: 5.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1139 EAEAEQPVFDSLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYREsyd 1218
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE--- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1219 wlirwiadaKQRQENIQavpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEplt 1298
Cdd:pfam02463 237 ---------ERIDLLQE-----LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1299 spLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAE 1378
Cdd:pfam02463 300 --SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1379 AHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLELHELKNLSEQQikdksqqvDEALKSRLRIEEEIHLI 1458
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELEL-----------KSEEEKEAQLLLELARQLEDLL--------KEEKKEELEILEEEEES 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1459 RIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALED 1538
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKD 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1539 LENLRMQAEEAERQVKQAEVEKER------QIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAE 1612
Cdd:pfam02463 519 GVGGRIISAHGRLGDLGVAVENYKvaistaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1613 RLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMA- 1691
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEi 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1692 ---------ENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVR 1762
Cdd:pfam02463 679 qelqekaesELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1763 SE-MDILIQLKSRAEKETMSNTEKSKQLLEAEATKLR-DLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKL 1840
Cdd:pfam02463 757 LKkEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1841 AAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQ 1920
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1921 RRVVEEEIRILKLNFEKASSGKLDL---ELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAA 1997
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLleeADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900
....*....|....*....|.
gi 1655274923 1998 EEEAARQRKAAQEELDRLQKK 2018
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQ 1017
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
162-261 |
1.90e-20 |
|
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: 89.16 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 162 AKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 241
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1655274923 242 D-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1354-2035 |
2.70e-20 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 100.04 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1354 KLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNL--SE 1431
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAlqQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1432 QQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQksnaEDELKQLRDRADAAEKLRKLAQE-----EAEKLRKQVSE 1506
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINRARKAAPLAAHikavtQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1507 ETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQ----VAHVAAQQSAAAELRSK 1582
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtlTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1583 QMSFAENVSKLEESLKQ---EHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQ--KANEAL------RLRLQAEE 1651
Cdd:TIGR00618 395 LQSLCKELDILQREQATidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceKLEKIHlqesaqSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1652 EAHKKSLAQEEAEKQKEEADReaKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRS 1731
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLAR--LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1732 LLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIA 1811
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1812 EEAKHQRQLAEEDAARQRAEA----ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQaNQ 1887
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLtltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-ET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1888 HKLEIE---EKIVLLKKSSDAEMERQKAIVDDTLKQ-RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSK 1963
Cdd:TIGR00618 712 HIEEYDrefNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFN 791
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1964 LRAEEEAEKLRRLVLEEEMRRKEAED-------KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEK 2035
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1795-2605 |
5.74e-20 |
|
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: 98.89 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1795 TKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE 1874
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1875 AYQRKILEDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKN 1954
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1955 IAEETQQSKLRAEEEAEKLrrlvlEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAE 2034
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKE-----KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2035 KQIVAAQQAALKCNMAEQQVQSVLAQQKEDsmmqnklkeeyekakalARDAEAAKERAEREAALLRQQAEEAERQKVAAE 2114
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLED-----------------LLKEEKKEELEILEEEEESIELKQGKLTEEKEE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2115 QEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQ-TLKQKFQVEQELTKVKLQLEETDKQ 2193
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARsGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2194 KSLLDDELQRLKDEV-DDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEdA 2272
Cdd:pfam02463 533 DLGVAVENYKVAISTaVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-A 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2273 ARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEkMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEE 2352
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKE-SGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2353 TEEyqrsleaERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKmefekln 2432
Cdd:pfam02463 691 KEE-------ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR------- 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2433 tskeaddlRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKL--IEDEKKKLES 2510
Cdd:pfam02463 757 --------LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELleEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2511 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAA-LNKQKEAEKDILNKQKEmqELERKRLEQERVLADENQKLREK 2589
Cdd:pfam02463 829 KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKeELLQELLLKEEELEEQK--LKDELESKEEKEKEEKKELEEES 906
|
810
....*....|....*.
gi 1655274923 2590 LQQMEEAQKSTLITEK 2605
Cdd:pfam02463 907 QKLNLLEEKENEIEER 922
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
161-260 |
8.98e-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: 87.15 E-value: 8.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
165-262 |
1.18e-19 |
|
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: 87.02 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 243
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1655274923 244 DVPHPDEKSIITYVSSLYD 262
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1912-2599 |
1.38e-19 |
|
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: 97.82 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1912 AIVDDTLKQRRVVEEE---IRILKLNFEKASSgKLDLELE-LNKLKNIAEET--QQSKLRAE-EEAEKLRRLVLEEE--- 1981
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEaagISKYKERRKETER-KLERTREnLDRLEDILNELerQLKSLERQaEKAERYKELKAELRele 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 -----MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQs 2056
Cdd:TIGR02168 227 lallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2057 vLAQQKEDSmmqnkLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEF 2136
Cdd:TIGR02168 306 -ILRERLAN-----LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2137 EAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQK-----SLLDDELQRLKDEVDDA 2211
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqaelEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2212 MRQKASVEEELFKVKiqmEELMKLKVRIEEENQRL-----MKKDKDNTQKFLVEEAENMKKLAEDAARLS---------- 2276
Cdd:TIGR02168 460 EEALEELREELEEAE---QALDAAERELAQLQARLdslerLQENLEGFSEGVKALLKNQSGLSGILGVLSelisvdegye 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2277 --IEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQ--AIQEASRLKAeaemlqRQKDLAQEQAQKLLEDKQLMQQRLDEE 2352
Cdd:TIGR02168 537 aaIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGrvTFLPLDSIKG------TEIQGNDREILKNIEGFLGVAKDLVKF 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2353 TEEYQRSLEAERKRQL------EIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLH-ETEIATKEQmtEVKK 2425
Cdd:TIGR02168 611 DPKLRKALSYLLGGVLvvddldNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILErRREIEELEE--KIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2426 MEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEK 2505
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA-LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2506 KKLEsQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 2585
Cdd:TIGR02168 768 ERLE-EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
730
....*....|....
gi 1655274923 2586 LREKLQQMEEAQKS 2599
Cdd:TIGR02168 847 IEELSEDIESLAAE 860
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1749-2595 |
2.76e-19 |
|
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: 96.68 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1749 QERKQLEDELSKVrSEMDILIQlKSRAEKETMSNTEKSKQLLEAEATKLRDlaeeasKLRAIAEEAKHQRQLAEEdaaRQ 1828
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEELEEVEENIERLDLIIDEKRQQLE------RLRREREKAERYQALLKE---KR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1829 RAEAERILKEKLAAisDATRLKTEAEIALKEKEAEN-ERLRRQAEDEAYQRKILEDQANqhkleieEKIvllKKSSDAEM 1907
Cdd:TIGR02169 222 EYEGYELLKEKEAL--ERQKEAIERQLASLEEELEKlTEEISELEKRLEEIEQLLEELN-------KKI---KDLGEEEQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEEtqqskLRAEEEAEKLRRLVLEEEMrrKEA 1987
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE-----LEREIEEERKRRDKLTEEY--AEL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1988 EDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKE-DSM 2066
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINElEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2067 M---QNKLKEEYEKAKALARDAEAAKERAEREAALLRqQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQ 2143
Cdd:TIGR02169 443 KedkALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD-RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2144 AEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKV--------------------KLQLEETDKQKSLLDDELQR 2203
Cdd:TIGR02169 522 GVHGTVAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflplnKMRDERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2204 LKDEVdDAMRQKASVEEELFKVKIQMEELmklkvrieEENQRLMKKDKDNT-QKFLVEEAENM-------KKLAEDAARL 2275
Cdd:TIGR02169 602 AVDLV-EFDPKYEPAFKYVFGDTLVVEDI--------EAARRLMGKYRMVTlEGELFEKSGAMtggsrapRGGILFSRSE 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2276 SIEAQE-AARLR--QIAEDDLNQQRTLAEKMLKEKMQAIQEASR----LKAEAEMLQRQkdlaQEQAQKLLEDKQLMQQR 2348
Cdd:TIGR02169 673 PAELQRlRERLEglKRELSSLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQE----EEKLKERLEELEEDLSS 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2349 LDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaqakaeeeakkfkkqadtiaARLHETEIATKEQmtEVKKMEF 2428
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---------------------ARLSHSRIPEIQA--ELSKLEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2429 EKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLqQTFLTEKEMLLKK----EKLIEDE 2504
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-LKEQIKSIEKEIENL-NGKKEELEEELEEleaaLRDLESR 883
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2505 KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKaTMDAALNKQKEAEKDILNKQKEMQElERKRLEQERVLADENQ 2584
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS-ELKAKLEALEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQ 961
|
890
....*....|.
gi 1655274923 2585 KLREKLQQMEE 2595
Cdd:TIGR02169 962 RVEEEIRALEP 972
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
161-259 |
3.38e-19 |
|
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: 85.37 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYqgiRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVY-RQTNLENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1655274923 240 PEDVDVPHPDEKSIITYVSS 259
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1504-2380 |
4.31e-19 |
|
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: 96.19 E-value: 4.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1504 VSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAER---QVKQAEVEKERQIQVAHVAAQQSAAAELR 1580
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1581 SKQMSFAE-NVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALR-LRLQAEEEAHKKSL 1658
Cdd:pfam02463 244 ELLRDEQEeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRkVDDEEKLKESEKEK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1659 AQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQEliRLRADFDNAEQQRSLLEDELY 1738
Cdd:pfam02463 324 KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELKS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1739 RLKNEVIAAQQERKQLEDELSKVR-SEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQ 1817
Cdd:pfam02463 402 EEEKEAQLLLELARQLEDLLKEEKkEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1818 RQLAEEDAARQRAEAERilkeklaaisdatrlkteaEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIV 1897
Cdd:pfam02463 482 LQEQLELLLSRQKLEER-------------------SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1898 LLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLV 1977
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1978 LEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSV 2057
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIK 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2058 LAQQKEDSMMQNKLKEEYEKakaLARDAEAAKERAEREAALLRQQAEEAErqkvaaeqeaanqakaQDDAERLRKDAEFE 2137
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEEL---LADRVQEAQDKINEELKLLKQKIDEEE----------------EEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2138 AAKLAQAEAAALKQKQQADEEmaKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddamrqkas 2217
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK---------- 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2218 vEEELFKVKIQMEELMKLKVRIEEENQRLMK-------KDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAE 2290
Cdd:pfam02463 832 -EEELEELALELKEEQKLEKLAEEELERLEEeitkeelLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2291 DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEET-------EEYQRSLEAE 2363
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGkvnlmaiEEFEEKEERY 990
|
890
....*....|....*...
gi 1655274923 2364 RKRQLEII-AEAEKLKLQ 2380
Cdd:pfam02463 991 NKDELEKErLEEEKKKLI 1008
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
46-146 |
1.28e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.79 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGR--MRFHKLQNVQIALDFLRHRQVKLVN 121
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1655274923 122 IRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1320-2257 |
1.36e-18 |
|
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: 94.73 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1320 LRTRYSELMTLTS-----QYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL 1394
Cdd:TIGR00606 171 LKQKFDEIFSATRyikalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1395 KLRmQEEVSKRETAAVDAEKqkqniqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSnaed 1474
Cdd:TIGR00606 251 KNR-LKEIEHNLSKIMKLDN-------EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 elkqlRDRADAAEKLRK-------LAQEEAEKLRKQVSEETQKKRLAEEELKHKSEaerKAANEKQKALEDLEnlrmQAE 1547
Cdd:TIGR00606 319 -----RELVDCQRELEKlnkerrlLNQEKTELLVEQGRLQLQADRHQEHIRARDSL---IQSLATRLELDGFE----RGP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1548 EAERQVKQA-EVEKERQIQVAHVAAQQsaAAELRSKQMSFAENVSKLEESLKQEHGTvlqLQQDAERLRKQQEDAENARE 1626
Cdd:TIGR00606 387 FSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKKGLGRT---IELKKEILEKKQEELKFVIK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1627 EAERELE------KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDmaenelERQRR 1700
Cdd:TIGR00606 462 ELQQLEGssdrilELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH------TTTRT 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1701 LAESTAQQKLAAEQ-----------ELIRLRADFDNAEQqrslLEDELYRLKNEViaaqqerKQLEDELSKVRSEMDILI 1769
Cdd:TIGR00606 536 QMEMLTKDKMDKDEqirkiksrhsdELTSLLGYFPNKKQ----LEDWLHSKSKEI-------NQTRDRLAKLNKELASLE 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 QLKSRAEKETMSNTEKSKQLLEA--EATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDAT 1847
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQ 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1848 R-LKTEAEIALKEKEAENERLRRQAEDEAYQRKIledqanqHKLEIEEKIVLLKKSSDA-EMERQKAIVDDTLKQRRVVE 1925
Cdd:TIGR00606 685 RvFQTEAELQEFISDLQSKLRLAPDKLKSTESEL-------KKKEKRRDEMLGLAPGRQsIIDLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1926 EEIRILKLNFEKASS--GKLDLELELNK--------LKNIAEETQQSKLRAEEEAEKLR-----RLVLEEEMRRKEAEDK 1990
Cdd:TIGR00606 758 RDIQRLKNDIEEQETllGTIMPEEESAKvcltdvtiMERFQMELKDVERKIAQQAAKLQgsdldRTVQQVNQEKQEKQHE 837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1991 VKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNK 2070
Cdd:TIGR00606 838 LDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2071 LKEEYEKAKALARDAEAAKERAEREAALLRqqaeeaERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALK 2150
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNKKAQDKVNDIK------EKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEK 991
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2151 QKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKiqME 2230
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK--RN 1069
|
970 980
....*....|....*....|....*..
gi 1655274923 2231 ELMKLKVRIEEENQRLMKKDKDNTQKF 2257
Cdd:TIGR00606 1070 HVLALGRQKGYEKEIKHFKKELREPQF 1096
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
164-260 |
1.80e-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: 83.52 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 164 EKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN----LENLEQAFNVAEKDLGVTRLLD 239
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1655274923 240 PEDVDVPHPDEKSIITYVSSL 260
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1333-2111 |
1.81e-18 |
|
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: 94.03 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1333 QYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKaIAKAEKEAQElklrmqeevskretaavDA 1412
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAD-IRRRESQSQE-----------------DL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1413 EKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIE---EEIHLIRIQLETTVKQKSNAEDELKQL--RDRADAAE 1487
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1488 KLRKLAQEEAEKLRKQVSEetqkkrlAEEELKH-KSEAERKaanekqkaLEDLenLRMQAEEAERQVKQAEVEkerqiqv 1566
Cdd:pfam15921 224 KILRELDTEISYLKGRIFP-------VEDQLEAlKSESQNK--------IELL--LQQHQDRIEQLISEHEVE------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1567 ahVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeaerelekwrqkaneaLRLR 1646
Cdd:pfam15921 280 --ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ-------------------------LRSE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1647 LqaeeeahkkslaqeeaekqkeeadREAKK--RSKAEESAlKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFD 1724
Cdd:pfam15921 333 L------------------------REAKRmyEDKIEELE-KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1725 NAEQQRSLLEDELYRL----KNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE---KETMSNTEKSKQLLEAEATKL 1797
Cdd:pfam15921 388 KREKELSLEKEQNKRLwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQgqmERQMAAIQGKNESLEKVSSLT 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1798 RDLAEEASKLRAIAEEAKhQRQLAEEDAARQRAEAERILKEKLAAI----SDATRLKTEAEIALKEKE---AENERLRR- 1869
Cdd:pfam15921 468 AQLESTKEMLRKVVEELT-AKKMTLESSERTVSDLTASLQEKERAIeatnAEITKLRSRVDLKLQELQhlkNEGDHLRNv 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1870 QAEDEAYQRKILED----QANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILK----LNFEKASSG 1941
Cdd:pfam15921 547 QTECEALKLQMAEKdkviEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKdkkdAKIRELEAR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1942 KLDLELELNKLKNIAEEtqqsKLRAEEEAEKLRRLVLEE---------------EMRRKEAEDKVKKIAAAEEEAARQRK 2006
Cdd:pfam15921 627 VSDLELEKVKLVNAGSE----RLRAVKDIKQERDQLLNEvktsrnelnslsedyEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2007 AAQEELDRLQKKAdevrKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNK----LKEEYEKAKALA 2082
Cdd:pfam15921 703 SAQSELEQTRNTL----KSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKekhfLKEEKNKLSQEL 778
|
810 820
....*....|....*....|....*....
gi 1655274923 2083 RDAEAAKERAEREAALLRQQaEEAERQKV 2111
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQ-ERRLKEKV 806
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1227-2037 |
1.89e-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: 93.98 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1227 AKQRQENIQAVPITDSKTLKEQLAKEKklLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAqvepltspLKKTKL 1306
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEE--LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1307 DSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEK---AAEKLKAEEQKKMAEMQAE--LDKQKQLAEAHA 1381
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKrleEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1382 KaIAKAEKEAQELKLRMQeevskretaavDAEKQKQNIQLELHELK----NLSEQ--QIKDKSQQVDEALKSRlriEEEI 1455
Cdd:TIGR02169 302 E-IASLERSIAEKERELE-----------DAEERLAKLEAEIDKLLaeieELEREieEERKRRDKLTEEYAEL---KEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1456 HLIRIQLETTVKQKSNAEDELKQLRDRADAA-------EKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKhKSEAERKA 1528
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLkreinelKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-ELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1529 ANEKQKALE-DLENLRMQAEEAERQV-----KQAEVEKER---QIQVAHVAAQQSAAaelRSKQMSFAENVSKLEESLKQ 1599
Cdd:TIGR02169 446 KALEIKKQEwKLEQLAADLSKYEQELydlkeEYDRVEKELsklQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1600 EHGTVLQLQQDAERL----------RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEE 1669
Cdd:TIGR02169 523 VHGTVAQLGSVGERYataievaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFA 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1670 AD--REAKKRSKAEESALKQRDMAENeLERQRRL--------------------------AESTAQQKLAAEQELIRLRA 1721
Cdd:TIGR02169 603 VDlvEFDPKYEPAFKYVFGDTLVVED-IEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1722 DFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE---KETMSNTEKSKQLLEAEATKLR 1798
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKerlEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1799 DLAEEASKLraiaEEAKHQRQLAEEDAARQRAEAE--------RILKEKLAAISDATRlktEAEIALKEKEAENERLRRQ 1870
Cdd:TIGR02169 762 ELEARIEEL----EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1871 AEDEAYQRKILEDQANQHKLEIEEkIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELN 1950
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQSKLRAEEEAE----------------------KLRRLVLEEEMRRKE-----AEDKVKKIAAAEEEAAR 2003
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSeiedpkgedeeipeeelsledvQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELKE 993
|
890 900 910
....*....|....*....|....*....|....
gi 1655274923 2004 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKQI 2037
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
161-260 |
2.10e-18 |
|
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: 83.36 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSL 260
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1515-2599 |
4.36e-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: 92.93 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1515 EEELKHKSEaerkaanEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE-----LRSKQMSFAEN 1589
Cdd:pfam01576 4 EEEMQAKEE-------ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEemrarLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1590 VSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAReeaerelekwrqKANEALRLRLQAEeeahKKSLaqeeaekqkee 1669
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQL------------DEEEAARQKLQLE----KVTT----------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1670 adrEAKKRsKAEESALKQRDmAENELERQRRLAE---STAQQKLAAEQELIRLRADFDNaeQQRSLLEDELYRLKNEVIA 1746
Cdd:pfam01576 130 ---EAKIK-KLEEDILLLED-QNSKLSKERKLLEeriSEFTSNLAEEEEKAKSLSKLKN--KHEAMISDLEERLKKEEKG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1747 AQQERK---QLEDELSKVRSEMdilIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKH----QRQ 1819
Cdd:pfam01576 203 RQELEKakrKLEGESTDLQEQI---AELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQiselQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1820 LAEEDAARQRAEAE-RILKEKLAAisdatrLKTEAEIALKEKEAENErLRRQAEDEAYQ-RKILEDQANQHKLEIEEkiv 1897
Cdd:pfam01576 280 LESERAARNKAEKQrRDLGEELEA------LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQLQE--- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1898 LLKKSSDAEMERQKAIvddtlkqrrvveEEIRILKLNFEKAssgKLDLELELNKLKNIAEETQQSKLraeeeaeklrrlv 1977
Cdd:pfam01576 350 MRQKHTQALEELTEQL------------EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQ------------- 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1978 lEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSV 2057
Cdd:pfam01576 402 -DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2058 LAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQkvaAEQEAANQAKAQDDAERLRKDAEfe 2137
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTLEALEEGKKRLQRELE-- 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2138 aaklaqaeaaalKQKQQADEEMAKHKKLAeqtlKQKFQVEQELTKVKLQLeetDKQKSLLD--DELQRLKDEV---DDAM 2212
Cdd:pfam01576 556 ------------ALTQQLEEKAAAYDKLE----KTKNRLQQELDDLLVDL---DHQRQLVSnlEKKQKKFDQMlaeEKAI 616
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2213 RQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARlsiEAQEAARLRQIAEDD 2292
Cdd:pfam01576 617 SARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGK---NVHELERSKRALEQQ 693
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2293 LNQQRTLAEKmLKEKMQAIQEAsRLKAEAEM----LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEeyqrsLEAERKRQL 2368
Cdd:pfam01576 694 VEEMKTQLEE-LEDELQATEDA-KLRLEVNMqalkAQFERDLQARDEQGEEKRRQLVKQVRELEAE-----LEDERKQRA 766
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2369 EIIAEAEKLKLQVSQLSeaqakaeeeakkfkkqadtiaARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITEL- 2447
Cdd:pfam01576 767 QAVAAKKKLELDLKELE---------------------AQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIl 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2448 ----EKEKARLKKEAEEHQ-NKSKEMADAQQKQIEREMTVLQQTF---LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKA 2519
Cdd:pfam01576 826 aqskESEKKLKNLEAELLQlQEDLAASERARRQAQQERDELADEIasgASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2520 KALKDEQDRQRQQMEEeklklkatmdaaLNKQKEAEKDILnkqkemQELERKRLEQERvladENQKLREKLQQMEEAQKS 2599
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQ------------LTTELAAERSTS------QKSESARQQLER----QNKELKAKLQEMEGTVKS 963
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1714-2588 |
6.63e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.05 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1714 QELIRLRADFDNAEQQRSLL----EDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETmsntEKSKQL 1789
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLkekrEYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRL----EEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1790 LEAEATKLRDLAEEasklraiaEEAKHQRQLAEEDAarQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 1869
Cdd:TIGR02169 274 LEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1870 QAEDEAYQRKILEDQANQHKLEIEEKIVLLkkssdAEMERQKAIVDDTLKQRRvveEEIrilklnfEKASSGKLDLELEL 1949
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAEL-----EEVDKEFAETRDELKDYR---EKL-------EKLKREINELKREL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1950 NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK----- 2024
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKelskl 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIVAAQQAALKCN--MAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKALARDAEAAKERAEREAalLRQQ 2102
Cdd:TIGR02169 489 QRELAEAEAQARASEERVRGGRAVeeVLKASIQGVHGTVAQ----LGSVGERYATAIEVAAGNRLNNVVVEDDA--VAKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2103 AEEAERQKVAAEQEAANQAKAQD---DAERLRKDA---------EFEAAKLAQAEAAALKQKQQADEEMAKHkklaeqtL 2170
Cdd:TIGR02169 563 AIELLKRRKAGRATFLPLNKMRDerrDLSILSEDGvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAARR-------L 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2171 KQKFQVeqeltkVKLQLEETDKQKSLLDDELqRLKDEVDDAMRQKASVE---EELFKVKIQMEELMKLKVRIEEENQRLM 2247
Cdd:TIGR02169 636 MGKYRM------VTLEGELFEKSGAMTGGSR-APRGGILFSRSEPAELQrlrERLEGLKRELSSLQSELRRIENRLDELS 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2248 KKDKDNTQKflVEEAENmkklaedaaRLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKmqaiQEASRLkaEAEMLQRQ 2327
Cdd:TIGR02169 709 QELSDASRK--IGEIEK---------EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK----SELKEL--EARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2328 KDLAQEQAQKLLEDKQLMQQRLDEETEEYqRSLEAERKRQLEIIAEAE----KLKLQVSQLSEAQAKAEEEAKKFKKQAD 2403
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSRIPEIQAEL-SKLEEEVSRIEARLREIEqklnRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2404 TIAARLHETEIATKEQMTEVKKMEfeklntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmadaQQKQIEREMTVL 2483
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELE-------AALRDLESRLGDLKKERDELEAQLRELERKIEE----LEAQIEKKRKRL 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2484 QQTfLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKdeqdrQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQK 2563
Cdd:TIGR02169 920 SEL-KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-----ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
890 900
....*....|....*....|....*
gi 1655274923 2564 EMQELERKRLEQERVLADENQKLRE 2588
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1349-2095 |
7.22e-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: 92.05 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1349 EKAAEKLKAEEQKkMAEMQAELDKQKQLAEAHAKAIAKAEKeAQELKLRMQE-EVSKRETAAVDAEKQKQNIQLELHELk 1427
Cdd:TIGR02169 173 EKALEELEEVEEN-IERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREyEGYELLKEKEALERQKEAIERQLASL- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1428 nlsEQQIKDKSQQVDEalksrlrIEEEIHLIRIQLEttvkqksnaedelkqlrdraDAAEKLRKLAQEEAEKLRKQVSEE 1507
Cdd:TIGR02169 250 ---EEELEKLTEEISE-------LEKRLEEIEQLLE--------------------ELNKKIKDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1508 TQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQ------------AEVEKERQIQVAHVAAQQSA 1575
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeyAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1576 AAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWrQKANEALRLRLQAEEEaHK 1655
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL-EEEKEDKALEIKKQEW-KL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1656 KSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAEneLERQRRLAESTAQQKLAAEQELirlRADFDNAEQQRSLL-- 1733
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--AEAQARASEERVRGGRAVEEVL---KASIQGVHGTVAQLgs 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1734 EDELY----------RLKNEVIA----AQQERKQLEDE---------LSKVRSE------------MDILIQLKSRAEKE 1778
Cdd:TIGR02169 533 VGERYataievaagnRLNNVVVEddavAKEAIELLKRRkagratflpLNKMRDErrdlsilsedgvIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1779 ------------TMSNTEKSKQLL------------------------EAEATKLRDLAEEASKLRAIAEEAKHQRQLae 1822
Cdd:TIGR02169 613 epafkyvfgdtlVVEDIEAARRLMgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKREL-- 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1823 EDAARQRAEAERILKEKLAAISDATR----LKTEAEIALKEKEAENERLRRQAED-EAYQRKILEDQANQHKLEIEEkiv 1897
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKSELKELEARI--- 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1898 llkkssdAEMERQKAIVDDTLK--QRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRR 1975
Cdd:TIGR02169 768 -------EELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1976 LVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQ-------EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAalKCN 2048
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKK--RKR 918
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1655274923 2049 MAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL-ARDAEAAKERAERE 2095
Cdd:TIGR02169 919 LSELKAKLEALEEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEEE 966
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
161-261 |
1.10e-17 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 81.58 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
|
90 100
....*....|....*....|..
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21259 81 EDmVRMREPDWKCVYTYIQEFY 102
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
47-144 |
1.20e-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: 81.23 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 47 KKTFTKWVNKHL-IKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPRE--KGRMRFHKLQNVQIALDFLRHRQV-KLVNI 122
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1655274923 123 RNDDI-ADGNPKLTLGLIWTIIL 144
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
157-262 |
1.81e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 80.76 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 157 SEDMSAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTR 236
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1655274923 237 LLDPEDV-DVPHPDEKSIITYVSSLYD 262
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
161-262 |
2.19e-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: 80.39 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21261 1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
|
90 100
....*....|....*....|....
gi 1655274923 241 EDVDV--PHPDEKSIITYVSSLYD 262
Cdd:cd21261 81 EDMMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
161-266 |
5.10e-17 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 79.71 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21258 1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
|
90 100
....*....|....*....|....*...
gi 1655274923 241 EDVDV--PHPDEKSIITYVSSLYDAMPR 266
Cdd:cd21258 81 EDMMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1810-2545 |
7.49e-17 |
|
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: 88.64 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1810 IAEEAKHQRQlaeeDAARQRAEAERIL-KEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQAnqH 1888
Cdd:pfam15921 79 VLEEYSHQVK----DLQRRLNESNELHeKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV--H 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1889 KLEIEEKIVL-LKKSSDAEMERQKAIvddtLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAE 1967
Cdd:pfam15921 153 ELEAAKCLKEdMLEDSNTQIEQLRKM----MLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1968 EEAE----KLRRLVLEEEMR--RKEAEDKVKKIAAAEEEAARQRKAAQE-ELDRLQKKADEVRKQKEEADKEAE--KQIV 2038
Cdd:pfam15921 229 LDTEisylKGRIFPVEDQLEalKSESQNKIELLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEiiQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2039 AAQQAALKCNMA--EQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARD--AEAAKER----------------------- 2091
Cdd:pfam15921 309 RNQNSMYMRQLSdlESTVSQLRSELREAKRMYEDKIEELEKQLVLANSelTEARTERdqfsqesgnlddqlqklladlhk 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2092 AEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDA-------ERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKK 2164
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRnmevqrlEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2165 LAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqKASVEEELFKVKIQMEELMKLK-------- 2236
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT---NAEITKLRSRVDLKLQELQHLKnegdhlrn 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2237 VRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQ-EAARLrqiaEDDLNQQR-TLAE-KMLKEKMQA--- 2310
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQvEKAQL----EKEINDRRlELQEfKILKDKKDAkir 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2311 ----------IQEASRLKAEAEMLQRQKDLAQEQAQkLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 2380
Cdd:pfam15921 622 elearvsdleLEKVKLVNAGSERLRAVKDIKQERDQ-LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2381 vsqlseaqakaeeeakkfkkqadtiaarLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAIT------ELEKEKARL 2454
Cdd:pfam15921 701 ----------------------------LKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITakrgqiDALQSKIQF 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2455 KKEAEEHQNKSKEMADAQQKQIEREMTvlqqTFLTEKEMLLKKEKLIEDEKKKLE---SQFEEEIKKAKALKDE-QDR-Q 2529
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELS----TVATEKNKMAGELEVLRSQERRLKekvANMEVALDKASLQFAEcQDIiQ 828
|
810
....*....|....*.
gi 1655274923 2530 RQQMEEEKLKLKATMD 2545
Cdd:pfam15921 829 RQEQESVRLKLQHTLD 844
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1536-2288 |
1.47e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 87.72 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1536 LEDLENLRMQAEEAERQVKQAEVEKE---RQIQVAHVAAQQSAAAELRSKQMSFAEnVSKLEESLKQEHGTVLQLQQDAE 1612
Cdd:TIGR00618 172 LFPLDQYTQLALMEFAKKKSLHGKAElltLRSQLLTLCTPCMPDTYHERKQVLEKE-LKHLREALQQTQQSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1613 RL-----RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEA-HKKSLAQEEAEKQKEEADREAKKRSKAEESALK 1686
Cdd:TIGR00618 251 AQeeqlkKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1687 QRDMA-ENELERQRRLaestaQQKLAAEQELIRlradfDNAEQQRSLLE--DELYRLKNEVIAAQQERKQLEDELSKVRS 1763
Cdd:TIGR00618 331 AAHVKqQSSIEEQRRL-----LQTLHSQEIHIR-----DAHEVATSIREisCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1764 EMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAkhQRQLAEEDAARQRAEAERILKEKLAAI 1843
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA--QCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1844 SDATRLKTE---AEIALKEKEAENERL--RRQAEDEAYQRKILEDQANQHKLE-IEEKIVLLKKssdaEMERQKAIVDDT 1917
Cdd:TIGR00618 479 EQIHLQETRkkaVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLET----SEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1918 LKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsKLRAEEEAEKLRRLVLEEEMRRKeaedkvkkiaaa 1997
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD-LTEKLSEAEDMLACEQHALLRKL------------ 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1998 eeeaarqrkaaQEELDRLQKKADEVRKQKEEADKEAEKqivaaqqAALKCNMAEQQVQSVLA---QQKEDSMMQNKLKEE 2074
Cdd:TIGR00618 622 -----------QPEQDLQDVRLHLQQCSQELALKLTAL-------HALQLTLTQERVREHALsirVLPKELLASRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2075 YEKAKAlaRDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQ 2154
Cdd:TIGR00618 684 KMQSEK--EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2155 ADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDEL-QRLKDEVDDAMRQKASVEEELFKVKIQMEELM 2233
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2234 KLKVRIEeenqRLMKKDKDNTQKFlveeaenmKKLAEDAARLSIEAQEAARLRQI 2288
Cdd:TIGR00618 842 ATLGEIT----HQLLKYEECSKQL--------AQLTQEQAKIIQLSDKLNGINQI 884
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
163-264 |
2.91e-16 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 77.82 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPED 242
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1655274923 243 -VDVPHPDEKSIITYVSSLYDAM 264
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1122-1746 |
3.23e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1122 DVKEVETYRTNLKKMRAEAEAeqpvfdsLEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQR 1201
Cdd:COG1196 223 KELEAELLLLKLRELEAELEE-------LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1202 ELDQLGRQLGYYRESydwlirwIADAKQRQENIQAvpitdskTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIK 1281
Cdd:COG1196 296 ELARLEQDIARLEER-------RRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1282 DYELQLVAYKAQVEpltsplkktKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQK 1361
Cdd:COG1196 362 EAEEALLEAEAELA---------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1362 KMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQV 1441
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1442 DEALKSRLRIEEEIHLIRI---QLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEEL 1518
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1519 KHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRskqmSFAENVSKLEESLK 1598
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE----GGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1599 QEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRS 1678
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1679 KAEESALKQRDMAENELERQRRLAESTAQQK----LAAEQELIRLRADFDNAEQQRSLLEDELYRLKnEVIA 1746
Cdd:COG1196 749 EEEALEELPEPPDLEELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQREDLEEARETLE-EAIE 819
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
165-262 |
1.28e-15 |
|
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: 75.69 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 165 KLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLD-PEDV 243
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1655274923 244 DVPHPDEKSIITYVSSLYD 262
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4021-4059 |
2.88e-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: 2.88e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 4021 LLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEMNEIL 4059
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
161-261 |
4.68e-15 |
|
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: 73.93 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEkDLGVTRLLDP 240
Cdd:cd21199 8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTI 86
|
90 100
....*....|....*....|..
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21199 87 DEmVSMERPDWQSVMSYVTAIY 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1960-2605 |
5.61e-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: 82.71 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1960 QQSKLRAEEEAEKLRRLVLEEE-----MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQ-----KKADEVRKQKEEA 2029
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEaagsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqaKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2030 DKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERA---------EREAALLR 2100
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeeelkllAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2101 QQAEEAERQKVAAEQEA----ANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKL--AEQTLKQKF 2174
Cdd:pfam02463 300 SELLKLERRKVDDEEKLkeseKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLeqLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2175 QVEQE--------LTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVK-IQMEELMKLKVRIEEENQR 2245
Cdd:pfam02463 380 KLESErlssaaklKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIeLKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2246 LMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQ 2325
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2326 RQK----DLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQ 2401
Cdd:pfam02463 540 NYKvaisTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2402 ADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDL---RKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIER 2478
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLaekSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2479 EMTVLQQTFLTEKEMLLKKEKLIEDEKKKLES-QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKD 2557
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRVQEAQdKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2558 ILNKQKEMQE--LERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 2605
Cdd:pfam02463 780 REKTEKLKVEeeKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK 829
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1115-1883 |
6.55e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 82.41 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1115 EVHTVPNDVKEVETYRTNLKKMRAEAEAEqpvFDSLEEELKKASAVSDKMSrvhserdAELDQHRQHLSSLQDRWKAVFT 1194
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEE---LAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1195 QIDLRQRELDQLGRQlgyyresydwlirwIADAKQRQENIqavpitdsKTLKEQLAKEK-KLLEEIEKNKDKVDECQKya 1273
Cdd:TIGR02168 380 QLETLRSKVAQLELQ--------------IASLNNEIERL--------EARLERLEDRReRLQQEIEELLKKLEEAEL-- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1274 kayidiiKDYELQLVAYKAQVEPLTSPL--KKTKLDSASDNIIQEYVTLRTRYSELMTLTSQyIKFITDTQRRLEDEEKA 1351
Cdd:TIGR02168 436 -------KELQAELEELEEELEELQEELerLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSEG 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1352 AEKLKAeEQKKMAEMQAELDKQKQLAEAHAKAIAKAekeaqeLKLRMQEEVSKRETAAVDA-EKQKQNiqlELHELKNLS 1430
Cdd:TIGR02168 508 VKALLK-NQSGLSGILGVLSELISVDEGYEAAIEAA------LGGRLQAVVVENLNAAKKAiAFLKQN---ELGRVTFLP 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1431 EQQIKDKSQQVDEAlkSRLRIEEEIHLIRIQLETTVKQKSNA-EDELKQLR---DRADAAEKLRKLAQEEA------EKL 1500
Cdd:TIGR02168 578 LDSIKGTEIQGNDR--EILKNIEGFLGVAKDLVKFDPKLRKAlSYLLGGVLvvdDLDNALELAKKLRPGYRivtldgDLV 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1501 RKQ-----VSEETQKKRLAE----EELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIqvahvAA 1571
Cdd:TIGR02168 656 RPGgvitgGSAKTNSSILERrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI-----SA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1572 QQSAAAELRSKqmsfaenVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRlRLQAEE 1651
Cdd:TIGR02168 731 LRKDLARLEAE-------VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALR 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1652 EAHKKSlaqeeaekqkeeadREAKKRSKAEESALKQR-DMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQR 1730
Cdd:TIGR02168 803 EALDEL--------------RAELTLLNEEAANLRERlESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1731 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRA- 1809
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEe 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1810 ---IAEEAKHQRQLAEEDAARQRAEAERiLKEKLAAISDATRLkteaeiALKEKEAENER---LRRQAEDEAYQRKILED 1883
Cdd:TIGR02168 949 yslTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERydfLTAQKEDLTEAKETLEE 1021
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2060-2376 |
7.20e-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: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2060 QQKEDSMMQNKLKEEYE-KAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDA----ERLRKDA 2134
Cdd:pfam17380 290 QEKFEKMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERkrelERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2135 EFEAAKLAQAEAAALKQKQQADEEMakhKKLAEQTLKQKFQVEQELTKVKLQLEETDK----QKSLLDDELQRLKDEVDd 2210
Cdd:pfam17380 370 IAMEISRMRELERLQMERQQKNERV---RQELEAARKVKILEEERQRKIQQQKVEMEQiraeQEEARQREVRRLEEERA- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2211 amRQKASVEEELFKVKIQMEELmklkvRIEEENQRLMKKDKDNTQKflveeaenMKKLAEDAARLSIEAQEAARLRQIAE 2290
Cdd:pfam17380 446 --REMERVRLEEQERQQQVERL-----RQQEEERKRKKLELEKEKR--------DRKRAEEQRRKILEKELEERKQAMIE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2291 DDlnQQRTLAEKMLKEKMQAI-QEASRLKAEAEmlqrqkdlaqEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQ-L 2368
Cdd:pfam17380 511 EE--RKRKLLEKEMEERQKAIyEEERRREAEEE----------RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREmM 578
|
....*...
gi 1655274923 2369 EIIAEAEK 2376
Cdd:pfam17380 579 RQIVESEK 586
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
46-146 |
1.08e-14 |
|
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: 72.72 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVNKHLIK--SQRHVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMRfhklQNVQIALDFLRHRQV 117
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1655274923 118 KLVNIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
43-142 |
1.17e-14 |
|
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: 72.95 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 43 DRVQKKTFTKWVNKHLIKSQ-RHVTDLYEDLRDGHNLISLLEVLSGDTLPRE---KGRMRFHKLQNVQIALDFLRHR-QV 117
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 1655274923 118 KLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1225-1618 |
1.27e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.73 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1225 ADAKQRQENIQ--AVPITDSKTLKEQLAKEKKLLEEIEKN---KDKVDECQKYAKayiDIIKDYELQlvaYKAQVEPLTS 1299
Cdd:PTZ00121 1374 EEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAaaaKKKADEAKKKAE---EKKKADEAK---KKAEEAKKAD 1447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1300 PLKKTKLDSASDNIIQEYVTLRTRYSELmtltsqyiKFITDTQRRLEDEEKAAE--KLKAEEQKKMAEMQAELDKQKQLA 1377
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEA--------KKKAEEAKKADEAKKKAEeaKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1378 EAH-AKAIAKAEKEAQELKLRMQEEVSKRETAAvDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKS-RLRIEEEI 1455
Cdd:PTZ00121 1520 EAKkADEAKKAEEAKKADEAKKAEEKKKADELK-KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeEARIEEVM 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1456 HLIRIQLETTVKQKSNAEDE---LKQLRDRADAAEKLRKLAQEEAEKLRK--QVSEETQKKRLAEEELKHKSEAERKAAN 1530
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1531 EKQKALEDlenlrmqAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSfaENVSKLEESLKQEHgtvlQLQQD 1610
Cdd:PTZ00121 1679 EAKKAEED-------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAE----EDKKK 1745
|
....*...
gi 1655274923 1611 AERLRKQQ 1618
Cdd:PTZ00121 1746 AEEAKKDE 1753
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1924-2526 |
2.64e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1924 VEEEIRILKLNFEKASSGKLDLElelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdKVKKIAAAEEEAAR 2003
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2004 QRKAAQEELDRLQKKADEVRKQKEEADKEAEKqivaaqqaaLKCNMAEqqvqsvLAQQKEDSMMQNKLKEEYEKAKALAR 2083
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEE---------LEEKVKE------LKELKEKAEEYIKLSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2084 DAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHK 2163
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2164 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEE-----LFKVKIQMEELMKLKVR 2238
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2239 IEEENQRLmKKDKDNTQKFLVEEAE--NMKKLAEDaarlsIEAQEAaRLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASR 2316
Cdd:PRK03918 471 IEEKERKL-RKELRELEKVLKKESEliKLKELAEQ-----LKELEE-KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2317 LKAEAEMLQ---RQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqAKAEE 2393
Cdd:PRK03918 544 LKKELEKLEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKEL----EREEK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2394 EAKKFKKQADTIAARLHETEIATKEQMTEVKkmEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmadaqq 2473
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREE------ 691
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2474 kqIEREMTVLQQtfltEKEMLLKKEKLIEDEKKKLE--SQFEEEIKKAKALKDEQ 2526
Cdd:PRK03918 692 --IKKTLEKLKE----ELEEREKAKKELEKLEKALErvEELREKVKKYKALLKER 740
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1692-2576 |
3.63e-14 |
|
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: 80.09 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1692 ENELERQRRLAESTaqqklaaEQELIRLRADFDNAEQQRSlledELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQL 1771
Cdd:TIGR00606 230 EAQLESSREIVKSY-------ENELDPLKNRLKEIEHNLS----KIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1772 KSRAEKETMSNTEKSKQLLEAEatkLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKT 1851
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERE---LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLAT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1852 EAEIALKEKEAENER--------LRRQAEDEAyqrkileDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRV 1923
Cdd:TIGR00606 376 RLELDGFERGPFSERqiknfhtlVIERQEDEA-------KTAAQLCADLQSKERLKQEQAD-EIRDEKKGLGRTIELKKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1924 VeeeirilklnfekassgkldLELELNKLKNIAEETQQSklraeeEAEKLRRLVLEEEMRRKEAE-DKVKKIAAAEEEAA 2002
Cdd:TIGR00606 448 I--------------------LEKKQEELKFVIKELQQL------EGSSDRILELDQELRKAERElSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEVRKQKE-EADKEAEKQIvaaQQAALKCNMAEQQVQSVLAQQKEDSMMQ------------- 2068
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQlNHHTTTRTQM---EMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledw 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2069 -NKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQD---DAERLRKDAEFEAAKLAQA 2144
Cdd:TIGR00606 579 lHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDeesDLERLKEEIEKSSKQRAML 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2145 EAAALKQKQQADEEMAKHKKLAEqTLKQKFQVEQELTKVKLQLEET-----DKQKSLlDDELQRLKDEVDDAMRQKASVE 2219
Cdd:TIGR00606 659 AGATAVYSQFITQLTDENQSCCP-VCQRVFQTEAELQEFISDLQSKlrlapDKLKST-ESELKKKEKRRDEMLGLAPGRQ 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2220 EELFKVKIQMEELMKLKVRIEEENQRLmkKDKDNTQKFLVEEAENMKKLAEDA-------ARLSIEAQEAAR--LRQIAE 2290
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRL--KNDIEEQETLLGTIMPEEESAKVCltdvtimERFQMELKDVERkiAQQAAK 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2291 DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLledkqlmQQRLDE-ETEEYQRSLEAERKRQLE 2369
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL-------KSKTNElKSEKLQIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2370 iiaeaEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEK 2449
Cdd:TIGR00606 888 -----EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2450 E----KARLKKEAEEHQNK---SKEMADAQQKQIEREMTVLQQTFLTEK--EMLLKKE---KLIEDEKKKLE---SQFEE 2514
Cdd:TIGR00606 963 KiqdgKDDYLKQKETELNTvnaQLEECEKHQEKINEDMRLMRQDIDTQKiqERWLQDNltlRKRENELKEVEeelKQHLK 1042
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2515 EIKKAKALkdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQE 2576
Cdd:TIGR00606 1043 EMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEK 1102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3375-3413 |
5.81e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.51 E-value: 5.81e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3375 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPELHEKL 3413
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1397-2590 |
5.95e-14 |
|
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: 79.06 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1397 RMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQqVDEALKSRLRIEEEIHLIRIQLETtvkQKSNAEDEL 1476
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNA-LQEQLQAETELCAEAEEMRARLAA---RKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1477 KQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKkrLAEEE-LKHKSEAERKAANEKQKALEdlENLRMQAEEAERQVKQ 1555
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQ--LDEEEaARQKLQLEKVTTEAKIKKLE--EDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1556 AEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENV-SKLEESLKQEHgtvlQLQQDAERLRKQQEDAENAREEAERELek 1634
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEE----KGRQELEKAKRKLEGESTDLQEQIAEL-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1635 wrQKANEALRLRLQAEEEAHKKSLaqeeaekqkeeadreakkrSKAEESALKQRDMAENELERQRRLAEstAQQKLAAEq 1714
Cdd:pfam01576 228 --QAQIAELRAQLAKKEEELQAAL-------------------ARLEEETAQKNNALKKIRELEAQISE--LQEDLESE- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1715 elirlRADFDNAEQQRSLLEDELYRLKNEV------IAAQQE-RKQLEDELSkvrsemdiliQLKSRAEKETMSNTEKSK 1787
Cdd:pfam01576 284 -----RAARNKAEKQRRDLGEELEALKTELedtldtTAAQQElRSKREQEVT----------ELKKALEEETRSHEAQLQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1788 QLLEAEATKLRDLAEEAsklraiaEEAKHQRQLAEEdaARQRAEAERilKEKLAAISDATRLKTEAEIALKEKEAENERL 1867
Cdd:pfam01576 349 EMRQKHTQALEELTEQL-------EQAKRNKANLEK--AKQALESEN--AELQAELRTLQQAKQDSEHKRKKLEGQLQEL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1868 RRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK--AIVDDTLKQ-RRVVEEEIRiLKLNFekaSSGKLD 1944
Cdd:pfam01576 418 QARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKdvSSLESQLQDtQELLQEETR-QKLNL---STRLRQ 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1945 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 2024
Cdd:pfam01576 494 LEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAE 2104
Cdd:pfam01576 574 TKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2105 EAERQKVAAEQEAANQAKAQDDA-------ERLRKDAEfEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFqvE 2177
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknvhelERSKRALE-QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF--E 730
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2178 QELTKVKLQLEETDKQkslLDDELQRLKDEVDDAMRQKAsveeELFKVKIQME-ELMKLKVRIEEENqrlmkKDKDNTQK 2256
Cdd:pfam01576 731 RDLQARDEQGEEKRRQ---LVKQVRELEAELEDERKQRA----QAVAAKKKLElDLKELEAQIDAAN-----KGREEAVK 798
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2257 FLVEEAENMKKLAEDAARLSIEAQEAarLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQ 2336
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEI--LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASG 876
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2337 K--LLEDKQLMQQR---LDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHE 2411
Cdd:pfam01576 877 KsaLQDEKRRLEARiaqLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQE 956
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2412 TEIATKEQmtevkkmefeklntskeaddLRKAITELEKEKARLKkEAEEHQNKSKEMADAQQKQIEREMtvlqqtflteK 2491
Cdd:pfam01576 957 MEGTVKSK--------------------FKSSIAALEAKIAQLE-EQLEQESRERQAANKLVRRTEKKL----------K 1005
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2492 EMLLkkekliedekkklesQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKatmdaalNKQKEAEKDILNKQKEMQELErK 2571
Cdd:pfam01576 1006 EVLL---------------QVEDERRHADQYKDQAEKGNSRMKQLKRQLE-------EAEEEASRANAARRKLQRELD-D 1062
|
1210
....*....|....*....
gi 1655274923 2572 RLEQERVLADENQKLREKL 2590
Cdd:pfam01576 1063 ATESNESMNREVSTLKSKL 1081
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
161-261 |
6.58e-14 |
|
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: 71.26 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
64-143 |
7.31e-14 |
|
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: 70.70 E-value: 7.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 64 HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM----RFHKLQNVQIALDFLRHRQV----KLVNIRNDDIADGNPKLT 135
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1655274923 136 LGLIWTII 143
Cdd:cd21223 105 LALLWRII 112
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1725-2381 |
9.23e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1725 NAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE--KETMSNTEKSKQLLEAeatKLRDLAE 1802
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEelEKELESLEGSKRKLEE---KIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1803 EASKLRAIAEEAKHQRQLAEEdaARQRAEAERILKEklaaisdatrLKTEAEIALKEKEAENERLRRQAEdeayqrkile 1882
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKE--LKEKAEEYIKLSE----------FYEEYLDELREIEKRLSRLEEEIN---------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1883 dqanqhklEIEEKIvllkkssdAEMERQKAIVDDTLKQRRVVEEEIRILKlNFEKASSGKLDLELELNKLKniaeetqqs 1962
Cdd:PRK03918 325 --------GIEERI--------KELEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLK--------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1963 KLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 2042
Cdd:PRK03918 379 KRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2043 AALKcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK 2122
Cdd:PRK03918 459 AELK--RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2123 AQDDAERLRKDAEfEAAKLAQAEAAALKQKQQADEEMAK-HKKLAEQTLKQKFQVEQELTKVK------LQLEETDKQKS 2195
Cdd:PRK03918 537 LKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAElLKELEELGFESVEELEERLKELEpfyneyLELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2196 LLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRlmkkdkdntqkflveeaENMKKLAEDAARL 2275
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR-----------------EEYLELSRELAGL 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2276 SIEAQEAARLRQIAEDDLnqqrtlaeKMLKEKMQAIQEAsrlKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEE 2355
Cdd:PRK03918 679 RAELEELEKRREEIKKTL--------EKLKEELEEREKA---KKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
650 660 670
....*....|....*....|....*....|
gi 1655274923 2356 YQRSLEAE---RKRQ-LEIIAEAEKLKLQV 2381
Cdd:PRK03918 748 IASEIFEElteGKYSgVRVKAEENKVKLFV 777
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1749-2587 |
1.01e-13 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 78.33 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1749 QERKQLE-DELSKVRSEMDILiqlksraeketmsNTEKSKQLLEAEatklrDLAEEASKLRAIAEEAKhqRQLAEE---D 1824
Cdd:NF041483 7 QESHRADdDHLSRFEAEMDRL-------------KTEREKAVQHAE-----DLGYQVEVLRAKLHEAR--RSLASRpayD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1825 AARQRAEAERILKEklaAISDATRLKTEAEIALKEKEAENERL---------RRQAE--DEAYQRKILEDQ--------- 1884
Cdd:NF041483 67 GADIGYQAEQLLRN---AQIQADQLRADAERELRDARAQTQRIlqehaehqaRLQAElhTEAVQRRQQLDQelaerrqtv 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1885 ----------ANQHKLEIEEKIVLLKKSSDAEMErqKAIVDDTLKQRRVVEEEIRILKLNFEKASS--------GKLDLE 1946
Cdd:NF041483 144 eshvnenvawAEQLRARTESQARRLLDESRAEAE--QALAAARAEAERLAEEARQRLGSEAESARAeaeailrrARKDAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1947 LELNKLKNIAE---------------ETQQSKLRAEE----------EAE-KLRRLVLEEEMRRKEAEDKVKKIAAAEEE 2000
Cdd:NF041483 222 RLLNAASTQAQeatdhaeqlrsstaaESDQARRQAAElsraaeqrmqEAEeALREARAEAEKVVAEAKEAAAKQLASAES 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2001 AARQR-KAAQEELDRL----QKKADEVRKQKE----EADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKL 2071
Cdd:NF041483 302 ANEQRtRTAKEEIARLvgeaTKEAEALKAEAEqalaDARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2072 KEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQ-----KVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaea 2146
Cdd:NF041483 382 EDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlkgaaKDDTKEYRAKTVELQEEARRLRGEAE----------- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2147 aalkqkQQADEEMAKHKKLAEQTLKQKFQveqeltkvklQLEETDKQKSLLddeLQRLKDEVDDaMRQKASVEEElfKVK 2226
Cdd:NF041483 451 ------QLRAEAVAEGERIRGEARREAVQ----------QIEEAARTAEEL---LTKAKADADE-LRSTATAESE--RVR 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2227 IQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAAR-LSIEAQEAARLRQI-AEDDLNQQRTLAEKML 2304
Cdd:NF041483 509 TEAIERATTLRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERAAReLREETERAIAARQAeAAEELTRLHTEAEERL 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2305 KEKMQAI----QEASRLKAEA-EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAE------RKRQlEIIAE 2373
Cdd:NF041483 589 TAAEEALadarAEAERIRREAaEETERLRTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEgenvavRLRS-EAAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2374 AEKLKlqvsqlSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEqmtevkkmefEKLNTSKEADD-LRKAITELEKEKA 2452
Cdd:NF041483 668 AERLK------SEAQESADRVRAEAAAAAERVGTEAAEALAAAQE----------EAARRRREAEEtLGSARAEADQERE 731
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2453 RLKKEAEEHQNKSKEMADAQQKQIERemtVLQQTFLTEKEMLLKKE---KLIEDEKKKLESQFEEEIKKAK-ALKDEQDR 2528
Cdd:NF041483 732 RAREQSEELLASARKRVEEAQAEAQR---LVEEADRRATELVSAAEqtaQQVRDSVAGLQEQAEEEIAGLRsAAEHAAER 808
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2529 QRQQMEEEKLKLKAtmDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLAD---ENQKLR 2587
Cdd:NF041483 809 TRTEAQEEADRVRS--DAYAERERASEDANRLRREAQEETEAAKALAERTVSEaiaEAERLR 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1894-2604 |
1.12e-13 |
|
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: 77.84 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1894 EKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkLDLELELNKLKNIAEETQQS-------KLRA 1966
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVS---LKLEEEIQENKDLIKENNATrhlcnllKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1967 EEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIvaaqqaalk 2046
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEI--------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2047 cNMAEQQVQSVLAQQKEDsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDD 2126
Cdd:pfam05483 236 -NDKEKQVSLLLIQITEK---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2127 AERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRlkd 2206
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK--- 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2207 evddamrqKASVEEELFKVKIQMEelmklkVRIEEENQRLMKKDKdntqkfLVEEAENMKKLAEDaarLSIEAQEAARLR 2286
Cdd:pfam05483 389 --------KSSELEEMTKFKNNKE------VELEELKKILAEDEK------LLDEKKQFEKIAEE---LKGKEQELIFLL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2287 QIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQ-RQKDLAQEQAQKLLEDKQLMQQRLDE--ETEEYQRSLEAE 2363
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEASDMtlELKKHQEDIINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2364 RKRQLEIIAEAEKLKLQVSQLseaQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKA 2443
Cdd:pfam05483 526 KKQEERMLKQIENLEEKEMNL---RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2444 -------ITELEKEKARLKKEAEEhQNKSKEMADAQQKQIEREMTVLQQTFlteKEMLLKKEKLIEDeKKKLESQFEEEI 2516
Cdd:pfam05483 603 ienknknIEELHQENKALKKKGSA-ENKQLNAYEIKVNKLELELASAKQKF---EEIIDNYQKEIED-KKISEEKLLEEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2517 KKAKALKDEqdrqrqqmeeeklklkatmdaALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK---LREKLQQM 2593
Cdd:pfam05483 678 EKAKAIADE---------------------AVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQE 736
|
730
....*....|.
gi 1655274923 2594 EEAQKSTLITE 2604
Cdd:pfam05483 737 QSSAKAALEIE 747
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3707-3745 |
1.77e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 1.77e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3707 LLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEIHDKL 3745
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1012-1904 |
1.84e-13 |
|
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: 77.70 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1012 VEKEPLKECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDILNSPQpsatapvLRSELELTVQKMdhaymlssVYLEKLKT 1091
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQ-------LKEKLELEEEYL--------LYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1092 VEMVIRNTQGAEGVLKQYENCLREVhtvpnDVKEVETYRTNLKKMRAEAEAEQ---PVFDSLEEELKKASAVSDKMSRVH 1168
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQE-----IEKEEEKLAQVLKENKEEEKEKKlqeEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1169 SERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQ 1248
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1249 LAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYE----------------LQLVAYKAQVEPLTSPLKKTKLDSASDN 1312
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKkeeleileeeeesielKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1313 IIQEYVTLRTRYSELM-TLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEA 1391
Cdd:pfam02463 470 SEDLLKETQLVKLQEQlELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1392 QELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSN 1471
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1472 AEDELKQLRDRADAAE----KLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAE 1547
Cdd:pfam02463 630 KDTELTKLKESAKAKEsglrKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1548 EAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREE 1627
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1628 AERELEKWRQKANEALRLRLQAEEEAHKKSLaqeEAEKQKEEADREAKKRSKAEESALKQRDMAENElERQRRLAESTAQ 1707
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEE---QLLIEQEEKIKEEELEELALELKEEQKLEKLAE-EELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1708 QKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMdiliqlKSRAEKETMSNTEKSK 1787
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI------KEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1788 QLLEAEATKlRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLkTEAEIALKEKEAENERL 1867
Cdd:pfam02463 940 LLLEEADEK-EKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL-EEEKKKLIRAIIEETCQ 1017
|
890 900 910
....*....|....*....|....*....|....*..
gi 1655274923 1868 RRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSD 1904
Cdd:pfam02463 1018 RLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPD 1054
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
40-145 |
1.92e-13 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 69.62 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDrvqKKTFTKWVNKHLIKSQRHvtDLYEDLRDGhnlISLLEVLsgDTL-P---------REKGRMRFHKLQNVQIAL 109
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655274923 110 DFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2717-2754 |
2.49e-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: 2.49e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 2717 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPELHNK 2754
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
161-261 |
2.89e-13 |
|
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: 68.90 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKdLGVTRLLDP 240
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAES-VGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1655274923 241 ED-VDVPHPDEKSIITYVSSLY 261
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1643-2344 |
3.12e-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: 76.70 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1643 LRLRLQAEEEAHKK-------SLAQEEAEKQKEEADREA-----KKRSKAEESALKQRDMAENELERQRRLAE------S 1704
Cdd:pfam15921 90 LQRRLNESNELHEKqkfylrqSVIDLQTKLQEMQMERDAmadirRRESQSQEDLRNQLQNTVHELEAAKCLKEdmledsN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1705 TAQQKL--------AAEQELIRLRADFDNAEQQRSLLEDELYRL--KNEVIAAQQERKQLEDELSKVRSEM----DILIQ 1770
Cdd:pfam15921 170 TQIEQLrkmmlsheGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISYLKGRIfpveDQLEA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1771 LKSRAEKET----MSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISda 1846
Cdd:pfam15921 250 LKSESQNKIelllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVS-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1847 tRLKTEAEIALKEKEAENERLRRQ---AEDEAYQRKILEDQANQHKLEIEEKIVLL-----KKSSDAEMERQK------- 1911
Cdd:pfam15921 328 -QLRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKELSLEKEQnkrlwdr 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1912 ----AIVDDTLKQ----RRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEE--- 1980
Cdd:pfam15921 407 dtgnSITIDHLRRelddRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEElta 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1981 -EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEK-QIVAAQQAALKCNMAEQ-QVQSV 2057
Cdd:pfam15921 487 kKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKLQMAEKdKVIEI 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2058 LAQQKEDsMMQNKLKEEYEKAKALARDAEAAKERAEREAAL----LRQQAEEAERQKVAAEQEAANQAKAQ---DDAERL 2130
Cdd:pfam15921 567 LRQQIEN-MTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELqefkILKDKKDAKIRELEARVSDLELEKVKlvnAGSERL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2131 RKDAEFeaaklaqaeaaalkqKQQADEEMAKHK-------KLAE--QTLKQKF-----QVEQELTKVKLQLEETDKQKSL 2196
Cdd:pfam15921 646 RAVKDI---------------KQERDQLLNEVKtsrnelnSLSEdyEVLKRNFrnkseEMETTTNKLKMQLKSAQSELEQ 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2197 LDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKlKVRIEEENQRLMKKDKdntqKFLVEEAenmKKLAEDaarLS 2276
Cdd:pfam15921 711 TRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNANKEK----HFLKEEK---NKLSQE---LS 779
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2277 IEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMqAIQEASRLKAEAE-MLQRQ-KDLAQEQAQKLLEDKQL 2344
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEV-ALDKASLQFAECQdIIQRQeQESVRLKLQHTLDVKEL 848
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1574-2381 |
3.40e-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: 76.65 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1574 SAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeaerelekwRQKANE--ALRLRLQ-AE 1650
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE------------------REKAERyqALLKEKReYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1651 EEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENElERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQR 1730
Cdd:TIGR02169 225 GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1731 SLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 1810
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1811 AEEAKHQRQLAEE----------------DAARQRAEAERILKEKLAAI-SDATRLKTEAEIALKEKEAENERLRRQAED 1873
Cdd:TIGR02169 384 RDELKDYREKLEKlkreinelkreldrlqEELQRLSEELADLNAAIAGIeAKINELEEEKEDKALEIKKQEWKLEQLAAD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1874 -EAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKAIVDDTLKQRRVVEEEIR---------ILKLN--------- 1934
Cdd:TIGR02169 464 lSKYEQELYDLKEEYDRVEKELS---KLQRELAEAEAQARASEERVRGGRAVEEVLKasiqgvhgtVAQLGsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1935 FEKASSGKLDLE-------------------------LELNKLKniAEETQQSKLRAE---------------------- 1967
Cdd:TIGR02169 541 IEVAAGNRLNNVvveddavakeaiellkrrkagratfLPLNKMR--DERRDLSILSEDgvigfavdlvefdpkyepafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1968 --------EEAEKLRRLVLEEEM--------------------------RRKEAEDKVKKIAAAEEEAARQRKAAQEELD 2013
Cdd:TIGR02169 619 vfgdtlvvEDIEAARRLMGKYRMvtlegelfeksgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2014 RLQKKADEVRkqkeEADKEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAE 2093
Cdd:TIGR02169 699 RIENRLDELS----QELSDASRKIGEIEKEI---EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2094 REAALLRQQAEEAErqkvaaeqeaanqakAQDDAERLrkdaefeaaklaqaeaaalkqkQQADEEMAKHKKLAEQTLKQK 2173
Cdd:TIGR02169 772 EDLHKLEEALNDLE---------------ARLSHSRI----------------------PEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2174 FQVEQELTKVKLQLEetdkqksLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM----KLKVRIEEENQRL--M 2247
Cdd:TIGR02169 815 REIEQKLNRLTLEKE-------YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleELEAALRDLESRLgdL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2248 KKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQqrtlaekmLKEKMQAIQEASRLKAEAEMLQRQ 2327
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE--------IEDPKGEDEEIPEEELSLEDVQAE 959
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2328 KDLAQEQAQKL-------LEDKQLMQQRLDeETEEYQRSLEAERKRQLEIIAEAEKLKLQV 2381
Cdd:TIGR02169 960 LQRVEEEIRALepvnmlaIQEYEEVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
161-258 |
4.49e-13 |
|
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: 68.18 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1655274923 240 PEDVDVPHPDEKSIITYVS 258
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2258-2569 |
5.87e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.55 E-value: 5.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2258 LVEEAENMKKLAEDAARLSIEAQEAARLRQIAED---DLNQQRTLAEKMlKEKMQAIQEASRLKAEAEML--QRQKDLAQ 2332
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAE-KARQAEMDRQAAIYAEQERMamERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2333 -EQAQKLLEDKQLMQQRLDEETE---EYQRsLEAERKRQLEIIAE----AEKLKLQVSQLSEAQAKAEEEAKKFKKQADT 2404
Cdd:pfam17380 353 iRQEERKRELERIRQEEIAMEISrmrELER-LQMERQQKNERVRQeleaARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2405 iaARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAitelEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQ 2484
Cdd:pfam17380 432 --ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ----EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2485 QTFLTEKemllKKEKLIEDEKKKLESQFEEEIKKAKAlkDEQDRQRQQMEEEKLKLKATMDA--------ALNKQKEAEK 2556
Cdd:pfam17380 506 QAMIEEE----RKRKLLEKEMEERQKAIYEEERRREA--EEERRKQQEMEERRRIQEQMRKAteersrleAMEREREMMR 579
|
330
....*....|...
gi 1655274923 2557 DILNKQKEMQELE 2569
Cdd:pfam17380 580 QIVESEKARAEYE 592
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
619-805 |
6.34e-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: 70.94 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 619 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 698
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 699 AALQTQWSWILQLCCCVEAHLKENTAYYQFFTDVKDAQDKMKKMQENMKkkySCDRTTTATRLEDLLQDAVDEKEQLNEF 778
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEELEAH 158
|
170 180
....*....|....*....|....*..
gi 1655274923 779 KTQVAGLNKRAKSIIQLKPRNPTTPIK 805
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIE 185
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1228-1572 |
1.95e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 74.00 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1228 KQRQENIQavpitdsKTLKEQLAKEKK-LLEEIEKNKdKVDECQKYAKAYID----IIKDYELQLVAYKAQVEPLTSPLK 1302
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaaIYAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1303 KTKLDsasdniiqeyvtlRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAhaK 1382
Cdd:pfam17380 359 KRELE-------------RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM--E 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1383 AIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELheLKNLSEQQiKDKSQQVDEALKSRLRIEEEIHLIriql 1462
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER--LRQQEEER-KRKKLELEKEKRDRKRAEEQRRKI---- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1463 ettvkqksnAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEEtQKKRLAEEELKHKSEAERKAANEKQKALEDLENL 1542
Cdd:pfam17380 497 ---------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340 350
....*....|....*....|....*....|
gi 1655274923 1543 RMQAEEAERQVKQAEVEKERQIQVAHVAAQ 1572
Cdd:pfam17380 567 RLEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1343-1838 |
2.76e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.26 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQNIQLE 1422
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-----------LEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1423 LHELKNLseQQIKDKSQQVdEALKSRLRIEEEihliriQLETTVKQksnaEDELKQLRDRADAAEKLRKLAQEEAEKLRK 1502
Cdd:COG4717 118 LEKLEKL--LQLLPLYQEL-EALEAELAELPE------RLEELEER----LEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1503 QVSEETqkkrlaEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQ------SAA 1576
Cdd:COG4717 185 QLSLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1577 AELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERlRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKK 1656
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR-EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1657 SLAQEEAEKqkeeadREAKKRSKAEESALKQRDMAENELERQRRLAESTAQ------QKLAAEQELIRLRADFDNAEQQ- 1729
Cdd:COG4717 338 ELLELLDRI------EELQELLREAEELEEELQLEELEQEIAALLAEAGVEdeeelrAALEQAEEYQELKEELEELEEQl 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1730 ---------------RSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksrAEKETMSNTEKSKQLLEAEa 1794
Cdd:COG4717 412 eellgeleellealdEEELEEELEELEEELEELEEELEELREELAELEAELEQL------EEDGELAELLQELEELKAE- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1655274923 1795 tkLRDLAEEASKLRAIAEE-AKHQRQLAEEDAARQRAEAERILKE 1838
Cdd:COG4717 485 --LRELAEEWAALKLALELlEEAREEYREERLPPVLERASEYFSR 527
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4295-4333 |
2.85e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 2.85e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 4295 LLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMVDRL 4333
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1770-2079 |
2.95e-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: 73.23 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 QLKSRAEKETMS-NTEKSKQLLEAEATKLRDLAEEAS----KLRAIAEEAKHQRQLAEEDAARqraEAERILKEKLAAIS 1844
Cdd:pfam17380 298 QERLRQEKEEKArEVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKR---ELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1845 DATRlktEAEIALKEKEAENERLRRQAEdEAYQRKILEDQaNQHKLEiEEKIVLLKKSSDAEMERQKAIvddtlkqRRVV 1924
Cdd:pfam17380 375 SRMR---ELERLQMERQQKNERVRQELE-AARKVKILEEE-RQRKIQ-QQKVEMEQIRAEQEEARQREV-------RRLE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1925 EEEIRILklnfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLvleEEMRRKEAEDKVKKIAAAEEEAARQ 2004
Cdd:pfam17380 442 EERAREM----ERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA---EEQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2005 RKAAQEELDRLQKK-ADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 2079
Cdd:pfam17380 515 RKLLEKEMEERQKAiYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
48-149 |
3.11e-12 |
|
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: 66.10 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 48 KTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1390-2037 |
3.70e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1390 EAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNL--SEQQIKDksqQVDEALKSRLRIEEEIHLIRIQLETTVK 1467
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFikRTENIEE---LIKEKEKELEEVLREINEISSELPELRE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1468 QKSNAEDELKQLrdradaaEKLRklaqEEAEKLRKQVSEETQKKRLAEEELKHKseaeRKAANEKQKALEDLEnlrmqae 1547
Cdd:PRK03918 222 ELEKLEKEVKEL-------EELK----EEIEELEKELESLEGSKRKLEEKIREL----EERIEELKKEIEELE------- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1548 EAERQVKQAEVEKERQIQVAhvaaqqsaaaELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREE 1627
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLS----------EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1628 AERELEKWRQKANEALRLR-LQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEEsalkqrdmAENELERQRRLAESTA 1706
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE--------EISKITARIGELKKEI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1707 QQKLAAEQELIRLRADFD------NAEQQRSLLED---ELYRLKNEVIAAQQERKQLEDELSKVRSEM----------DI 1767
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPvcgrelTEEHRKELLEEytaELKRIEKELKEIEEKERKLRKELRELEKVLkkeseliklkEL 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1768 LIQLKSRAEKETMSNTEKskqlLEAEATKLRDLAEEASKLRA----IAEEAKHQRQLAEEDAARQRAEAEriLKEKLAAI 1843
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEE----LEKKAEEYEKLKEKLIKLKGeiksLKKELEKLEELKKKLAELEKKLDE--LEEELAEL 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1844 sdatrLKTEAEIALKEKEAENERLRrqaEDEAYQRKILEDQANQHKLEIEEKivlLKKSSDAEMERQKAIVDDTLKQRRV 1923
Cdd:PRK03918 576 -----LKELEELGFESVEELEERLK---ELEPFYNEYLELKDAEKELEREEK---ELKKLEEELDKAFEELAETEKRLEE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1924 VEEEIRILKLNF-----EKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRrlvlEEEMRRKEAEDKVKKIaaae 1998
Cdd:PRK03918 645 LRKELEELEKKYseeeyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK----EELEEREKAKKELEKL---- 716
|
650 660 670
....*....|....*....|....*....|....*....
gi 1655274923 1999 eeaarqrKAAQEELDRLQKKadeVRKQKEEADKEAEKQI 2037
Cdd:PRK03918 717 -------EKALERVEELREK---VKKYKALLKERALSKV 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1682-2136 |
4.00e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1682 ESALKQRDMAENELERQRRLAESTAQqklAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKV 1761
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1762 RSEMDILIQL--------KSRAEKEtMSNTEKSKQLLEAEATKLRDLAEEAsKLRAIAEEAKHQRQLAEedAARQRAEAE 1833
Cdd:COG4913 322 REELDELEAQirgnggdrLEQLERE-IERLERELEERERRRARLEALLAAL-GLPLPASAEEFAALRAE--AAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1834 RILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAE--DEAYQ--RKILEDQANQHK---------LEIEEK----- 1895
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLalRDALAEALGLDEaelpfvgelIEVRPEeerwr 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1896 --------------IVllkkssDAEMERQ-KAIVDDTLKQRRVVEEEIRILKLNFEKAS------SGKLD---------L 1945
Cdd:COG4913 478 gaiervlggfaltlLV------PPEHYAAaLRWVNRLHLRGRLVYERVRTGLPDPERPRldpdslAGKLDfkphpfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1946 ELELNKLKNIA--EETQQskLRAEEEA--------------EK------LRRLVLEEEMRRK--EAEDKVKKIAAAEEEA 2001
Cdd:COG4913 552 EAELGRRFDYVcvDSPEE--LRRHPRAitragqvkgngtrhEKddrrriRSRYVLGFDNRAKlaALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2002 ARQRKAAQEELDRLQKKADEVRKQKEEADKEAEkqiVAAQQAALkcnmaeQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL 2081
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEYSWDEID---VASAEREI------AELEAELERLDASSDDLAALEEQLEELEAE 700
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2082 ARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEF 2136
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1690-2036 |
5.00e-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: 72.46 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1690 MAENELERQrrLAESTAQQKLAAEQELirlRADFDNAEQQRslledeLYRLKNEVIAAQQERKQLEDELSKVRSEMDIli 1769
Cdd:pfam17380 265 MTENEFLNQ--LLHIVQHQKAVSERQQ---QEKFEKMEQER------LRQEKEEKAREVERRRKLEEAEKARQAEMDR-- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 QLKSRAEKETMSnTEKSKQLleaEATKLRDLAEEASKLRA--IAEEAKHQRQLaeedaarQRAEAERILKEKlaaisdat 1847
Cdd:pfam17380 332 QAAIYAEQERMA-MEREREL---ERIRQEERKRELERIRQeeIAMEISRMREL-------ERLQMERQQKNE-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1848 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEI----EEKIVLLKKSSDAEMERQkaivddtlkqrrv 1923
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVrrleEERAREMERVRLEEQERQ------------- 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1924 veEEIRILKLNFEKASSGKLDLELELNKLKNIAEetqQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAAR 2003
Cdd:pfam17380 460 --QQVERLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER 534
|
330 340 350
....*....|....*....|....*....|...
gi 1655274923 2004 QRKAaqEELDRLQKKADEVRKQKEEADKEAEKQ 2036
Cdd:pfam17380 535 RREA--EEERRKQQEMEERRRIQEQMRKATEER 565
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3045-3082 |
5.88e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 5.88e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 3045 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPELHEKL 3082
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
163-262 |
6.78e-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: 64.67 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 163 KEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMgKVYRQTN----LENLEQAFNVAEK-DLGVTRL 237
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPK-INKKPKSpfkkRENINLFLNACKKlGLPELDL 79
|
90 100
....*....|....*....|....*
gi 1655274923 238 LDPEDVdVPHPDEKSIITYVSSLYD 262
Cdd:cd00014 80 FEPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2316-2625 |
6.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2316 RLKAEAE------MLQRQKDLAQEQAQKL-LEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaq 2388
Cdd:COG1196 204 PLERQAEkaeryrELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2389 akaeeeakkfkkqaDTIAARLHETEIATKEQMTEVKKMEFEKlntsKEADDLRKAITELEKEKARLKKEAEEHQnksKEM 2468
Cdd:COG1196 281 --------------LELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEELE---EEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2469 ADAQQKQIEREmtvlqqtflTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAAL 2548
Cdd:COG1196 340 EELEEELEEAE---------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2549 NKQKEAEKdiLNKQKEMQELERKRLEQERvLADENQKLREKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVLDG 2625
Cdd:COG1196 411 ALLERLER--LEEELEELEEALAELEEEE-EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
523-712 |
6.90e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 67.86 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 523 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 599
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 600 LQYAKLLNSSKSRLRNLD---SLHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDI 676
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1655274923 677 QAMGDRLVKDGHPGK-KTVEAFTAALQTQWSWILQLC 712
Cdd:cd00176 166 NELAEELLEEGHPDAdEEIEEKLEELNERWEELLELA 202
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
163-258 |
7.14e-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: 64.71 E-value: 7.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 163 KEKLLLWSQRMtdgYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDPE 241
Cdd:cd21229 5 KKLMLAWLQAV---LPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1655274923 242 DVDVPHPDEKSIITYVS 258
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1245-1814 |
1.07e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1245 LKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTlrtRY 1324
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE---EY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1325 SELMTLTSQYIKFITDTQRRLEDEEKAAEKLKaEEQKKMAEMQAELDKqkqlaeahakaIAKAEKEAQELKLRMQEEVSK 1404
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIE-ERIKELEEKEERLEE-----------LKKKLKELEKRLEELEERHEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1405 RETAavdaeKQKQNiQLELHElKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLI---RIQLETTVKQKSNAEDELKQLRD 1481
Cdd:PRK03918 364 YEEA-----KAKKE-ELERLK-KRLTGLTPEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1482 RADAAEklRKLAQEEAEKLRKQVSEETQKkrlAEEELKHKSEAERKAANEK---QKALEDLENLRMQAEEAErQVKQAEv 1558
Cdd:PRK03918 437 KCPVCG--RELTEEHRKELLEEYTAELKR---IEKELKEIEEKERKLRKELrelEKVLKKESELIKLKELAE-QLKELE- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1559 EKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGtvlqLQQDAERLRKQQEDAENAREEAERELEKWRQK 1638
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1639 ANEALRLRLQAEEEAHKKSLaqeeaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIR 1718
Cdd:PRK03918 586 SVEELEERLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1719 LRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksRAEKETMSNTEKSKQLLEAEATKLR 1798
Cdd:PRK03918 652 LEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVE 724
|
570
....*....|....*.
gi 1655274923 1799 DLAEEASKLRAIAEEA 1814
Cdd:PRK03918 725 ELREKVKKYKALLKER 740
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2010-2605 |
1.09e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2010 EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAK 2089
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2090 ER---AEREAALLRQQAEEAErqkvaaeqeaanqakaqddaERLRKDaefeaaklaqaeaaalkqkqqadEEMAKHKKLA 2166
Cdd:PRK03918 238 EEieeLEKELESLEGSKRKLE--------------------EKIREL-----------------------EERIEELKKE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2167 EQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRL 2246
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2247 MKKDKD----NTQKFLVEEAENMKKLA-----EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRL 2317
Cdd:PRK03918 355 EELEERhelyEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2318 KAEAEMLQRQkdLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEA--ERKRQLEIIAEAE----KLKLQVSQLSEAQAKA 2391
Cdd:PRK03918 435 KGKCPVCGRE--LTEEHRKELLEEYTAELKRIEKELKEIEEKERKlrKELRELEKVLKKEseliKLKELAEQLKELEEKL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2392 EEEAKKFKKQADTIAARLHETEIATKEQMTEVKKmEFEKLNT-SKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMAD 2470
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK-ELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2471 AQQKQIE---REMTVLQQTfLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKAtmdaa 2547
Cdd:PRK03918 592 ERLKELEpfyNEYLELKDA-EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR----- 665
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2548 lNKQKEAEKDILNKQKEMQELERKRLEQERVLadenQKLREKLQQMEEAQKSTLITEK 2605
Cdd:PRK03918 666 -EEYLELSRELAGLRAELEELEKRREEIKKTL----EKLKEELEEREKAKKELEKLEK 718
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
161-263 |
1.18e-11 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 64.30 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTNLENLEQAFNVAEKDLGVTRLLDP 240
Cdd:cd21196 3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
|
90 100
....*....|....*....|...
gi 1655274923 241 EDVdVPHPDEKSIITYVSSLYDA 263
Cdd:cd21196 83 QAV-VAGSDPLGLIAYLSHFHSA 104
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1344-1975 |
1.49e-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: 70.91 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1344 RLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK------------------R 1405
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatrhlcnllK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1406 ETAAVDAEK------QKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRL----RIEEEIHLIRIQLETTVKQKSNAEDE 1475
Cdd:pfam05483 162 ETCARSAEKtkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEYKKEINDKEKQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1476 LKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANE-------KQKALEDLENLRMQAEE 1548
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKEledikmsLQRSMSTQKALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1549 AERQVKQAEVEKERQIQVAHVA--AQQSAAAELRSKQMSFAE----NVSKLEESLKQEHGTVLQLQQDAERLR------- 1615
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAkaAHSFVVTEFEATTCSLEEllrtEQQRLEKNEDQLKIITMELQKKSSELEemtkfkn 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1616 -KQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSkaEESALKQRDMAENE 1694
Cdd:pfam05483 402 nKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS--EEHYLKEVEDLKTE 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1695 LERQR-RLAESTAQ--------QKLAAEQ-----ELIRLRADFDNAEQQR-------SLLEDELYRLKNEVIAAQQERKQ 1753
Cdd:pfam05483 480 LEKEKlKNIELTAHcdklllenKELTQEAsdmtlELKKHQEDIINCKKQEermlkqiENLEEKEMNLRDELESVREEFIQ 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1754 LEDElskVRSEMDiLIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKlrAIAEEAKHQRQLAEEDAARQRA-EA 1832
Cdd:pfam05483 560 KGDE---VKCKLD-KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNK--NIEELHQENKALKKKGSAENKQlNA 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1833 ERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQA-EDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK 1911
Cdd:pfam05483 634 YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHK 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 1912 AIVDDTLKQRrvvEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRR 1975
Cdd:pfam05483 714 HQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2010-2597 |
1.62e-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: 71.15 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2010 EELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLA-QQKEDSMMQNKLKEEYEKAKALARDAEAA 2088
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQvLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2089 KERAEREAALLRQQAEEAERQkvaaeQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAaalkqKQQADEEMAKHKKlAEQ 2168
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELR-----AQEAVLEETQERINRARKAAPLAAHIKAVTQI-----EQQAQRIHTELQS-KMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2169 TLKQKFQVEQELTKVKLQLEETDKqkslLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmk 2248
Cdd:TIGR00618 322 SRAKLLMKRAAHVKQQSSIEEQRR----LLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2249 kdKDNTQKFLVEEAENMKKLAEDAARlSIEAQEAARLR---QIAEDDLNQQRTLAEKMLKEKMQAIQEASR----LKAEA 2321
Cdd:TIGR00618 396 --QSLCKELDILQREQATIDTRTSAF-RDLQGQLAHAKkqqELQQRYAELCAAAITCTAQCEKLEKIHLQEsaqsLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2322 EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ-----VSQLSEAQAKAEEEAK 2396
Cdd:TIGR00618 473 QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2397 KFKKQADTIAA---RLHETEIATKEQMTEVKKmefEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQ 2473
Cdd:TIGR00618 553 SERKQRASLKEqmqEIQQSFSILTQCDNRSKE---DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2474 K-----QIEREMTvLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMeeeklKLKATMDAAL 2548
Cdd:TIGR00618 630 VrlhlqQCSQELA-LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLT-----YWKEMLAQCQ 703
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2549 NKQKEAEKDILNKQKEMQELE------RKRLEQERVLADENQK-----LREKLQQMEEAQ 2597
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIEnassslGSDLAAREDALNQSLKelmhqARTVLKARTEAH 763
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
41-140 |
1.66e-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: 63.98 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRvQKKTFTKWVNKhlIKSQRHVTDLYEDLRDGHNLISLLEVLSGDT--------LPREKGRMRFHKLQNVQIALDFL 112
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1655274923 113 RHRQVKLVNIRNDDIADGNPKLTLGLIW 140
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1325-1809 |
1.71e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.84 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1325 SELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKkmaemQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK 1404
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEER-----REELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1405 RETAAVDAEkqkqniqlELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD 1484
Cdd:PRK02224 288 LEELEEERD--------DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1485 ----AAEKLRKLAQEEAEKLRKQVSE--------ETQKKRLAE--------EELKHKSEAERKAANEKQKALE-DLENLR 1543
Cdd:PRK02224 360 elreEAAELESELEEAREAVEDRREEieeleeeiEELRERFGDapvdlgnaEDFLEELREERDELREREAELEaTLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1544 MQAEEA--------------------------ERQVKQAEVEKER---QIQVAHVAA---QQSAAAELRSKQMSFAENVS 1591
Cdd:PRK02224 440 ERVEEAealleagkcpecgqpvegsphvetieEDRERVEELEAELedlEEEVEEVEErleRAEDLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1592 KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAD 1671
Cdd:PRK02224 520 DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAENELERQRRLAE-STAQQKLAAEQELIRL---RADFDNAEQQRSLLEDELYRLKneviaa 1747
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELNDERRERLAEkRERKRELEAEFDEARIeeaREDKERAEEYLEQVEEKLDELR------ 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1748 qQERKQLEDELSKVRSEMDILIQLKSRAEKetmsntekskqlLEAEATKLRDLAEEASKLRA 1809
Cdd:PRK02224 674 -EERDDLQAEIGAVENELEELEELRERREA------------LENRVEALEALYDEAEELES 722
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1273-1874 |
1.72e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1273 AKAYIDIIKDYELQLVAYKAQVEPLTsPLKKTKldsasdniiQEYVTLRTRYSELMTLtsqyikfitDTQRRLEDEEKAA 1352
Cdd:COG4913 230 LVEHFDDLERAHEALEDAREQIELLE-PIRELA---------ERYAAARERLAELEYL---------RAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1353 EKLKAEEQkkmaEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAA----VDAEKQKQNIQLELHELKN 1428
Cdd:COG4913 291 ELLEAELE----ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLereiERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1429 L----------SEQQIKDKSQQVDEALKsrlRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE 1498
Cdd:COG4913 367 LlaalglplpaSAEEFAALRAEAAALLE---ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1499 KLRKQVSEETQkkrLAEEELKHKSEA-ERKAANEK-QKALEDLenLRMQA------EEAERQVKQA--EVEKERQIQVAH 1568
Cdd:COG4913 444 ALRDALAEALG---LDEAELPFVGELiEVRPEEERwRGAIERV--LGGFAltllvpPEHYAAALRWvnRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1569 VAAQQSAAAELRSKQMSFAENV----SKLEESLKQEHG---------TVLQLQQD-----AERLRKQqedaenareeAER 1630
Cdd:COG4913 519 VRTGLPDPERPRLDPDSLAGKLdfkpHPFRAWLEAELGrrfdyvcvdSPEELRRHpraitRAGQVKG----------NGT 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1631 ELEKWRQKA----------NEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELER-QR 1699
Cdd:COG4913 589 RHEKDDRRRirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1700 RLAEstaqqklaAEQELIRLRADFDNAEQqrslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKET 1779
Cdd:COG4913 669 EIAE--------LEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1780 MSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKE--------------KLAAISD 1845
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPE 816
|
650 660 670
....*....|....*....|....*....|
gi 1655274923 1846 -ATRLKTEAEIALKEKEAENERLRRQAEDE 1874
Cdd:COG4913 817 yLALLDRLEEDGLPEYEERFKELLNENSIE 846
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1065-1810 |
2.71e-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: 70.38 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1065 RSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHT--VPNDVKEVETYRTNLKKMRAEAEA 1142
Cdd:TIGR00618 165 KKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHerKQVLEKELKHLREALQQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1143 EQPVFDSLEEELKKASAVSDKMSR---------VHSERDAELDQHRQ---------HLSSLQDRWKAVFTQIDLRQRELD 1204
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARieelraqeaVLEETQERINRARKaaplaahikAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1205 QL--GRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEknkdKVDECQKYAKAYIDIIKD 1282
Cdd:TIGR00618 325 KLlmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH----TLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1283 YELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEyvtLRTRYSELMTLTSQyiKFITDTQRRLEDEEKAAEKLKAEEQkK 1362
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE---LQQRYAELCAAAIT--CTAQCEKLEKIHLQESAQSLKEREQ-Q 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1363 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKReTAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVD 1442
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQL-ETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1443 EALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRdraDAAEKLRKLAQEEAEkLRKQVSEETQKKrlaEEELKHKS 1522
Cdd:TIGR00618 553 SERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ---NITVRLQDLTEKLSE-AEDMLACEQHAL---LRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1523 EAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQmSFAENVSKLEESLKQEHG 1602
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-SEKEQLTYWKEMLAQCQT 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1603 TVLQLQQDAERLRKQQEDAenareeaerelekwrQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADRE-AKKRSKAE 1681
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEI---------------ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTeAHFNNNEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1682 ESALKQRDMAENELER----QRRLAEsTAQQKLAAEQELIRLRADFDnaEQQRSLledelyrlknEVIAAQQERKQLede 1757
Cdd:TIGR00618 770 VTAALQTGAELSHLAAeiqfFNRLRE-EDTHLLKTLEAEIGQEIPSD--EDILNL----------QCETLVQEEEQF--- 833
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1758 LSKVRSEMDILIQLKSRAEKetMSNTEKSKQLLEAEATKLRDLAEEASKLRAI 1810
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLK--YEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1350-1885 |
2.99e-11 |
|
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: 70.25 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1350 KAAEKLKAEEQKKMAEMQAELDKQ-----KQLAEAHAK----------AIAKAEKE---AQELKLRMQEEvsKRETAAVD 1411
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLlrtldDQWKEKRDElngelsaadaAVAKDRSEleaLEDQHGAFLDA--DIETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1412 AEkQKQNIQLEL------HELKNLSEQQIKDKSQQVDEALKSRL-----RIEEEIHLIRiqlETTVKQKSNAEDELKQL- 1479
Cdd:pfam12128 346 QE-QLPSWQSELenleerLKALTGKHQDVTAKYNRRRSKIKEQNnrdiaGIKDKLAKIR---EARDRQLAVAEDDLQALe 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1480 ---RDRADAA-------EKLRKLAQEEAEKLRKQV---SEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQA 1546
Cdd:pfam12128 422 selREQLEAGklefneeEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRR 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1547 EEAERQVKQAEVE-KERQIQVAHVAAQQSAAAE-----LRSKQMSFAENVSKLEESlKQEHGTVLQLQQDAERLRKQQED 1620
Cdd:pfam12128 502 DQASEALRQASRRlEERQSALDELELQLFPQAGtllhfLRKEAPDWEQSIGKVISP-ELLHRTDLDPEVWDGSVGGELNL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1621 AENAREEAERELEKWRQkANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQrdMAENELERQRR 1700
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAA-SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFART--ALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1701 LAESTAQQKLAAEQELIRLRadfDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM---------DILIQL 1771
Cdd:pfam12128 658 LFDEKQSEKDKKNKALAERK---DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwqvvegaldAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1772 KSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAK--HQRQlaeEDAARQRAEAER----------ILKEK 1839
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRtlERKI---ERIAVRRQEVLRyfdwyqetwlQRRPR 811
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1655274923 1840 LAA-ISDATRLKTEAEIALKEKEAENERLRRQAEDEayqRKILEDQA 1885
Cdd:pfam12128 812 LATqLSNIERAISELQQQLARLIADTKLRRAKLEME---RKASEKQQ 855
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1673-1875 |
4.30e-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: 68.25 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1673 EAKKRSKAEESALKQR-DMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQER 1751
Cdd:COG4942 20 DAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1752 KQLEDELSKV---------RSEMDILiqLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ--- 1819
Cdd:COG4942 100 EAQKEELAELlralyrlgrQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAele 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1820 --LAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAEN-----ERLRRQAEDEA 1875
Cdd:COG4942 178 alLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElealiARLEAEAAAAA 240
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1471-2479 |
4.85e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.60 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1471 NAEDELKQLRDRADAAEKLRKlAQEEAEKLRKQVSEETQKKRLAEEELKHKS-------EAERkAANEKQKALEDLENLR 1543
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAA-EQYRLVEMARELAELNEAESDLEQDYQAASdhlnlvqTALR-QQEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1544 MQAEEaerqvkQAEVEKERQIQVAHVAAQQSAAAElrsKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQE---D 1620
Cdd:PRK04863 362 ERLEE------QNEVVEEADEQQEENEARAEAAEE---EVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcgL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1621 AENAREEAERELEKWRQKANEALRLRLQAEE---------EAHKKSLAQEEAEKQKEeaDREAKKRS--KAEESALKQRD 1689
Cdd:PRK04863 433 PDLTADNAEDWLEEFQAKEQEATEELLSLEQklsvaqaahSQFEQAYQLVRKIAGEV--SRSEAWDVarELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1690 MAENELERQRRLAEstAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEviaAQQERKQLEDELSKV---RSEM- 1765
Cdd:PRK04863 511 LAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSESVSEArerRMALr 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1766 DILIQLKSRAEKetmsNTEKSKQLLEAEA--TKLRDLAEEA--------SKLRAIAEEAKHQRQLAEEDAARQRAEAERI 1835
Cdd:PRK04863 586 QQLEQLQARIQR----LAARAPAWLAAQDalARLREQSGEEfedsqdvtEYMQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1836 LKEKLAAISDATRLKTEAE-------------IALKEK---EAENERLR-----RQAEDEAYQRKILEDQANQHKLeIEE 1894
Cdd:PRK04863 662 ERLSQPGGSEDPRLNALAErfggvllseiyddVSLEDApyfSALYGPARhaivvPDLSDAAEQLAGLEDCPEDLYL-IEG 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1895 KIVLLKKSSDAEMERQKAIVDdtlkqrRVVEEEIRILKLNfEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLR 1974
Cdd:PRK04863 741 DPDSFDDSVFSVEELEKAVVV------KIADRQWRYSRFP-EVPLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQ 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1975 RLVL------------------EEEMR-----RKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEE--A 2029
Cdd:PRK04863 814 RLHQafsrfigshlavafeadpEAELRqlnrrRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlA 893
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2030 DK--EAEKQIVAAQQAAL---KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAE----AAKERAEREAALLR 2100
Cdd:PRK04863 894 DRveEIREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKqqafALTEVVQRRAHFSY 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2101 QQAEEaerqkvaaeqeaaNQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKL------AEQTLKqkf 2174
Cdd:PRK04863 974 EDAAE-------------MLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLkssydaKRQMLQ--- 1037
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2175 QVEQELTKVKLQLEETdkqkslLDDELQRLKDEVDDAMRQKASVEEELFKvKIQMEELmklkvRIEEENQRLMKKDKDNT 2254
Cdd:PRK04863 1038 ELKQELQDLGVPADSG------AEERARARRDELHARLSANRSRRNQLEK-QLTFCEA-----EMDNLTKKLRKLERDYH 1105
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2255 QkfLVEEAENMKKLAEDAARLSIEAQEAARL--RQIAEDDLNQQRTLAEKMLKEKMQAIqeasrlkAEAEMLQrqkdlaq 2332
Cdd:PRK04863 1106 E--MREQVVNAKAGWCAVLRLVKDNGVERRLhrRELAYLSADELRSMSDKALGALRLAV-------ADNEHLR------- 1169
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2333 eQAQKLLEDkqlmqqrldeeteeyqrSLEAERKRQLeIIAEAEKLKLQVSQlseaqakaeeeakkfkkqaDTIaarlhet 2412
Cdd:PRK04863 1170 -DVLRLSED-----------------PKRPERKVQF-YIAVYQHLRERIRQ-------------------DII------- 1204
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2413 eiatkeqmtevkkmefeklntskEADDLRKAITELEKEKARLKKEAEEHQNK----SKEMADAQQKQIERE 2479
Cdd:PRK04863 1205 -----------------------RTDDPVEAIEQMEIELSRLTEELTSREQKlaisSESVANIIRKTIQRE 1252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1721-2467 |
5.35e-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: 69.37 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1721 ADFDNAE---QQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSemdiLIQLKSRAEKETMSNTEKSKQLLEAEATKL 1797
Cdd:pfam05483 68 SDFENSEglsRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1798 RDLAEEASKLRaiaeeakHQRQLAEEDAARQRAEAERILKEKlaaiSDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1877
Cdd:pfam05483 144 KDLIKENNATR-------HLCNLLKETCARSAEKTKKYEYER----EETRQVYMDLNNNIEKMILAFEELRVQAENARLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1878 R--KILEDQANQHKLEIEEKivllKKSSDAEMERQKAIVDDTlkqrrvvEEEIRILKLNFEkassgkldLELELNKLKNI 1955
Cdd:pfam05483 213 MhfKLKEDHEKIQHLEEEYK----KEINDKEKQVSLLLIQIT-------EKENKMKDLTFL--------LEESRDKANQL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1956 AEETQQsklraeeEAEKLRRLVLEEEMRRKEAEDkvkkIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEK 2035
Cdd:pfam05483 274 EEKTKL-------QDENLKELIEKKDHLTKELED----IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2036 QIVAAQQAALKCNMAEQQVQSVLAQQkedsmmQNKLKEEYEKAKALARDAEAAKERAEREAALLR-QQAEEAERQKVAAE 2114
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTE------QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnKEVELEELKKILAE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2115 QEAANQAKAQddAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQK 2194
Cdd:pfam05483 417 DEKLLDEKKQ--FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2195 SLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKlKVRIEEENQRLMKKDKDNTQKFLVEEAENMK----KLAE 2270
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVREEFIQKGDEVKckldKSEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2271 DAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLD 2350
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2351 EETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQ---------------LSEAQAKAEEEAKKFKKQADTIAARLHETEIA 2415
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavklqkeidkrcqhkIAEMVALMEKHKHQYDKIIEERDSELGLYKNK 733
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2416 TKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKE 2467
Cdd:pfam05483 734 EQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1746-2486 |
6.51e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 69.23 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1746 AAQQERKQLEDELSKVrsemDILIQLKSRAEKETMSnTEKSKQLLEAEATKLRDLAEEasklRAIAEEAKHQRQLAEEDA 1825
Cdd:TIGR00618 160 AKSKEKKELLMNLFPL----DQYTQLALMEFAKKKS-LHGKAELLTLRSQLLTLCTPC----MPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1826 ARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVllkkssdA 1905
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAV-------T 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1906 EMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkniaeETQQSKLRAEEEAEKLRRlvlEEEMRRK 1985
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTL-----HSQEIHIRDAHEVATSIR---EISCQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1986 EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKE------AEKQIVAAQQAALKCNMA-EQQVQSVL 2058
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlahAKKQQELQQRYAELCAAAiTCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2059 AQQKEDSMMQNKLKEEYEKAKALARDAEAAKE-RAEREAALLRQQAE--------------------------------- 2104
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRkKAVVLARLLELQEEpcplcgscihpnparqdidnpgpltrrmqrgeq 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2105 -----EAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQE 2179
Cdd:TIGR00618 536 tyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2180 LTKVKLQLEETDKQKSLlddELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM--KLKVRIEEENQRLMKKDKDNTQKF 2257
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRL---HLQQCSQELALKLTALHALQLTLTQERVREHALSirVLPKELLASRQLALQKMQSEKEQL 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2258 ------LVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKE-------KMQAIQEASRLKAEAEML 2324
Cdd:TIGR00618 693 tywkemLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKARTEAHFNNNEEVTA 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2325 QRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEII-AEAEKLKLQVSQLSEAQAKAEEEAKKFKKQAD 2403
Cdd:TIGR00618 773 ALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2404 TIAARLHETEIATKEQ---MTEVKKME-FEKLNTSKEADDLRKAITELEKEKARLKKEAEE---HQNKSKEMADAQQKQI 2476
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQakiIQLSDKLNgINQIKIQFDGDALIKFLHEITLYANVRLANQSEgrfHGRYADSHVNARKYQG 932
|
810
....*....|
gi 1655274923 2477 EREMTVLQQT 2486
Cdd:TIGR00618 933 LALLVADAYT 942
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1455-1832 |
7.15e-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: 68.61 E-value: 7.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1455 IHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRklaqeEAEKLRKQvsEETQKKRLAEEELKHKSEAER-KAANEKQ 1533
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR-----EVERRRKL--EEAEKARQAEMDRQAAIYAEQeRMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1534 KALEdlenlRMQAEEAERQVKQ-------AEVEKERQIQVAHVAAQQSAAaelRSKQMSFAENVSKLEESLKQEhgTVLQ 1606
Cdd:pfam17380 348 RELE-----RIRQEERKRELERirqeeiaMEISRMRELERLQMERQQKNE---RVRQELEAARKVKILEEERQR--KIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1607 LQQDAERLRKQQEDAENAreeAERELEKwrQKANEALRLRLQAEEEAHKkslaqeeaekQKEEADREAKKRSKAEESALK 1686
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQR---EVRRLEE--ERAREMERVRLEEQERQQQ----------VERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1687 QRDMAENELERQRRLaestaqqklaaEQELIRLRADFDNAEQQRSLLEDELYRLKNeVIAAQQERKQLEDElskvrsemd 1766
Cdd:pfam17380 483 KRDRKRAEEQRRKIL-----------EKELEERKQAMIEEERKRKLLEKEMEERQK-AIYEEERRREAEEE--------- 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 1767 iliqlkSRAEKEtmsnTEKSKQLLEaeatKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEA 1832
Cdd:pfam17380 542 ------RRKQQE----MEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1957-2296 |
7.99e-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: 68.61 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1957 EETQQSKLRAEEEA---EKLRRLVLEEEMRRKEAE-DKVKKIAAAEEEAARQRkaaQEELDRLQKkadEVRKQKEEADKE 2032
Cdd:pfam17380 294 EKMEQERLRQEKEEkarEVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMER---ERELERIRQ---EERKRELERIRQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2033 AEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVA 2112
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2113 AEQEAANQAKAQDDAERLRKdaefeaaklaqaeaaalkqkqqaDEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDK 2192
Cdd:pfam17380 448 MERVRLEEQERQQQVERLRQ-----------------------QEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2193 QKSLLDDELQRLKDEVDDAMRQKASVEEElfkvkiqmeelmklKVRIEEENQRLMKKDKDNTQKflveeAENMKKLAEDA 2272
Cdd:pfam17380 505 KQAMIEEERKRKLLEKEMEERQKAIYEEE--------------RRREAEEERRKQQEMEERRRI-----QEQMRKATEER 565
|
330 340
....*....|....*....|....
gi 1655274923 2273 ARLSIEAQEAARLRQIAEDDLNQQ 2296
Cdd:pfam17380 566 SRLEAMEREREMMRQIVESEKARA 589
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2301-2599 |
1.39e-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: 67.84 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEdkQLMQQRLDEETEEYQRslEAERKRQLEiiaEAEKLKlq 2380
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFE--KMEQERLRQEKEEKAR--EVERRRKLE---EAEKAR-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2381 vsqlseaqakaeeeakkfKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEK--EKARLKKEA 2458
Cdd:pfam17380 326 ------------------QAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRmrELERLQMER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2459 EEHQNKSKEMADAQQKQI----EREMTVLQQTFLTEKeMLLKKEKLIEDEKKKLESQFEEEIKKAKalKDEQDRQ----- 2529
Cdd:pfam17380 388 QQKNERVRQELEAARKVKileeERQRKIQQQKVEMEQ-IRAEQEEARQREVRRLEEERAREMERVR--LEEQERQqqver 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2530 -RQQMEEEKLKlKATMDAALNKQKEAE---KDILnkQKEMQELERKRLEQERvladeNQKLREKlqQMEEAQKS 2599
Cdd:pfam17380 465 lRQQEEERKRK-KLELEKEKRDRKRAEeqrRKIL--EKELEERKQAMIEEER-----KRKLLEK--EMEERQKA 528
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1675-2109 |
1.64e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1675 KKRSKAEESALKQRDmaenELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLK---------NEVI 1745
Cdd:COG4717 60 KPQGRKPELNLKELK----ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEkllqllplyQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1746 AAQQERKQLEDELSKVRSEMDILIQLKSRAEKetmsntekskqlLEAEATKLR-DLAEEASKLRAIAEEAKHQRQLAEED 1824
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEE------------LEAELAELQeELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1825 AARQRAEAERILKEKLAAISDAtrlktEAEIALKEKEAENERLRRQAEDEAYQRKIL---------EDQANQHKLEIEEK 1895
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEEL-----EEELEQLENELEAAALEERLKEARLLLLIAaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1896 IVLL----------KKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDlelELNKLKNIAEETQQSKLR 1965
Cdd:COG4717 279 LFLVlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE---ELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1966 AEEEAEKLRRLVLEEEMRRKEAEDKVKKIaaaeeEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAL 2045
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDE-----EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2046 kcnmaEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKE--RAEREAALLRQQAEEAERQ 2109
Cdd:COG4717 431 -----EEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEE 491
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3945-3983 |
1.74e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.74e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3945 LLEAQAATGYIIDPIKSLKLTVNEAVSMGTVGPEFKDKL 3983
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2793-2830 |
1.74e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.49 E-value: 1.74e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 2793 VLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEMNKI 2830
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2161-2600 |
1.89e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 67.35 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2161 KHKKLAEQTLKQKFQV----------EQELTKVKLQLEETDKQKSLLDDELQRLKD-------EVDDAMRQKASVEEELF 2223
Cdd:TIGR04523 212 KNKSLESQISELKKQNnqlkdniekkQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsekqkELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2224 KVKIQMEELMKLK-------VRIEEENQrlmKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQ 2296
Cdd:TIGR04523 292 QLKSEISDLNNQKeqdwnkeLKSELKNQ---EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2297 RTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIiaeaEK 2376
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI----KD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2377 LKLQVSQLSEAqakaeeeakkfkkqadtiaarLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKK 2456
Cdd:TIGR04523 445 LTNQDSVKELI---------------------IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2457 EAEEHQNKSKEMADAQQKQIEREMTVlqqtfltEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEE 2536
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKL-------ESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2537 KLKLKATMDAA--LNKQKEAEKDILNKQKEMQELERKRLEQERVLAD-ENQKLREKLQQMEEAQKST 2600
Cdd:TIGR04523 577 QKSLKKKQEEKqeLIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKkENEKLSSIIKNIKSKKNKL 643
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2164-2588 |
2.09e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2164 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEeelfkvkiQMEELMKLKVRIEEEN 2243
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--------LYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2244 QRLmkkdkdntqKFLVEEAENMKKLAEDAARLSIEAQEAarlrqiaeddlnqQRTLAEKMLKEKMQAIQEASRLKAEAEM 2323
Cdd:COG4717 146 ERL---------EELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2324 LQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAE----------------------AEKLKLQV 2381
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2382 SQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEh 2461
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2462 qnkskemadAQQKQIEREMT-VLQQTFLTEKEMLLKKEKL------IEDEKKKLESQFEEEIKKAKALKDEQDRQrqQME 2534
Cdd:COG4717 363 ---------LQLEELEQEIAaLLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEE--ELE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2535 EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELE------RKRLEQERVLADENQKLRE 2588
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEedgelaELLQELEELKAELRELAEE 491
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1528-2105 |
2.23e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1528 AANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQmsfaenvskleeSLKQEHGTVLQL 1607
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAAL------------RLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1608 QQDAERLRKQQedaenareeaerelekwrqKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADR--EAKKRSKAEESAL 1685
Cdd:COG4913 294 EAELEELRAEL-------------------ARLEAELERLEARLDALREELDELEAQIRGNGGDRleQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRdmaENELERQRRLAESTAQQKLAAEQELIRLRADF----DNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSkv 1761
Cdd:COG4913 355 EER---ERRRARLEALLAALGLPLPASAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1762 rsemdiliQLKSRAeketmSNtekskqlLEAEATKLRDLAEEA-----SKLRAIAEEAkhqrQLAEEDAARQRAeAERIL 1836
Cdd:COG4913 430 --------SLERRK-----SN-------IPARLLALRDALAEAlgldeAELPFVGELI----EVRPEEERWRGA-IERVL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1837 ----------KEKLAAIS---DATRLKTEAEIaLKEKEAENERLRRQAEDEAYQRKI--------------LEDQANQHK 1889
Cdd:COG4913 485 ggfaltllvpPEHYAAALrwvNRLHLRGRLVY-ERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawleaeLGRRFDYVC 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1890 LEIEEKI----------VLLKKSSDA-EMERQKAIVD------DTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKL 1952
Cdd:COG4913 564 VDSPEELrrhpraitraGQVKGNGTRhEKDDRRRIRSryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1953 KNIAEETQQSKLRAEEE------AEKLRRlvLEEEMRR-KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQ 2025
Cdd:COG4913 644 QERREALQRLAEYSWDEidvasaEREIAE--LEAELERlDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2026 KEEADKEAEKQIVAAQQAAlkcNMAEQQVQSVLAQQKEDSMMQNKLKeeyEKAKALARDAEAAKERAEREAALLRQQAEE 2105
Cdd:COG4913 722 LEQAEEELDELQDRLEAAE---DLARLELRALLEERFAAALGDAVER---ELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1780-2557 |
2.44e-10 |
|
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: 67.28 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1780 MSNTEKSKQLLEAEATKLRDLAEEASKLraIAEEAKHQRqLAEEDAarQRAEAERILKEKLAAISDATRLKTEAeIALKE 1859
Cdd:COG3096 274 MRHANERRELSERALELRRELFGARRQL--AEEQYRLVE-MARELE--ELSARESDLEQDYQAASDHLNLVQTA-LRQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1860 K--------EAENERLRRQA---EDEAYQRKILEDQANQHKLEIEEKivllkKSSDAEmeRQKAIvdDTLkQRRVVEEEI 1928
Cdd:COG3096 348 KieryqedlEELTERLEEQEevvEEAAEQLAEAEARLEAAEEEVDSL-----KSQLAD--YQQAL--DVQ-QTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1929 RILKLNFEKASSGKLDLELElnklkNIAEETQQskLRAEEEAEKLRRLVLEEEMRRKEAedkvkkiaaaeeeAARQRKAA 2008
Cdd:COG3096 418 AVQALEKARALCGLPDLTPE-----NAEDYLAA--FRAKEQQATEEVLELEQKLSVADA-------------ARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2009 qeeLDRLQKKADEV-RKQKEEADKEA-----EKQIVAAQQAALKCNMAE-----QQVQSVLAQQKEDSMMQNK------- 2070
Cdd:COG3096 478 ---YELVCKIAGEVeRSQAWQTARELlrryrSQQALAQRLQQLRAQLAEleqrlRQQQNAERLLEEFCQRIGQqldaaee 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2071 LKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRK--DAEFEAAklaqaeaaa 2148
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREqsGEALADS--------- 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2149 lkqkQQADEEMakhkklaEQTLKQKFQVEQELTKVKLQLEETDKQKSLL-------DDELQRLKDE-------------- 2207
Cdd:COG3096 626 ----QEVTAAM-------QQLLEREREATVERDELAARKQALESQIERLsqpggaeDPRLLALAERlggvllseiyddvt 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2208 VDDA---------MRQkASVEEELFKVKIQM---------------------------EELMKLKVRIEEENQ------- 2244
Cdd:COG3096 695 LEDApyfsalygpARH-AIVVPDLSAVKEQLagledcpedlyliegdpdsfddsvfdaEELEDAVVVKLSDRQwrysrfp 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2245 ---RLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLA-----EKMLKEKMQAIQEASR 2316
Cdd:COG3096 774 evpLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELER 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2317 LKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEYQRSLEAERK--------RQLEIIAEA- 2374
Cdd:COG3096 851 ELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREELDAAQEAQAFiqqhgkalAQLEPLVAVl 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2375 -------EKLKLQVSQLSeaqAKAEEEAKKFKKQADTIAARLHeteiatkeqmtevkkmefekLNTSKEADDLRKAITEL 2447
Cdd:COG3096 930 qsdpeqfEQLQADYLQAK---EQQRRLKQQIFALSEVVQRRPH--------------------FSYEDAVGLLGENSDLN 986
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2448 EKEKARLkKEAEEHQNKSKEMADAQQKQIE---REMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEeikKAKALKD 2524
Cdd:COG3096 987 EKLRARL-EQAEEARREAREQLRQAQAQYSqynQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE---RARIRRD 1062
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1655274923 2525 E------QDRQRQ-QMEEEKLKLKATMDAALNKQKEAEKD 2557
Cdd:COG3096 1063 ElheelsQNRSRRsQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1343-1896 |
2.62e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEKlkAEEQKKMaemqaeLDKQKQLAEAHAKAIAKAEkEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLE 1422
Cdd:COG4913 235 DDLERAHEALED--AREQIEL------LEPIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLELLEAELEELRAELA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1423 LHElknlseQQIKDKSQQVDEALKSRLRIEEEIhliriqlettvkqKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRK 1502
Cdd:COG4913 306 RLE------AELERLEARLDALREELDELEAQI-------------RGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1503 QVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIqvahvaaqqsaaAELRSK 1582
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI------------ASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1583 QMSFAENVSKLEESLKQEHGT----------VLQLQQDAERlrkqqedaenareeaerelekWRQKANEAL---RLRLQA 1649
Cdd:COG4913 435 KSNIPARLLALRDALAEALGLdeaelpfvgeLIEVRPEEER---------------------WRGAIERVLggfALTLLV 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1650 EEEAHKKSL-------AQEEAEKQKEEADREAKKRSKAEESALKQR-DMAENELER--QRRLAESTAQQKLAAEQEL--- 1716
Cdd:COG4913 494 PPEHYAAALrwvnrlhLRGRLVYERVRTGLPDPERPRLDPDSLAGKlDFKPHPFRAwlEAELGRRFDYVCVDSPEELrrh 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1717 ----------------------IRLRAD----FDNAEQqRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQ 1770
Cdd:COG4913 574 praitragqvkgngtrhekddrRRIRSRyvlgFDNRAK-LAALEAELAELEEELAEAEERLEALEAELDALQERREALQR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1771 LKSRAEKE--------TMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR---QRAEAERILKEK 1839
Cdd:COG4913 653 LAEYSWDEidvasaerEIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDEL 732
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 1840 LAAISDATRLKTEAEIALKEK--EAENERLRRQAEDEAYQRKI--LEDQANQHKLEIEEKI 1896
Cdd:COG4913 733 QDRLEAAEDLARLELRALLEErfAAALGDAVERELRENLEERIdaLRARLNRAEEELERAM 793
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3451-3489 |
2.87e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.87e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3451 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVAKTL 3489
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1777-2110 |
2.98e-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: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1777 KETMSNTEKSKQLLEAEATKLRDLAEEasklraIAEEAKHQRQLAEEDAARQrAEAERilkeKLAAISDATRLKTEAE-- 1854
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEE------KAREVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAMEREre 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1855 ---IALKEKEAENERLRRQaedeayqrkiledqanqhklEIEEKIVLLKKSSDAEMERQKaivddtlKQRRVVEE--EIR 1929
Cdd:pfam17380 350 lerIRQEERKRELERIRQE--------------------EIAMEISRMRELERLQMERQQ-------KNERVRQEleAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1930 ILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLR--AEEEAEKLRRLVLEEE--------MRRKEAEDKVKKIAAAEE 1999
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRrlEEERAREMERVRLEEQerqqqverLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2000 EaaRQRKAAQEELDRLQKKADEVRKQK----EEADKEAEKQIVAAQQAalkcnMAEQQvqsvlaQQKEDSMMQNKLKEEY 2075
Cdd:pfam17380 483 K--RDRKRAEEQRRKILEKELEERKQAmieeERKRKLLEKEMEERQKA-----IYEEE------RRREAEEERRKQQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1655274923 2076 EKAKALARDAEAAKERA-----EREAALLRQQAEEAERQK 2110
Cdd:pfam17380 550 ERRRIQEQMRKATEERSrleamEREREMMRQIVESEKARA 589
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3784-3821 |
3.93e-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: 3.93e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 3784 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKETNEKL 3821
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1714-2371 |
4.49e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1714 QELIRLRADFDNAEQQRSLLEdELYRLKNEVIAAQQERKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAE 1793
Cdd:COG4913 235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFA---QRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1794 atkLRDLAEEASKLRAIAEEAKHQRQLA----EEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRR 1869
Cdd:COG4913 311 ---LERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1870 QAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdaemerqkaivddtlkQRRVVEEEIRILKlnfekasSGKLDLELEL 1949
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRR------------------ELRELEAEIASLE-------RRKSNIPARL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1950 NKLKN-IAEETQQSK-----------LRAEEE-----AEKL-----RRLVLEEEmrrkeAEDKVKKIAAAEEEAARQRka 2007
Cdd:COG4913 443 LALRDaLAEALGLDEaelpfvgelieVRPEEErwrgaIERVlggfaLTLLVPPE-----HYAAALRWVNRLHLRGRLV-- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2008 aqeeLDRLQKKADEVRKQKEEADKEAEK-------------QIVAAQQAALKCNMAEQ------------QV-QSVLAQQ 2061
Cdd:COG4913 516 ----YERVRTGLPDPERPRLDPDSLAGKldfkphpfrawleAELGRRFDYVCVDSPEElrrhpraitragQVkGNGTRHE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2062 KEDsmmQNKLKEEYekakALARDAEAAKERAEREAALLRQQAEEAERQkvaaeqeaanQAKAQDDAERLRKdaefeaakl 2141
Cdd:COG4913 592 KDD---RRRIRSRY----VLGFDNRAKLAALEAELAELEEELAEAEER----------LEALEAELDALQE--------- 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2142 aqaeaaalkqkqqadeemakhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLD---DELQRLKDEVDDAMRQKASV 2218
Cdd:COG4913 646 ---------------------RREALQRLAEYSWDEIDVASAEREIAELEAELERLDassDDLAALEEQLEELEAELEEL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2219 EEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmkkLAEDAARLSIEAQEAARLRQIAE--DDLNQQ 2296
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALGDAVERELRENLEEriDALRAR 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2297 RTLAEKMLKEKMQAIQ-----EASRLKAEAE-------MLQRQK--DLAqEQAQKLledKQLMQQRLDEETEEYQRSLEA 2362
Cdd:COG4913 782 LNRAEEELERAMRAFNrewpaETADLDADLEslpeylaLLDRLEedGLP-EYEERF---KELLNENSIEFVADLLSKLRR 857
|
730
....*....|..
gi 1655274923 2363 ER---KRQLEII 2371
Cdd:COG4913 858 AIreiKERIDPL 869
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
47-143 |
5.05e-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: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 47 KKTFTKWVNKHLIKSQ---------RHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDFL 112
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1655274923 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1672-2384 |
6.68e-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: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAA-EQELIRLRADFDNAEQQRSLLEDELYRLKNEVI---AA 1747
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDElNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaAA 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1748 QQER-KQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRD----LAEEASKLRAIAEEA-------- 1814
Cdd:pfam12128 345 DQEQlPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDklakIREARDRQLAVAEDDlqalesel 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1815 --KHQRQLAE-EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERL------RRQAEDEAYQRKILEDQA 1885
Cdd:pfam12128 425 reQLEAGKLEfNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQeaanaeVERLQSELRQARKRRDQA 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1886 NQHkLEIEEKIVLLKKSSDAEMERQKAIVDDTL-----KQRRVVEEEIRILklnFEKASSGKLDLELELNKLKNIAEETQ 1960
Cdd:pfam12128 505 SEA-LRQASRRLEERQSALDELELQLFPQAGTLlhflrKEAPDWEQSIGKV---ISPELLHRTDLDPEVWDGSVGGELNL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1961 QSKLRAEEEAEKLRRLVLEEEMRRK--EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIV 2038
Cdd:pfam12128 581 YGVKLDLKRIDVPEWAASEEELRERldKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2039 AAQQAALKCNMAEQQVQsvlaQQKEDSMmqNKLKEEyekAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAA 2118
Cdd:pfam12128 661 EKQSEKDKKNKALAERK----DSANERL--NSLEAQ---LKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2119 NQAKAQDDAERLRKDAEFEAAKLAQAEAAALK-QKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQksll 2197
Cdd:pfam12128 732 ALLKAAIAARRSGAKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQ---- 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2198 ddELQRLKDevddamrQKASVEEELFKVKIQmeeLMKLKVRIEEENQRLMKKDKDNtQKFLVEEAENMKKLAEDAARLsi 2277
Cdd:pfam12128 808 --RRPRLAT-------QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKAS-EKQQVRLSENLRGLRCEMSKL-- 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2278 eaqeaARLRQIAEDDlnqqrtlaekmlkekmQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLED-----KQLMQQRLDEE 2352
Cdd:pfam12128 873 -----ATLKEDANSE----------------QAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHfknviADHSGSGLAET 931
|
730 740 750
....*....|....*....|....*....|..
gi 1655274923 2353 TEEYQRSLEAERKRQLEIIAEAEKLKlQVSQL 2384
Cdd:pfam12128 932 WESLREEDHYQNDKGIRLLDYRKLVP-YLEQW 962
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1081-1561 |
7.50e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1081 LSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAV 1160
Cdd:PRK03918 212 ISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1161 SDKMSRVHSERDAELDQHRQ---HLSSLQDRWKAVFTQIDLRQ---RELDQLGRQLGYYRESYDWLIRWI---ADAKQRQ 1231
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREiekRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHelyEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1232 ENIQAVpitDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLvayKAQVEPLTS-----PLKKTKL 1306
Cdd:PRK03918 372 EELERL---KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL---KKAIEELKKakgkcPVCGREL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1307 DSasdniiQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEE-----QKKMAEMQAELdkQKQLAEAHA 1381
Cdd:PRK03918 446 TE------EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEselikLKELAEQLKEL--EEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1382 KAIAKAEKEAQELKLRM------QEEVSKRETAAVDAEKQKQNIQLELHEL-KNLSE--QQIKDKSQQVDEALKSRLRIE 1452
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLiklkgeIKSLKKELEKLEELKKKLAELEKKLDELeEELAEllKELEELGFESVEELEERLKEL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1453 EEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEetQKKRLAEEELKHKSEAERKAANEK 1532
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE--LEKKYSEEEYEELREEYLELSREL 675
|
490 500
....*....|....*....|....*....
gi 1655274923 1533 QKALEDLENLRMQAEEAERQVKQAEVEKE 1561
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1134-1937 |
7.91e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1134 KKMRAEAEAEQpVFDSLEEELKKASAVSDKMSRVHSERDaELDQHRQHLSSLQD--------RWKAVFTQIDLRQRELDQ 1205
Cdd:TIGR02169 171 KKEKALEELEE-VEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREyegyellkEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1206 LGRQLGYYRESYDWLIRWIADAKQRQENIQAVpiTDSKTLKEQLAKEKKLLE---EIEKNKDKVDECQKYAKAYIDIIKD 1282
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKK--IKDLGEEEQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1283 YELQLVAYKAQVEPLTSPLKKTKLDSASdnIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAE---- 1358
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDK--LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREinel 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1359 --EQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELK---NLSEQQ 1433
Cdd:TIGR02169 405 krELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKeeyDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1434 IKDKSQQVDEALKSRLRIEEE-----------------IH-----LIRIQLETTVKQKSNAEDELKQL--RDRADAAEKL 1489
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERvrggraveevlkasiqgVHgtvaqLGSVGERYATAIEVAAGNRLNNVvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1490 RKLAQEEAEK-----LRKQVSEETQKKRLAEEELKHKS----EAERKAANEKQKALED---LENLrmqaEEAERQVKQAE 1557
Cdd:TIGR02169 565 ELLKRRKAGRatflpLNKMRDERRDLSILSEDGVIGFAvdlvEFDPKYEPAFKYVFGDtlvVEDI----EAARRLMGKYR 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1558 --------VEKERQIQVAHVAAQ--QSAAAELRSKQMSFAENVSKLEESLKQehgtvlqLQQDAERLRKQQEDAENAREE 1627
Cdd:TIGR02169 641 mvtlegelFEKSGAMTGGSRAPRggILFSRSEPAELQRLRERLEGLKRELSS-------LQSELRRIENRLDELSQELSD 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1628 AERELEKWRQKANealrlRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAE--------ESALKQRDMAENELErqR 1699
Cdd:TIGR02169 714 ASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElearieelEEDLHKLEEALNDLE--A 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1700 RLAESTAQQKLAAEQELirlradfdnaEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM-DILIQLKSRAEKE 1778
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKL----------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRiDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1779 TMSNTEKSKQLLEAEATK--LRDLAEEASKLRaiAEEAKHQRQLAEEDAARQRAEAERILKEKLAAisdatRLKTEAEiA 1856
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEaaLRDLESRLGDLK--KERDELEAQLRELERKIEELEAQIEKKRKRLS-----ELKAKLE-A 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1857 LKEKEAENERLRRQAEDEAYQRKILEDQAnQHKLEIEEKIVLLKKSSDA---EMERQKAIVDDTLKQRRVVEEEIRILKL 1933
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQ-AELQRVEEEIRALEPVNMLaiqEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....
gi 1655274923 1934 NFEK 1937
Cdd:TIGR02169 1008 RIEE 1011
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-146 |
8.86e-10 |
|
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: 59.14 E-value: 8.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 47 KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLP----REKGRMRFHKLQNVQIALDFLRHRQVKLVNI 122
Cdd:cd21222 18 KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMEDAGISTPKI 97
|
90 100
....*....|....*....|....
gi 1655274923 123 RNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21222 98 RPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1377-1617 |
8.99e-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: 64.01 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1377 AEAHAKAIAKAEKEAQELKLRMQEEVSKREtaavDAEKQKQNIQLELHELknlsEQQIKDKSQQVDEalksrlrIEEEIH 1456
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1457 LIRIQLETTVKQKSNAEDELKQLRDR-ADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEeLKHKSEAERKAANEKQKA 1535
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1536 LEDLENLRmqaeeaerqvkqAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLR 1615
Cdd:COG4942 159 LAELAALR------------AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
..
gi 1655274923 1616 KQ 1617
Cdd:COG4942 227 AL 228
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1672-2599 |
1.20e-09 |
|
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: 64.97 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALkqrdmaenELERQRRlaesTAQQKLAAEQE-LIRLRADFDNAEQQRSLLEDElYRLKNEVIAAQQE 1750
Cdd:COG3096 275 RHANERRELSERAL--------ELRRELF----GARRQLAEEQYrLVEMARELEELSARESDLEQD-YQAASDHLNLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1751 RKQLEDELSKVRSEMDiliQLKSRAEKETMSNTEKSKQLLEAEATKLRdlAEEASKlRAIAEEAKHQRQLaeeDAARQRA 1830
Cdd:COG3096 342 ALRQQEKIERYQEDLE---ELTERLEEQEEVVEEAAEQLAEAEARLEA--AEEEVD-SLKSQLADYQQAL---DVQQTRA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1831 EAERilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSDaEM 1907
Cdd:COG3096 413 IQYQ---QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKlsvADAARRQFEKAYELVCKIAG-EV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ERQKAivDDTLKQrrvVEEEIRILKLNFEKASSGKLDL-ELE-----LNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEE 1981
Cdd:COG3096 489 ERSQA--WQTARE---LLRRYRSQQALAQRLQQLRAQLaELEqrlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRkqkeeadkeaekqivAAQQAALKcnMAEQQVQSVLAQQ 2061
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL---------------AAQDALER--LREQSGEALADSQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2062 KEDSMMQNKLKEEYEkAKALARDAEAAKERAEREAALLRQQ--AEEAERQKVAAEQEAANQAKAQDDAerlrkdaefeaa 2139
Cdd:COG3096 627 EVTAAMQQLLERERE-ATVERDELAARKQALESQIERLSQPggAEDPRLLALAERLGGVLLSEIYDDV------------ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2140 klaqaeaaalkqkqqADEEMAKHKKL---AEQTLkqkfqVEQELTKVKLQLEETDkqkSLLDDEL--QRLKDEVDDAMRq 2214
Cdd:COG3096 694 ---------------TLEDAPYFSALygpARHAI-----VVPDLSAVKEQLAGLE---DCPEDLYliEGDPDSFDDSVF- 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2215 kaSVEEELFKVKIQMEELMKLKVRIEEEnQRLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAARLRQIAEDDLN 2294
Cdd:COG3096 750 --DAEELEDAVVVKLSDRQWRYSRFPEV-PLFGRAAREKRLEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2295 QQRTLA-----EKMLKEKMQAIQEASRLKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQQRLDEETEEY 2356
Cdd:COG3096 824 GHLAVAfapdpEAELAALRQRRSELERELAQHRaqeqQLRQQLDQLKEQLQllnkllpqaNLLADETL-ADRLEELREEL 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2357 QRSLEAERK--------RQLEIIAEA--------EKLKLQVSQLSEAQAKAEEEAKKFkkqADTIAARLHeteiatkeqm 2420
Cdd:COG3096 903 DAAQEAQAFiqqhgkalAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAL---SEVVQRRPH---------- 969
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2421 tevkkmefekLNTSKEADDLRKAITELEKEKARLKkEAEEHQNKSKEMADAQQKQIE---REMTVLQQTFLTEKEMLLKK 2497
Cdd:COG3096 970 ----------FSYEDAVGLLGENSDLNEKLRARLE-QAEEARREAREQLRQAQAQYSqynQVLASLKSSRDAKQQTLQEL 1038
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2498 EKLIEDEKKKLESQFEEeikKAKALKDEqdrqrqqmeeeklklkatMDAALNkQKEAEKDILNKQKEMQELERKRLEQEr 2577
Cdd:COG3096 1039 EQELEELGVQADAEAEE---RARIRRDE------------------LHEELS-QNRSRRSQLEKQLTRCEAEMDSLQKR- 1095
|
970 980
....*....|....*....|..
gi 1655274923 2578 vLADENQKLREKLQQMEEAQKS 2599
Cdd:COG3096 1096 -LRKAERDYKQEREQVVQAKAG 1116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1526-1879 |
1.51e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 64.37 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1526 RKAANEKQKAlEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQS--AAAELRSKQMSFAENVSKLEESLKQEhgt 1603
Cdd:pfam17380 281 QKAVSERQQQ-EKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQE--- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1604 vlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAeeeahkkslaqeeaekqkeeadreAKKRSKAEEs 1683
Cdd:pfam17380 357 --ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA------------------------ARKVKILEE- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1684 alkqrdmaenelERQRRLAESTAQ-QKLAAEQELIRlradfdnaEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVR 1762
Cdd:pfam17380 410 ------------ERQRKIQQQKVEmEQIRAEQEEAR--------QREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1763 SEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLA-EEDAARQRAEAER---ILKE 1838
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAiYEEERRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1655274923 1839 KLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1879
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1319-1973 |
1.61e-09 |
|
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: 64.39 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1319 TLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDkqkqlaeahakAIAKAEKEAQElklrm 1398
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----------ALAVAEKAGQA----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1399 qeEVSKRETAAVDAEKQKQNI----QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTvkqksnaed 1474
Cdd:pfam07111 116 --EAEGLRAALAGAEMVRKNLeegsQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETK--------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 elkqlrdRADAAEKLrKLAQEEAEKLRKQVSEetqkkrlAEEELkhkseaerkaanEKQKALedLENLRMQ-AEEAERQV 1553
Cdd:pfam07111 185 -------RAGEAKQL-AEAQKEAELLRKQLSK-------TQEEL------------EAQVTL--VESLRKYvGEQVPPEV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1554 KQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLeeslkqEHGTVLQLQQDAERLRKQQEDAENAREEAERELE 1633
Cdd:pfam07111 236 HSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSL------THMLALQEEELTRKIQPSDSLEPEFPKKCRSLLN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1634 KWRQKANeALRLRLQAEEEAHKKSLaqeeAEKQKEEADREAKKRSKAEESALKQRDM----AENELER-----------Q 1698
Cdd:pfam07111 310 RWREKVF-ALMVQLKAQDLEHRDSV----KQLRGQVAELQEQVTSQSQEQAILQRALqdkaAEVEVERmsakglqmelsR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1699 RRLAESTAQQKLAAEQELIRLRADFDNAEQQRslLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAE-- 1776
Cdd:pfam07111 385 AQEARRRQQQQTASAEEQLKFVVNAMSSTQIW--LETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQlr 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1777 KETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIA 1856
Cdd:pfam07111 463 QESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1857 LKEKEAENERLRRQ--AEDEAYQRKILEDQANQHKLEIEEKIVLL------------KKSSDAEMERQKAIVDDTLKQRR 1922
Cdd:pfam07111 542 SVGQQLEVARQGQQesTEEAASLRQELTQQQEIYGQALQEKVAEVetrlreqlsdtkRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1923 VVEE-----EIRILKLNFEKASSGKLDLEL-ELNKLKNIAEET-QQSKLRAEEEAEKL 1973
Cdd:pfam07111 622 ATQEkernqELRRLQDEARKEEGQRLARRVqELERDKNLMLATlQQEGLLSRYKQQRL 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1588-2064 |
1.61e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1588 ENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKqk 1667
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1668 eeadREAKKRSKAEESALKQRDMAENELER-QRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIA 1746
Cdd:COG4717 149 ----EELEERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1747 AQQERKQLEDELS------KVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQL 1820
Cdd:COG4717 225 LEEELEQLENELEaaaleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1821 AE-EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDeayqrkiLEDQANQHKLEIEEKIVLL 1899
Cdd:COG4717 305 EElQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE-------LEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1900 KKSSDAEMERQKAIvdDTLKQRRVVEEEIRILklnfekassgKLDLELELNKLKNIAEETQQSKLRAEEEaeklrrlvlE 1979
Cdd:COG4717 378 EAGVEDEEELRAAL--EQAEEYQELKEELEEL----------EEQLEELLGELEELLEALDEEELEEELE---------E 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1980 EEMRRKEAEDKVKKIaaaeeeaARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKcnMAEQQVQSVLA 2059
Cdd:COG4717 437 LEEELEELEEELEEL-------REELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALK--LALELLEEARE 507
|
....*
gi 1655274923 2060 QQKED 2064
Cdd:COG4717 508 EYREE 512
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1342-1541 |
1.82e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 63.29 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKaaEKLKAEEQKKMAEMQA--ELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKretAAVDAEKQKQni 1419
Cdd:PRK09510 100 QERLKQLEK--ERLAAQEQKKQAEEAAkqAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKAE-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1420 qlelhelknlSEQQIKDKSqqvdEALKsrlrieeeihliriQLETTVKQKSNAEDELKQlrdRADAAEKLRKLAQEEAEK 1499
Cdd:PRK09510 173 ----------AEAAKKAAA----EAKK--------------KAEAEAAAKAAAEAKKKA---EAEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655274923 1500 LRKQVSE--ETQKKRLAEEELKHKSEAERKAANEkQKALEDLEN 1541
Cdd:PRK09510 222 EAKAAAAkaAAEAKAAAEKAAAAKAAEKAAAAKA-AAEVDDLFG 264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1357-1537 |
2.57e-09 |
|
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: 60.71 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1357 AEEQKKMAEMQA---ELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQ 1433
Cdd:COG1579 3 PEDLRALLDLQEldsELDRLEHRLKELPAELAELEDELAAL----EARLEAAKTELEDLEKEIKRLELEIEEV----EAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1434 IKDKSQQVDEALKSRlrieeEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRL 1513
Cdd:COG1579 75 IKKYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|....
gi 1655274923 1514 AEEELkhksEAERKAANEKQKALE 1537
Cdd:COG1579 150 ELAEL----EAELEELEAEREELA 169
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2156-2605 |
2.58e-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: 63.98 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2156 DEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLL-------DDELQRLKDEVDDAMRQKASVEEELFKVKIQ 2228
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIELLLQQHQDRIEQLIS 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2229 MEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEN-----MKKLAE---DAARLSIEAQEAARLRQIAEDDLNQQRTLA 2300
Cdd:pfam15921 275 EHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNqnsmyMRQLSDlesTVSQLRSELREAKRMYEDKIEELEKQLVLA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKE----KMQAIQEASRL-----KAEAEMLQRQKDLAQEQAQ-------------------KLLEDKQLMQQRLDEE 2352
Cdd:pfam15921 355 NSELTEarteRDQFSQESGNLddqlqKLLADLHKREKELSLEKEQnkrlwdrdtgnsitidhlrRELDDRNMEVQRLEAL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2353 TEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLN 2432
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2433 TSKEADDLRKAITELEKEKARLKKEAEEHQNKSKE-------MADAQQ------KQIEREMTVLQQTFLTEKEMLLKK-- 2497
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEcealklqMAEKDKvieilrQQIENMTQLVGQHGRTAGAMQVEKaq 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2498 -EKLIEDEKKklesqfeeEIKKAKALKDEQDRQRQQMEE-------EKLKL--------------KATMDAALNKQKEAE 2555
Cdd:pfam15921 595 lEKEINDRRL--------ELQEFKILKDKKDAKIRELEArvsdlelEKVKLvnagserlravkdiKQERDQLLNEVKTSR 666
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2556 KDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLITEK 2605
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4371-4409 |
3.28e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 3.28e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 4371 FLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTAQKL 4409
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1950-2134 |
4.06e-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: 61.79 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1950 NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaeeeaarQRKAAQEEldrlQKKADEVRKQKEEA 2029
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELE---------------QRAAAEKA----AKQAEQAAKQAEEK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2030 DKEAE--KQIVAAQQAALKCNMAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKALARDAEA-----AKERAEREAallRQQ 2102
Cdd:TIGR02794 118 QKQAEeaKAKQAAEAKAKAEAEAERKAKEEAAKQAE----EEAKAKAAAEAKKKAEEAKKkaeaeAKAKAEAEA---KAK 190
|
170 180 190
....*....|....*....|....*....|..
gi 1655274923 2103 AEEAERQKVAAEQEAANQAKAQDDAERLRKDA 2134
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3120-3158 |
5.19e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 54.26 E-value: 5.19e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3120 LLDAQMTTGGIIDPVKSHRVPHDVACNRSYFDDEMKQHL 3158
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
967-1614 |
5.97e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 967 DSLLRSMEKGQQDETLCKNYISEVKDLRLRIEDceartvarirKPVEKEPLKECIQKT-AEQAKVQVELEGLKKDLDKVS 1045
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEE----------ERKRRDKLTEEYAELkEELEDLRAELEEVDKEFAETR 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1046 TKTQDilnspqpsatapvLRSELELTVQKMDHAYMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDvkE 1125
Cdd:TIGR02169 385 DELKD-------------YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL--E 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1126 VETYRTNLKKMRAEAEAEQPVFDSLEEELKKasaVSDKMSRVHSERDaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQ 1205
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDR---VEKELSKLQRELA-EAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1206 LGRQLGYYRESYDWLIRWIADAKqrqenIQAVPITDSKTLKE--QLAKEKKL--LEEIEKNKDKVDECQKyAKAYIDIIK 1281
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKMRDERRDL-SILSEDGVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1282 DYELQLVAYKAQVEP-----LTSPLKKTKLDSASDNIIQ-EYVTLRTRYSE---LMTLTSQYIKFITDTQR-------RL 1345
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPafkyvFGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRsepaelqRL 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1346 EDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELK------------LRMQEEVSKRETAAVDAE 1413
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeklkerleeLEEDLSSLEQEIENVKSE 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1414 KQK-----QNIQLELHELK--------NLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR 1480
Cdd:TIGR02169 760 LKEleariEELEEDLHKLEealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1481 DRADAAEKLRKLAQEEAEKLRKQVSE---ETQKKRLAEEELKHKSEAERKaanEKQKALEDLENLRMQAEEAERQVKQAE 1557
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEEleeELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELEAQIEKKR 916
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1558 VEKERQIQVAHVAAQQSAAAELRSKQMsfaENVSKLEESLKQEHGTVLQLQQDAERL 1614
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGED---EEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1952-2355 |
6.02e-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: 62.22 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1952 LKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKkiaaaeeeaaRQRKAAQEELDRLQKkadEVRKQKEEADK 2031
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE----------RQRRELESRVAELKE---ELRQSREKHEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2032 EAEKQivaAQQAALKCNMAEQQvqSVLAQQKEDSmmQNKLKEEYEKAKALARDA-------EAAKERAEREAALLRQqaE 2104
Cdd:pfam07888 99 LEEKY---KELSASSEELSEEK--DALLAQRAAH--EARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKE--E 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2105 EAERQKVAAEQEaanqakaQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKklaeqtLKQKFQVEQELTKVK 2184
Cdd:pfam07888 170 EAERKQLQAKLQ-------QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK------LTTAHRKEAENEALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2185 LQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEEL------MKLKVRieeENQRLMKKDKDNTQKFL 2258
Cdd:pfam07888 237 EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2259 VEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRQKDLAQEQAQKL 2338
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQEL 390
|
410
....*....|....*..
gi 1655274923 2339 LEDKQLMQQRLDEETEE 2355
Cdd:pfam07888 391 LEYIRQLEQRLETVADA 407
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2005-2488 |
6.14e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2005 RKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL--A 2082
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2083 RDAEAAKERAEREAALLRQQAEEAERQkvaaeqeAANQAKAQDDAERLRKDAEfeaaklaqaeaaalkqkqqadeemAKH 2162
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEER-------LEELRELEEELEELEAELA------------------------ELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2163 KKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQmEELMKLKVRIEEE 2242
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2243 NQRLMKKDKDNTQKFLVEE---------------AENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQR-------TLA 2300
Cdd:COG4717 256 AALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalglppDLS 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKlledKQLMQQRLDEETEEYQRSLEAERKRQlEIIAEAEKLKLQ 2380
Cdd:COG4717 336 PEELLELLDRIEELQELLREAEELEEELQLEELEQEI----AALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2381 VSQLseaqaKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFE------KLNTSKEADDLRKAITELEKEKARL 2454
Cdd:COG4717 411 LEEL-----LGELEELLEALDEEELEEELEELEEELEELEEELEELREElaeleaELEQLEEDGELAELLQELEELKAEL 485
|
490 500 510
....*....|....*....|....*....|....
gi 1655274923 2455 KKEAEEHQNkskemADAQQKQIEREMTVLQQTFL 2488
Cdd:COG4717 486 RELAEEWAA-----LKLALELLEEAREEYREERL 514
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4293-4330 |
6.62e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 6.62e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 4293 QRLLEAQACTGGIIDPTTGERFTVTVATEKGLVDKAMV 4330
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1339-1556 |
9.98e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1339 TDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELklrmQEEVSKRETAAVDAEKQKQN 1418
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1419 IQLELHELKNLSEQQIKD--------------KSQQVDEALKsRLRIEEEIHLIRIQLETTVKQKSnaeDELKQLRDRAD 1484
Cdd:COG4942 95 LRAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVR-RLQYLKYLAPARREQAEELRADL---AELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 1485 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENL--RMQAEEAERQVKQA 1556
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTP 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1328-1880 |
1.13e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.78 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1328 MTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQK-KMAEMQAELDKQKQlAEAHAKAIAKAEKEAQELKLRMQEEVSKRE 1406
Cdd:pfam12128 356 LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIRE-ARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1407 taavdAEKQKQNIQLELHELKNLSEQQikdksqQVDEALKSRLRI-EEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD- 1484
Cdd:pfam12128 435 -----FNEEEYRLKSRLGELKLRLNQA------TATPELLLQLENfDERIERAREEQEAANAEVERLQSELRQARKRRDq 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1485 AAEKLR---------KLAQEEAEK------------LRKQVSEETQK-KRLAEEELKHKSEAERKAANEKQKALEDLE-- 1540
Cdd:pfam12128 504 ASEALRqasrrleerQSALDELELqlfpqagtllhfLRKEAPDWEQSiGKVISPELLHRTDLDPEVWDGSVGGELNLYgv 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1541 NLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAEnvSKLEESLKQEHGTVLQLQQDAERLRKQQED 1620
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN--GELEKASREETFARTALKNARLDLRRLFDE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1621 AENAREEAERELEKWRQKANEALRlRLQAEEEAHKKSLAQEEaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRR 1700
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLN-SLEAQLKQLDKKHQAWL----------EEQKEQKREARTEKQAYWQVVEGALDAQ 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1701 LA---ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQ---LKSR 1774
Cdd:pfam12128 731 LAllkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlQRRP 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1775 AEKETMSNTEKSKQLLEAEATKLrdlaEEASKLRaiaeEAKHQRQLAEEDAARQRAEAE----RILKEKLAAIS-DATRL 1849
Cdd:pfam12128 811 RLATQLSNIERAISELQQQLARL----IADTKLR----RAKLEMERKASEKQQVRLSENlrglRCEMSKLATLKeDANSE 882
|
570 580 590
....*....|....*....|....*....|.
gi 1655274923 1850 KTEAEIALKEKEAENERLRRQAEDEAYQRKI 1880
Cdd:pfam12128 883 QAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
48-142 |
1.14e-08 |
|
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: 55.81 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 48 KTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTL------PREKGRMrfhkLQNVQIALDFLRHRQVKL 119
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1655274923 120 VNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1355-1557 |
1.15e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.04 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1355 LKAEEQKKMAEMQAELDKQKQLAEAHA-KAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQ--KQNIQLELHELKNLSE 1431
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAkkKAEERREAETARAEAE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1432 QQIKDKSQQVDEAlksrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRD---RADaAEKLRKLAQEEAEKlrkqvsEET 1508
Cdd:COG2268 266 AAYEIAEANAERE------VQRQLEIAEREREIELQEKEAEREEAELEADvrkPAE-AEKQAAEAEAEAEA------EAI 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655274923 1509 QKKRLAEEELKhksEAERKAANEKQKALEDLENLRMQAEEAERQVKQAE 1557
Cdd:COG2268 333 RAKGLAEAEGK---RALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1960-2134 |
1.22e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1960 QQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaeeeaaRQRKAAQEEldrlQKKADEVRKQKEEADKEAEKQIVA 2039
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLE--------------KERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2040 AQQAALKCNMAEQQVQSVLAQQKEDSmmqnklKEEYEKAKALARDAEAAKERAEREAAllrQQAEEAERQKVAAEQEAAN 2119
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAE------AKKKAEAEAAKKAAAEAKKKAEAEAA---AKAAAEAKKKAEAEAKKKA 211
|
170
....*....|....*
gi 1655274923 2120 QAKAQDDAERLRKDA 2134
Cdd:PRK09510 212 AAEAKKKAAAEAKAA 226
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1349-1577 |
1.45e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.24 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1349 EKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKREtaavdAEKQKQNIQLELHELKN 1428
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1429 LSEQQIKDKSQQvDEALKSRLRIEEEIHliriQLETTVKQKSNAEDELKQLRDRADAAEKlrklAQEEAEKLRKQVSEET 1508
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEEAAK----QAEEEAKAKAAAEAKKKAEEAKKKAEAE----AKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1509 QKKRLAEEElKHKSEAERKAANEKQKAledlenlrmQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAA 1577
Cdd:TIGR02794 195 KAKAEAAKA-KAAAEAAAKAEAEAAAA---------AAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-145 |
1.63e-08 |
|
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: 55.59 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVLSGDTLPREKG-----RMRFHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21299 5 EERCFRLWINSLGIDT--YVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILH 145
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1134-1615 |
2.46e-08 |
|
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: 60.52 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1134 KKMRAEAEAEQPVFDSLEEELKKASavsdkmsrvhsERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYY 1213
Cdd:pfam05557 69 EALREQAELNRLKKKYLEALNKKLN-----------EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1214 RESYDWLIRWIADAKQRQENIQAvpitDSKTLKEQLAKEKKLLEEIEKNKDkvdecqkyakaYIDIIKDYELQLvaykAQ 1293
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEK----QQSSLAEAEQRIKELEFEIQSQEQ-----------DSEIVKNSKSEL----AR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1294 VEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSElmtltsqyikfitDTQRRLEDEEKAAEKLKAEEQKKmAEMQAELDKQ 1373
Cdd:pfam05557 199 IPELEKELERLREHNKHLNENIENKLLLKEEVE-------------DLKRKLEREEKYREEAATLELEK-EKLEQELQSW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1374 KQLAEAHAKAIAKAEKEAQELKLRMQEEV--SKRETAAVDAEKQKQNIQLELHE-----LKNLSEQQIKDKSQqvdEALK 1446
Cdd:pfam05557 265 VKLAQDTGLNLRSPEDLSRRIEQLQQREIvlKEENSSLTSSARQLEKARRELEQelaqyLKKIEDLNKKLKRH---KALV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1447 SRLR-----IEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAE-KLRKQVSEET---QKKRLAEEE 1517
Cdd:pfam05557 342 RRLQrrvllLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEmEAQLSVAEEElggYKQQAQTLE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1518 LKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEK-ERQIQVAHVAAQQSAAAElRSKQMSFAEN-VSKLEE 1595
Cdd:pfam05557 422 RELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKnELEMELERRCLQGDYDPK-KTKVLHLSMNpAAEAYQ 500
|
490 500
....*....|....*....|
gi 1655274923 1596 SLKQEHGtvlQLQQDAERLR 1615
Cdd:pfam05557 501 QRKNQLE---KLQAEIERLK 517
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1976-2168 |
2.49e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.47 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1976 LVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEEldrlQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQ 2055
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK----QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2056 SVLAQQKEDsmmqNKLKEEYEKAKALARDAE--AAKERAEREAALLRQQAEEAERQKvaaeqeaANQAKAQDDAERLRKD 2133
Cdd:TIGR02794 123 EAKAKQAAE----AKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKA-------EAEAKAKAEAEAKAKA 191
|
170 180 190
....*....|....*....|....*....|....*
gi 1655274923 2134 AEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQ 2168
Cdd:TIGR02794 192 EEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAE 226
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
156-258 |
2.84e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 54.79 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 156 QSEDMSAKEKLLLWSQ-RMTDgyqgIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLG 233
Cdd:cd21315 11 DGKGPTPKQRLLGWIQsKVPD----LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLD 86
|
90 100
....*....|....*....|....*
gi 1655274923 234 VTRLLDPEDVDVPHPDEKSIITYVS 258
Cdd:cd21315 87 VPQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1467-1709 |
3.45e-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: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1467 KQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKhKSEAERKAANEKqkaledLENLRMQA 1546
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAE------LAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1547 EEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSkqmsfAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENARE 1626
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLS-----PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1627 EAERELEKWRQ--KANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAES 1704
Cdd:COG4942 168 ELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*
gi 1655274923 1705 TAQQK 1709
Cdd:COG4942 248 FAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1348-1585 |
3.62e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1348 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAhakaiakaEKEAQELKLRMQEEvskretaavdaEKQKQNIQlelhelk 1427
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQ--------ERLKQLEKERLAAQ-----------EQKKQAEE------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1428 nlSEQQIKDKSQQVDEALKSRLRieeeihliriqlettvKQKSNAEDELKQLRDRA-DAAEKLRKLAQEEAEK-----LR 1501
Cdd:PRK09510 123 --AAKQAALKQKQAEEAAAKAAA----------------AAKAKAEAEAKRAAAAAkKAAAEAKKKAEAEAAKkaaaeAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1502 KQVSEETQKKRLAEEELKHKSEAERKAANE-KQKAledlenlrmqAEEAERQVKQAEVEKERQIQVAhvAAQQSAAAELR 1580
Cdd:PRK09510 185 KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEaKKKA----------AAEAKAAAAKAAAEAKAAAEKA--AAAKAAEKAAA 252
|
....*
gi 1655274923 1581 SKQMS 1585
Cdd:PRK09510 253 AKAAA 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1796-2369 |
3.72e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1796 KLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAE-RILKEKLAAIsDATRLKTEAEIALKEKEAENERLRRQAEDE 1874
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGL-ESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1875 ayqrkILED--QANQHKLEIEEKIVLLKkSSDAEMERQKAIVDDTLKQRRVVEEEIR------ILKLNFEKASSGKL--- 1943
Cdd:PRK02224 242 -----VLEEheERREELETLEAEIEDLR-ETIAETEREREELAEEVRDLRERLEELEeerddlLAEAGLDDADAEAVear 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1944 --DLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE 2021
Cdd:PRK02224 316 reELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2022 VRKQKEEAD-------------------------------KEAEKQIVAAQQ--AALKCNMAEQQVqsvlaqqkEDSMMQ 2068
Cdd:PRK02224 396 LRERFGDAPvdlgnaedfleelreerdelrereaeleatlRTARERVEEAEAllEAGKCPECGQPV--------EGSPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2069 NKLKEEYEKAKALARDAEAAK-ERAEREAALLR-QQAEEAERQkvaaeqeAANQAKAQDDAERLRKDAEFEAAKLAQAEA 2146
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEeEVEEVEERLERaEDLVEAEDR-------IERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2147 AALKQKQQADEEMAKHKKLAEqtlkqkfQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDdamrqkasveeelfkvk 2226
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAA-------EAEEEAEEAREEVAELNSKLAELKERIESLERIRT----------------- 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2227 iQMEELMKLKVRIEEENQRLMKKDKDNTQK--FLVEEAENMKKLAE--DAARLSiEAQEAarlRQIAEDDLNQqrtLAEK 2302
Cdd:PRK02224 597 -LLAAIADAEDEIERLREKREALAELNDERreRLAEKRERKRELEAefDEARIE-EARED---KERAEEYLEQ---VEEK 668
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2303 M--LKEKMQAIQeaSRLKAEAEMLQRQKDLAQEQAQklLEDKQLMQQRLDEETEEYQ---RSLEAE-RKRQLE 2369
Cdd:PRK02224 669 LdeLREERDDLQ--AEIGAVENELEELEELRERREA--LENRVEALEALYDEAEELEsmyGDLRAElRQRNVE 737
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1672-2558 |
5.80e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRdmaeNELERQRRlaestaqqKLAAEQE-LIRLRADFDNAEQQRSLLEDELYRLK---NEVIAA 1747
Cdd:PRK04863 276 RHANERRVHLEEALELR----RELYTSRR--------QLAAEQYrLVEMARELAELNEAESDLEQDYQAASdhlNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1748 QQERKQLEdelskvRSEMDILiQLKSRAEKETMSNTEKSKQLLEAEATKlrDLAEEaSKLRAIAEEAKHQRQLaeeDAAR 1827
Cdd:PRK04863 344 LRQQEKIE------RYQADLE-ELEERLEEQNEVVEEADEQQEENEARA--EAAEE-EVDELKSQLADYQQAL---DVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1828 QRAEAERilkEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQ---ANQHKLEIEEKIVLLKKSSD 1904
Cdd:PRK04863 411 TRAIQYQ---QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKlsvAQAAHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1905 aEMERQKAivDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNK---LKNIAEETQQSKLRAEEEAEKLRRLVLEEE 1981
Cdd:PRK04863 488 -EVSRSEA--WDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 MRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRkqkeeadkeaekqivAAQQAALKcnMAEQQVQSVLAQQ 2061
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL---------------AAQDALAR--LREQSGEEFEDSQ 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2062 KEDSMMQNKLkeEYEKAKALARD-AEAAKERAEREAALLRQ-QAEEAERQKVAaeqeaanqakaqddAER--------LR 2131
Cdd:PRK04863 628 DVTEYMQQLL--ERERELTVERDeLAARKQALDEEIERLSQpGGSEDPRLNAL--------------AERfggvllseIY 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2132 KDAEFeaaklaqaeaaalkqkQQADEEMAKHKKLAEQTlkqkfqVEQELTKVKLQLEETDkqkSLLDD------ELQRLK 2205
Cdd:PRK04863 692 DDVSL----------------EDAPYFSALYGPARHAI------VVPDLSDAAEQLAGLE---DCPEDlyliegDPDSFD 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2206 DEVDDAmrqkasveEELFKVKIQMEELMKLKV-RIEEEnQRLMKKDKDNTQKFLVEEAEnmkKLAEDAARLSIEAQEAAR 2284
Cdd:PRK04863 747 DSVFSV--------EELEKAVVVKIADRQWRYsRFPEV-PLFGRAAREKRIEQLRAERE---ELAERYATLSFDVQKLQR 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2285 LRQIAEDDLNQQRTLA-----EKMLKEKMQAIQEASRLKAEAE----MLQRQKDLAQEQAQ---------KLLEDKQLmQ 2346
Cdd:PRK04863 815 LHQAFSRFIGSHLAVAfeadpEAELRQLNRRRVELERALADHEsqeqQQRSQLEQAKEGLSalnrllprlNLLADETL-A 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2347 QRLDEETEEYQRSLEAERK--------RQLEIIAEA--------EKLKLQVSQLseaQAKAEEEAKKFKKQADTIAARLH 2410
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFvqqhgnalAQLEPIVSVlqsdpeqfEQLKQDYQQA---QQTQRDAKQQAFALTEVVQRRAH 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2411 eteiatkeqmtevkkmefekLNTSKEADDLRKAITELEKEKARLKkEAEEHQNKSKEM---ADAQQKQIEREMTVLQQTF 2487
Cdd:PRK04863 971 --------------------FSYEDAAEMLAKNSDLNEKLRQRLE-QAEQERTRAREQlrqAQAQLAQYNQVLASLKSSY 1029
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2488 LTEKEMLlkKEKLIEDEKKKLESQFEEEIKkAKALKDE-------QDRQRQQMEEEKLKLKATMDAALNKQKEAEKDI 2558
Cdd:PRK04863 1030 DAKRQML--QELKQELQDLGVPADSGAEER-ARARRDElharlsaNRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1857-2592 |
5.83e-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: 59.68 E-value: 5.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1857 LKEKEAENERLR---RQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTL--KQRRVVEEEIRIL 1931
Cdd:TIGR00606 250 LKNRLKEIEHNLskiMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVreKERELVDCQRELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1932 KLNFEKA--SSGKLDLELELNKLKNIAEETQ-QSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKK-IAAAEEEAARQRKA 2007
Cdd:TIGR00606 330 KLNKERRllNQEKTELLVEQGRLQLQADRHQeHIRARDSLIQSLATRLELDGFERGPFSERQIKNfHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2008 AQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ-QKEDSMMQNKLKEEYEKAKALaRDAE 2086
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKElQQLEGSSDRILELDQELRKAE-RELS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2087 AAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAER-LRKDAEFEAAKLAQAEAAALKQKQQADEEMAK---- 2161
Cdd:TIGR00606 489 KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTtTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSllgy 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2162 --HKKLAEQTL----KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDevddamrQKASVEEELFKV-KIQMEE--L 2232
Cdd:TIGR00606 569 fpNKKQLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE-------QLSSYEDKLFDVcGSQDEEsdL 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2233 MKLKVRIEEEN-QRLMKKDKDNTQKFLVEEAENMKK----LAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEK 2307
Cdd:TIGR00606 642 ERLKEEIEKSSkQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2308 MQAIQEasrLKAEAEMLQRQKDLAQEQAQKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEA 2387
Cdd:TIGR00606 722 EKRRDE---MLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2388 QAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNT-SKEADDLRKAITELEKEKARLKKEAEEHQNKSK 2466
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2467 EMADA-QQKQIEREMTVLQQTFLTE--KEMLLKKEKLIEDE--KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLK 2541
Cdd:TIGR00606 875 QIGTNlQRRQQFEEQLVELSTEVQSliREIKDAKEQDSPLEtfLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH 954
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2542 ATMDAALNKQKEAEKDILnKQKEMQelerkrLEQERVLADENQKLREKLQQ 2592
Cdd:TIGR00606 955 GYMKDIENKIQDGKDDYL-KQKETE------LNTVNAQLEECEKHQEKINE 998
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1123-1558 |
7.02e-08 |
|
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: 59.36 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1123 VKEVETYRTNLKKMRAE-AEAEQPVFDSLEEELKKASAVSDKMSRVHSERdaelDQHRQHLSSLQDRWKAVFTQIDLRQR 1201
Cdd:pfam15921 316 MRQLSDLESTVSQLRSElREAKRMYEDKIEELEKQLVLANSELTEARTER----DQFSQESGNLDDQLQKLLADLHKREK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1202 ELDQLGRQLGYYRE-------SYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAK 1274
Cdd:pfam15921 392 ELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1275 AYIDIIKDYELQLVAYKAQVEP-------LTSPLKKTKLDSASDNiiQEYVTLRTRYsELMTLTSQYIKFITDTQRRLED 1347
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESsertvsdLTASLQEKERAIEATN--AEITKLRSRV-DLKLQELQHLKNEGDHLRNVQT 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1348 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAI-------AKAEKEAQELKLRMQE---EVSKRETAAVDAEKQKQ 1417
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAgamqvekAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVS 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1418 NIQLELHELKNLSEQQ---IKDKSQQVDEAL------KSRLR-IEEEIHLIRI-------QLETTVK----QKSNAEDEL 1476
Cdd:pfam15921 629 DLELEKVKLVNAGSERlraVKDIKQERDQLLnevktsRNELNsLSEDYEVLKRnfrnkseEMETTTNklkmQLKSAQSEL 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1477 KQLRDRADAAEKLRKLAQEEAEKLRKQVSEE---------------------TQKKRLAEEELKHKSEAERKAANEKQKA 1535
Cdd:pfam15921 709 EQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgqidalqskiqfleeamtnaNKEKHFLKEEKNKLSQELSTVATEKNKM 788
|
490 500
....*....|....*....|...
gi 1655274923 1536 LEDLENLRMQAEEAERQVKQAEV 1558
Cdd:pfam15921 789 AGELEVLRSQERRLKEKVANMEV 811
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1345-2304 |
8.05e-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: 59.20 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1345 LEDEEKAAEKLKAEEQKKMAEMQAELDKQK----------QLAEAH----AKAIAKAEK--------EAQELKLRMQEEV 1402
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMARELEELSaresdleqdyQAASDHlnlvQTALRQQEKieryqedlEELTERLEEQEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1403 skRETAA---VDAEKQKQNIQLELHELKNlseqQIKDKSQQVDEaLKSRlrieeeihliRIQLETTVKQKSNAEdELKQL 1479
Cdd:COG3096 370 --VEEAAeqlAEAEARLEAAEEEVDSLKS----QLADYQQALDV-QQTR----------AIQYQQAVQALEKAR-ALCGL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1480 RD-RADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEelkhkseaerkAANEKQKALEDLENLrmqaeeaerqvkQAEV 1558
Cdd:COG3096 432 PDlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA-----------ARRQFEKAYELVCKI------------AGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1559 EKERqiqvAHVAAQQsAAAELRSKQMsFAENVSKLEESLKqEHGTVLQLQQDAERLRKQQEDAENareeaerelekwRQK 1638
Cdd:COG3096 489 ERSQ----AWQTARE-LLRRYRSQQA-LAQRLQQLRAQLA-ELEQRLRQQQNAERLLEEFCQRIG------------QQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1639 ANEALRLRLQAEEEAHKKSLAqeeaekqkeeadrEAKKRSKAEESALKQRdmaENELERQRRLAESTAQQKLAAEQELIR 1718
Cdd:COG3096 550 DAAEELEELLAELEAQLEELE-------------EQAAEAVEQRSELRQQ---LEQLRARIKELAARAPAWLAAQDALER 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1719 LRadfdnaEQQRSLLEDelyrlKNEVIAAQQERKQLEDELSKVRSEmdiLIQLKSRAEKETmsnteksKQLLE---AEAT 1795
Cdd:COG3096 614 LR------EQSGEALAD-----SQEVTAAMQQLLEREREATVERDE---LAARKQALESQI-------ERLSQpggAEDP 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1796 KLRDLAE-----------------EASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAIS-------DATRLKT 1851
Cdd:COG3096 673 RLLALAErlggvllseiyddvtleDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfdDSVFDAE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1852 EAEIALKEKEAENE-RLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSdaeMERQKaivddtlkQRRVVEeeiri 1930
Cdd:COG3096 753 ELEDAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKAS---FDVQK--------LQRLHQ----- 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1931 lklNFEKASSGKLDLELELNklkniaeetqqsklrAEEEAEKLRRlvleeemRRKEAEDKVKKIAAAEEEAARQRKAAQE 2010
Cdd:COG3096 817 ---AFSQFVGGHLAVAFAPD---------------PEAELAALRQ-------RRSELERELAQHRAQEQQLRQQLDQLKE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2011 ELDRLQKKADEVRKQKEE--ADK--EAEKQIVAAQQAAL---KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALAR 2083
Cdd:COG3096 872 QLQLLNKLLPQANLLADEtlADRleELREELDAAQEAQAfiqQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQR 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2084 D----AEAAKERAEREAALLRQQAEEaerqkvaaeqeaaNQAKAQDDAERLRKDAEfeaaklaqaeaaalkqkqQADEEM 2159
Cdd:COG3096 952 RlkqqIFALSEVVQRRPHFSYEDAVG-------------LLGENSDLNEKLRARLE------------------QAEEAR 1000
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2160 AKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVE-----EELFKVKIQMEELMK 2234
Cdd:COG3096 1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRrdelhEELSQNRSRRSQLEK 1080
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2235 LKVRIEEE----NQRLMKKDKDNTQkfLVEEAENMKKLAEDAARLSIEAQEAARL--RQIAEDDLNQQRTLAEKML 2304
Cdd:COG3096 1081 QLTRCEAEmdslQKRLRKAERDYKQ--EREQVVQAKAGWCAVLRLARDNDVERRLhrRELAYLSADELRSMSDKAL 1154
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4019-4055 |
8.35e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.94 E-value: 8.35e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 4019 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGFFDEEM 4055
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
161-263 |
8.81e-08 |
|
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: 53.54 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 161 SAKEKLLLWSQRMTdgyQGIRCDNFTTSWRDGKLFNAVIHKNYPRLIDMGKVYRQTN-LENLEQAFNVAEKDLGVTRLLD 239
Cdd:cd21314 11 TPKQRLLGWIQNKV---PQLPITNFNRDWQDGKALGALVDNCAPGLCPDWESWDPNQpVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1655274923 240 PEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1945-2374 |
9.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1945 LELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQK------- 2017
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllpl 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2018 -----KADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMMQNKL--KEEYEKAKALARDAEAAKE 2090
Cdd:COG4717 131 yqeleALEAELAELPERLEELEERLEELRELEEELEELEAELAE-LQEELEELLEQLSLatEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2091 RAEREAALLRQQAEEAERQkvaaEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEM----------- 2159
Cdd:COG4717 210 ELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2160 -----AKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELmk 2234
Cdd:COG4717 286 lallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2235 LKVRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLsieAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEA 2314
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2315 -SRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEA 2374
Cdd:COG4717 441 lEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1543-2032 |
9.36e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1543 RMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAE 1622
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1623 NAREEAEreleKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLA 1702
Cdd:PRK02224 255 TLEAEIE----DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1703 ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDIL--------IQLKSR 1774
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELrerfgdapVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1775 AE-----KETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIA---------EEAKHQRQLAEEDAARQRAEAERilkEKL 1840
Cdd:PRK02224 411 EDfleelREERDELREREAELEATLRTARERVEEAEALLEAGkcpecgqpvEGSPHVETIEEDRERVEELEAEL---EDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1841 AAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivLLKKSSDAEMERQKAIVDDTLKQ 1920
Cdd:PRK02224 488 EEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE---LRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1921 RRVVEEEIRILKLNFEKASsgkLDLELE-LNKLKNIAEETQQSKLRAEEEAEKL---------RRLVLEEEM-RRKEAED 1989
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAE---LKERIEsLERIRTLLAAIADAEDEIERLREKRealaelndeRRERLAEKReRKRELEA 641
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1655274923 1990 KVKKIAAAEEEAARQRkaAQEELDRLQKKADEVRKQKEEADKE 2032
Cdd:PRK02224 642 EFDEARIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAE 682
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1683-1887 |
9.98e-08 |
|
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: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1683 SALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSK-- 1760
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1761 --------VRSEMDILIQLKSRAEkeTMSNTEKSKQLLEAEatklRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEA 1832
Cdd:COG3883 93 ralyrsggSVSYLDVLLGSESFSD--FLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 1833 ERILKEKLAAISDATRLKteAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQ 1887
Cdd:COG3883 167 EAAKAELEAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1715-2478 |
1.00e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 58.70 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1715 ELIRlraDFDNAEQQRS-LLEDELYRlknEVIaaQQERKQLEDELSKVRSemdILIQLKSRAEKETMSNTEKSKQLLEAE 1793
Cdd:pfam12128 123 ELGR---FMKNAGIQRTnLLNTREYR---SII--QNDRTLLGRERVELRS---LARQFALCDSESPLRHIDKIAKAMHSK 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1794 ATKLRDL----AEEASKLRAIAEEAKHQRQ-----LAEEDAARqRAEAERILKEKLAAISDaTRLKTEAEIALKEKEAEN 1864
Cdd:pfam12128 192 EGKFRDVksmiVAILEDDGVVPPKSRLNRQqvehwIRDIQAIA-GIMKIRPEFTKLQQEFN-TLESAELRLSHLHFGYKS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1865 ERLRRQAEDEAYQ--RKILEDQANQHKLEIEEKIVLL---KKSSDAEMERQKAIVDDTLKQRRVVEEE-IRILKLNFEKA 1938
Cdd:pfam12128 270 DETLIASRQEERQetSAELNQLLRTLDDQWKEKRDELngeLSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1939 SSGKLDLElELNKLKNIAEETQQSklrAEEEAEKLRRLVLEEEMRrkEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK 2018
Cdd:pfam12128 350 PSWQSELE-NLEERLKALTGKHQD---VTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESE 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2019 -ADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMqNKLKEEYEKAKALARDA--EAAKERAERE 2095
Cdd:pfam12128 424 lREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERI-ERAREEQEAANAEVERLqsELRQARKRRD 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2096 AALLRQQAEEA---ERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHkklaeqtlkq 2172
Cdd:pfam12128 503 QASEALRQASRrleERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDG---------- 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2173 kfQVEQELT--KVKLQLEETDKQKSL-LDDELQRLKDEVDDAMRQKASVEEElfkvkiQMEELMKLKVRIeeenqrlmkk 2249
Cdd:pfam12128 573 --SVGGELNlyGVKLDLKRIDVPEWAaSEEELRERLDKAEEALQSAREKQAA------AEEQLVQANGEL---------- 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2250 dkDNTQKFLVEEAENMKKLAEDAARLSIEAQeaarlrqiaeddlNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQR-QK 2328
Cdd:pfam12128 635 --EKASREETFARTALKNARLDLRRLFDEKQ-------------SEKDKKNKALAERKDSANERLNSLEAQLKQLDKkHQ 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2329 DLAQEQAQKLLEDKQLMQQrldeeteeYQRSLEAERKRQLEIIAEAeKLKLQVS---QLSEAQAKAEEEAKKFKKQADTI 2405
Cdd:pfam12128 700 AWLEEQKEQKREARTEKQA--------YWQVVEGALDAQLALLKAA-IAARRSGakaELKALETWYKRDLASLGVDPDVI 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2406 AARlhETEIATKEQ------------------MTEVKKMEFEKLNTSKEadDLRKAITELEKEKARLKKEAEEHQNKSKE 2467
Cdd:pfam12128 771 AKL--KREIRTLERkieriavrrqevlryfdwYQETWLQRRPRLATQLS--NIERAISELQQQLARLIADTKLRRAKLEM 846
|
810
....*....|.
gi 1655274923 2468 MADAQQKQIER 2478
Cdd:pfam12128 847 ERKASEKQQVR 857
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1957-2604 |
1.01e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1957 EETQQSKLRAEEEAEKLRRLVLEEEmRRKEAEDKVKKIAAAEEEAARQRkaAQEELDRLQKKADEVRKQKEEADKEAEKQ 2036
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2037 IVAAQQAALKCNMAEQQVQSVLAQQKEDsmmqnkLKEEyekakalARDAEAAKERAEREAALLRQQAEEAErqkvaaeqe 2116
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQ------LERE-------IERLERELEERERRRARLEALLAALG--------- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2117 aANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSL 2196
Cdd:COG4913 373 -LPLPASAEEFAALRAEAA--------------ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2197 LDDELQRLKDEVDDAMRQKasvEEELFKVKiqmeELMklKVRIEEEN-----QRLMkkdkdNTQKF--LVEEAenmkklA 2269
Cdd:COG4913 438 IPARLLALRDALAEALGLD---EAELPFVG----ELI--EVRPEEERwrgaiERVL-----GGFALtlLVPPE------H 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2270 EDAARLSIEA-QEAARLR--QIAEDDLNQQR------TLAEKM-LKE-------KMQAIQEASRLKAEAE---------- 2322
Cdd:COG4913 498 YAAALRWVNRlHLRGRLVyeRVRTGLPDPERprldpdSLAGKLdFKPhpfrawlEAELGRRFDYVCVDSPeelrrhprai 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2323 ----MLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKF 2398
Cdd:COG4913 578 tragQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2399 KKQADTIAArlhETEIATKE-QMTEVKK--MEFEKLNtsKEADDLRKAITELEKEKARLKKEAEEHQnksKEMADAQQkQ 2475
Cdd:COG4913 658 WDEIDVASA---EREIAELEaELERLDAssDDLAALE--EQLEELEAELEELEEELDELKGEIGRLE---KELEQAEE-E 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2476 IEREMTVLQQtfLTEKEMLLKKEKLieDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAE 2555
Cdd:COG4913 729 LDELQDRLEA--AEDLARLELRALL--EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAET 804
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2556 KDILNKQKEMQELER--KRLEQERvLADENQKLREKLQQMEEAQKSTLITE 2604
Cdd:COG4913 805 ADLDADLESLPEYLAllDRLEEDG-LPEYEERFKELLNENSIEFVADLLSK 854
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1672-2130 |
1.19e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 57.99 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQrdMAENELERQRRLA--ESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQ 1749
Cdd:COG5278 82 EEARAEIDELLAELRS--LTADNPEQQARLDelEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1750 ERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQR 1829
Cdd:COG5278 160 LLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1830 AEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMER 1909
Cdd:COG5278 240 LALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1910 QKAIVDDTLKQRRVVEEEIRIlklnfekassgkLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAED 1989
Cdd:COG5278 320 AAAAALAALLALALATALAAA------------AAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEA 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1990 KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQN 2069
Cdd:COG5278 388 VELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2070 KLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERL 2130
Cdd:COG5278 468 LAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASA 528
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1348-1530 |
1.29e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 57.71 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1348 EEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELK 1427
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1428 NlSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQ--LETTVKQKSNAEDELKQlrdRADAAEKLRKLAQEEAEKLRKQVS 1505
Cdd:pfam05262 259 N-LPKPADTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVA 334
|
170 180
....*....|....*....|....*.
gi 1655274923 1506 EETQK-KRLAEEELKHKSEAERKAAN 1530
Cdd:pfam05262 335 EDLQKtKPQVEAQPTSLNEDAIDSSN 360
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1009-1911 |
1.42e-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: 58.13 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1009 RKPVEKEPLKECIQKTAEQAKVQVELEGLKKDLDKVSTKTQDilnspqpsatapvLRSELEltvQKMDHAYmlssvylek 1088
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEK-------------DNSELE---LKMEKVF--------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1089 lktvemvirntQGAEGVLKQYEnclrevHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVH 1168
Cdd:TIGR00606 297 -----------QGTDEQLNDLY------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRH 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1169 SERDAELDQHRQHLSSlqdrwkavftqidlrQRELDQLGRQLGYYREsydwLIRWIADAKQRQENIQAVPITDSKTLKEQ 1248
Cdd:TIGR00606 360 QEHIRARDSLIQSLAT---------------RLELDGFERGPFSERQ----IKNFHTLVIERQEDEAKTAAQLCADLQSK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1249 LAKEKKLLEEIEKNKDKVDECQKYAKAYIDiIKDYELQLVAYKAQvepltsplkktKLDSASDNIIQEYVTLRTRYSELM 1328
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILE-KKQEELKFVIKELQ-----------QLEGSSDRILELDQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1329 TL-TSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLaEAHAKAIAKAEKEAQELKLRMQEEVskreT 1407
Cdd:TIGR00606 489 KAeKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSDEL----T 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1408 AAVDAEKQKQNIQLELHELKNlSEQQIKDKSQQVDEALKSrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAE 1487
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSK-EINQTRDRLAKLNKELAS---LEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1488 KLRKLaQEEAEKLRKQVSEETQKKRLAE---EELKHKSEA-------ERKAANEKQKALEDLENLRMQA----EEAERQV 1553
Cdd:TIGR00606 640 DLERL-KEEIEKSSKQRAMLAGATAVYSqfiTQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLApdklKSTESEL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1554 KQaeVEKERQIQVAHVAAQQS-------AAAELRSKQMSFAENVSKLEESLKQEH---GTVLQLQQDAERLRKQQEDAEN 1623
Cdd:TIGR00606 719 KK--KEKRRDEMLGLAPGRQSiidlkekEIPELRNKLQKVNRDIQRLKNDIEEQEtllGTIMPEEESAKVCLTDVTIMER 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1624 AREEAERELEKWRQKANEA-----------LRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAE 1692
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLqgsdldrtvqqVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1693 NELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQ-QRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQL 1771
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1772 KSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRA-IAEEAKHQRQlaEEDAARQRaeaERILKEKLaaisdaTRLK 1850
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEkINEDMRLMRQ--DIDTQKIQ---ERWLQDNL------TLRK 1025
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 1851 TEAEIalkekeAENERLRRQAEDEAYQRKILEDQANQHKLeiEEKIVLLKKSSDAEMERQK 1911
Cdd:TIGR00606 1026 RENEL------KEVEEELKQHLKEMGQMQVLQMKQEHQKL--EENIDLIKRNHVLALGRQK 1078
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
41-148 |
1.52e-07 |
|
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: 53.47 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEVL-------SGDTLPREKGRMRFHKLQNVQIALDFLR 113
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655274923 114 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 148
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1340-1881 |
1.55e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1340 DTQRRLEdEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIA-----KAEKEAQELKLRMQEEVSKRETAAVDAEK 1414
Cdd:PRK04863 524 ELEQRLR-QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLEslsesVSEARERRMALRQQLEQLQARIQRLAARA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1415 QK-QNIQLELHELKNLSEQQIKDkSQQVDEALKSRLRIEEEIHLIRIQLETTVK----------QKSNAEDE-LKQLRDR 1482
Cdd:PRK04863 603 PAwLAAQDALARLREQSGEEFED-SQDVTEYMQQLLERERELTVERDELAARKQaldeeierlsQPGGSEDPrLNALAER 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1483 -------------------------------------ADAAEKLRKL-------------------AQEEAEKLRKQVSE 1506
Cdd:PRK04863 682 fggvllseiyddvsledapyfsalygparhaivvpdlSDAAEQLAGLedcpedlyliegdpdsfddSVFSVEELEKAVVV 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1507 ETQKK-----RLAEEELKHkseaerKAANEKQkaledLENLRMQAEEAERQVKQA--EVEK-ERQIQV--------AHVA 1570
Cdd:PRK04863 762 KIADRqwrysRFPEVPLFG------RAAREKR-----IEQLRAEREELAERYATLsfDVQKlQRLHQAfsrfigshLAVA 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1571 AQQSAAAELRSKQmsfaENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAE 1650
Cdd:PRK04863 831 FEADPEAELRQLN----RRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIREQLDEA 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1651 EEA------HKKSLAQEEAEKQKEEAD-------REAKKRSKAEESALKQRDMAENELeRQRR--LAESTAQQKLAAEQE 1715
Cdd:PRK04863 907 EEAkrfvqqHGNALAQLEPIVSVLQSDpeqfeqlKQDYQQAQQTQRDAKQQAFALTEV-VQRRahFSYEDAAEMLAKNSD 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1716 L-IRLRADFDNAEQQRSLLEDEL------YRLKNEVI--------AAQQERKQLEDELSK--VRSEMDILIQLKSRAEK- 1777
Cdd:PRK04863 986 LnEKLRQRLEQAEQERTRAREQLrqaqaqLAQYNQVLaslkssydAKRQMLQELKQELQDlgVPADSGAEERARARRDEl 1065
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1778 -ETMSNT-------EKSKQLLEAEAT----KLRDLAEEASKLRAIAEEAKHQRQLAeEDAARQRAEAERILKEKLAAISd 1845
Cdd:PRK04863 1066 hARLSANrsrrnqlEKQLTFCEAEMDnltkKLRKLERDYHEMREQVVNAKAGWCAV-LRLVKDNGVERRLHRRELAYLS- 1143
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1655274923 1846 ATRLKTEAEI---ALKEKEAENERLR---RQAEDEAY-QRKIL 1881
Cdd:PRK04863 1144 ADELRSMSDKalgALRLAVADNEHLRdvlRLSEDPKRpERKVQ 1186
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1148-1881 |
1.84e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1148 DSLEEELKKASAVSDkmsrvhsERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESydwlIRWIADA 1227
Cdd:COG3096 357 EELTERLEEQEEVVE-------EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQA----VQALEKA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1228 KQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKyAKAYIDiiKDYELqlvaykaqVEPLTSPLKKTKLD 1307
Cdd:COG3096 426 RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADA-ARRQFE--KAYEL--------VCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1308 SASDNIIQEYVTLRTRYSELMTLTSQYikfiTDTQRRLEdEEKAAEKLKAEEQKKMA----------EMQAELDKQK--- 1374
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLR-QQQNAERLLEEFCQRIGqqldaaeeleELLAELEAQLeel 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1375 --QLAEAHAKAIAkAEKEAQELKLRMQeEVSKRETAAVDAekqkqniQLELHELKNLSEQQIKDkSQQVDEALKSRLRIE 1452
Cdd:COG3096 570 eeQAAEAVEQRSE-LRQQLEQLRARIK-ELAARAPAWLAA-------QDALERLREQSGEALAD-SQEVTAAMQQLLERE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1453 EEIHLIRIQLETT----------VKQKSNAED-ELKQLRDR-------------------------------------AD 1484
Cdd:COG3096 640 REATVERDELAARkqalesqierLSQPGGAEDpRLLALAERlggvllseiyddvtledapyfsalygparhaivvpdlSA 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1485 AAEKLRKL-------------AQEEAEKLRkqVSEETQKK---RLAEEELKHKSEAER----KAANEKQkaledLENLRM 1544
Cdd:COG3096 720 VKEQLAGLedcpedlyliegdPDSFDDSVF--DAEELEDAvvvKLSDRQWRYSRFPEVplfgRAAREKR-----LEELRA 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1545 QAEEAERQVKQAEVEKERQIQVAH-----------VAAQQSAAAELRSKQMSFAEnvskLEESLKQEHGTVLQLQQDAER 1613
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQafsqfvgghlaVAFAPDPEAELAALRQRRSE----LERELAQHRAQEQQLRQQLDQ 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1614 LRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEA------HKKSLAQEEAEKQKEEAD-------REAKKRSKA 1680
Cdd:COG3096 869 LKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLEPLVAVLQSDpeqfeqlQADYLQAKE 948
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1681 EESALKQRDMAENELeRQRR--LAESTAQQKLAAEQELI-RLRADFDNAEQQRSLLEDELYRLKNEVI------------ 1745
Cdd:COG3096 949 QQRRLKQQIFALSEV-VQRRphFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSqynqvlaslkss 1027
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1746 --AAQQERKQLEDELS------------KVRSEMDILIQL--KSRAEKetmSNTEKSKQLLEAE----ATKLRDLAEEAS 1805
Cdd:COG3096 1028 rdAKQQTLQELEQELEelgvqadaeaeeRARIRRDELHEElsQNRSRR---SQLEKQLTRCEAEmdslQKRLRKAERDYK 1104
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1806 KLRAIAEEAK-------------------HQRQLAEEDAarqraeaerilkEKLAAISDatrlktEAEIALKEKEAENER 1866
Cdd:COG3096 1105 QEREQVVQAKagwcavlrlardndverrlHRRELAYLSA------------DELRSMSD------KALGALRLAVADNEH 1166
|
890
....*....|....*....
gi 1655274923 1867 LR---RQAEDEAY-QRKIL 1881
Cdd:COG3096 1167 LRdalRLSEDPRRpERKVQ 1185
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1951-2128 |
2.01e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQSKLRAEEEAEKLRRLVLEEEmRRKEAEDKVKKIAAAEEEAARQRKA---AQEELDRLQKKADEVRKQKE 2027
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKE-RLAAQEQKKQAEEAAKQAALKQKQAeeaAAKAAAAAKAKAEAEAKRAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2028 EADK--EAEKQIVAAQQAALKcnmAEQQvqsvlAQQKEDSMMQNKLKEEYEK---AKALARDAEAAKERAEREAALLRQQ 2102
Cdd:PRK09510 158 AAAKkaAAEAKKKAEAEAAKK---AAAE-----AKKKAEAEAAAKAAAEAKKkaeAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
170 180
....*....|....*....|....*.
gi 1655274923 2103 AEEAERQKVAAEQEAANQAKAQDDAE 2128
Cdd:PRK09510 230 AAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1908-2594 |
2.18e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ERQKAIvDDTLKQRRVveEEIRilklnfEKASSGKLDLELELNKLKNIAEETQqSKLRAEEEAEKLRRLVlEEEMRRKEA 1987
Cdd:PRK02224 150 DRQDMI-DDLLQLGKL--EEYR------ERASDARLGVERVLSDQRGSLDQLK-AQIEEKEEKDLHERLN-GLESELAEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1988 EDKVKKIAAAEEEAARQRKAA----------QEELDRLQKKADEVRKQKEEADKEAEkqivaaqqaALKCNMAEQQVQsv 2057
Cdd:PRK02224 219 DEEIERYEEQREQARETRDEAdevleeheerREELETLEAEIEDLRETIAETERERE---------ELAEEVRDLRER-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2058 laqqkedsmmqnklKEEYEKAKALARdAEAAKERAEREAALLRQQAEEAERQKVAA--EQEAANQAKAQDDAERLRKDAE 2135
Cdd:PRK02224 288 --------------LEELEEERDDLL-AEAGLDDADAEAVEARREELEDRDEELRDrlEECRVAAQAHNEEAESLREDAD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2136 feaaklaqaeaaalkqkqqADEEMAKHKKLAEQTLkqkfqvEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQK 2215
Cdd:PRK02224 353 -------------------DLEERAEELREEAAEL------ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2216 ASVEEELFKVKIQMEEL----MKLKVRIE------EENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARL 2285
Cdd:PRK02224 408 GNAEDFLEELREERDELrereAELEATLRtarervEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2286 RQIAEDdlnqqrtlaekmLKEKMQAIQEASRLKAEAEMLQRQKDLAQEqaqkLLEDKQlmqqrldEETEEYQRSLEAERK 2365
Cdd:PRK02224 488 EEEVEE------------VEERLERAEDLVEAEDRIERLEERREDLEE----LIAERR-------ETIEEKRERAEELRE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2366 RQLEIIAEAEklklqvsQLSEAQAKAeeeakkfkkqadtiaarlhetEIATKEQMTEVKKMEfEKLNTSKEADDLRKAIT 2445
Cdd:PRK02224 545 RAAELEAEAE-------EKREAAAEA---------------------EEEAEEAREEVAELN-SKLAELKERIESLERIR 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2446 ELEKEKARLKKEAEEHQNKSKEMADAQQKQIERemtvlqqtfLTEKemllkkekliEDEKKKLESQFEEE-IKKAKALKD 2524
Cdd:PRK02224 596 TLLAAIADAEDEIERLREKREALAELNDERRER---------LAEK----------RERKRELEAEFDEArIEEAREDKE 656
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2525 EQDRQRQQMEEEKlklkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQervLADENQKLREKLQQME 2594
Cdd:PRK02224 657 RAEEYLEQVEEKL------------DELREERDDLQAEIGAVENELEELEE---LRERREALENRVEALE 711
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2188-2556 |
2.27e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 57.33 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2188 EETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVK---IQMEELMKLKVRIEEENQRLMKKDKDNT----QKFLVE 2260
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKlsdIKTEYLYELNVLKEKSEAELTSKTKKELdaafEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2261 EAENMKKLAEdAARLSIEAQEAARLRQiaEDDLNQQRTLAEKMLKEKmqaIQEASRLKAEAEMlqrqkDLAQEQAQKLLE 2340
Cdd:NF033838 134 TLEPGKKVAE-ATKKVEEAEKKAKDQK--EEDRRNYPTNTYKTLELE---IAESDVEVKKAEL-----ELVKEEAKEPRD 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2341 DKQLMQQRLDEETEEyqrsleAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETeiATKEQM 2420
Cdd:NF033838 203 EEKIKQAKAKVESKK------AEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG--VLGEPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2421 TEVKKMEFEKLNTSKEADDL--------RKAITELEKEKARLKKEAEEHQNKSKE-MADAQQKQIEREMTVLQQTfLTEK 2491
Cdd:NF033838 275 TPDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKAKDQKEEDRRnYPTNTYKTLELEIAESDVK-VKEA 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2492 EMLLKKE--KLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALnKQKEAEK 2556
Cdd:NF033838 354 ELELVKEeaKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKV-KEKPAEQ 419
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
156-263 |
2.34e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.02 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 156 QSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVAEKDLGV 234
Cdd:cd21313 3 DAKKQTPKQRLLGWIQ---NKIPYLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1655274923 235 TRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2306-2599 |
2.47e-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: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2306 EKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKqlmqqrldEETEEYQRSLEAERKRQL-EIIAEAEKLKLQVSQL 2384
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER--------EKAERYQALLKEKREYEGyELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2385 SEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMefeklnTSKEADDLRKAITELEKEKARLKKEAEEHQNK 2464
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2465 SKEMADAQQK-QIEREMTVLQQTFLTEK--EMLLKKEKLIE------DEKKKLESQFEEEIKKAKALKDEQDRQRQQME- 2534
Cdd:TIGR02169 317 LEDAEERLAKlEAEIDKLLAEIEELEREieEERKRRDKLTEeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEk 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2535 --EEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE--------QERVLADEnQKLREKLQQMEEAQKS 2599
Cdd:TIGR02169 397 lkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEleeekedkALEIKKQE-WKLEQLAADLSKYEQE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2372-2582 |
2.56e-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: 56.31 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2372 AEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEfeklntsKEADDLRKAITELEKEK 2451
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2452 ARLKKEAEEHQNKSKEMADAQQK-----------------QIEREMTVLQQtFLTEKEMLLKKEKLIEDEKKKLESQFEE 2514
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRlgrqpplalllspedflDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2515 EIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELER--KRLEQERVLADE 2582
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2422-2600 |
3.03e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2422 EVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQ-------QTFLTEKEML 2494
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2495 lkkEKLIEDEKKKLESQfeeeikkaKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE 2574
Cdd:COG3883 125 ---SKIADADADLLEEL--------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
170 180
....*....|....*....|....*.
gi 1655274923 2575 QERVLADENQKLREKLQQMEEAQKST 2600
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1340-1560 |
3.35e-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: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1340 DTQRRLEDEEKAAEKLKAEEQKKMAEM--QAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAvdAEKQKQ 1417
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELeqRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAE--AERKAK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1418 NiqlelhELKNLSEQQIKDKSQQvdealksrlrieeeihliriqlettVKQKSNAEDELKQLRDRADAAEKLRKLAQEE- 1496
Cdd:TIGR02794 146 E------EAAKQAEEEAKAKAAA-------------------------EAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1497 ---AEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDL--ENLRMQAEEAERQVKQAEVEK 1560
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLasGSNAEKQGGARGAAAGSEVDK 263
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2231-2595 |
3.36e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2231 ELMKLKVRIEEENQRLMkkdkdNTQKFLVEEAENMKKLAED----AARLSIeAQEAARLR-QI--AEDDLNQqrtlAEKM 2303
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLEE----LEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2304 LKEKMQAIQEASRlkaEAEMLQRQKDLAQEQAQKLleDKQL--MQQRLDEETE---EYQRSLEA-ERKRQLeiiaeaekl 2377
Cdd:PRK04863 364 LEEQNEVVEEADE---QQEENEARAEAAEEEVDEL--KSQLadYQQALDVQQTraiQYQQAVQAlERAKQL--------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2378 kLQVSQLSeaqakaeeeakkfkkqADTIAARLHETEIATKEQMTEVKKMEfEKLNTSKEADD--------LRKAITELEK 2449
Cdd:PRK04863 430 -CGLPDLT----------------ADNAEDWLEEFQAKEQEATEELLSLE-QKLSVAQAAHSqfeqayqlVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2450 EKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTF---------LTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAK 2520
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLrqqqraerlLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2521 ALKDEQDRQRQQMEEEKLKLKA-------------TMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLR 2587
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQAriqrlaarapawlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELA 651
|
....*...
gi 1655274923 2588 EKLQQMEE 2595
Cdd:PRK04863 652 ARKQALDE 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2177-2597 |
3.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.97 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2177 EQELTKVKLQLEETDKQKslldDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQK 2256
Cdd:PRK02224 212 ESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2257 FLVEEAENMKKLAE-DAARLSIEAQEAARlrqiaeDDLNQQRTLAEKMLKEKMQAIQEAsrlKAEAEMLQRQKDLAQEQA 2335
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAH---NEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2336 QKLLEDKQlmqqRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETE-- 2413
Cdd:PRK02224 359 EELREEAA----ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEat 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2414 -------IATKEQMTEVKK-----MEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAqqKQIEREMT 2481
Cdd:PRK02224 435 lrtarerVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL--VEAEDRIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2482 VLQQTFLTEKEMLLKKEKLIE----------DEKKKLESQFEEEIKKAKALKDEQDRQRQQ---MEEEKLKLKATMDAaL 2548
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEekreraeelrERAAELEAEAEEKREAAAEAEEEAEEAREEvaeLNSKLAELKERIES-L 591
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2549 NKQKEAEKDILNKQKEMQEL----------------------ERKRLEQERVLADENQKLREKLQQMEEAQ 2597
Cdd:PRK02224 592 ERIRTLLAAIADAEDEIERLrekrealaelnderrerlaekrERKRELEAEFDEARIEEAREDKERAEEYL 662
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2003-2199 |
3.58e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEVRKQKE------EADKEAEKQIVAAQQAalkcnmAEQQVQSVLAQQKEDSMMQNKLKEEYE 2076
Cdd:PRK09510 81 RKKKEQQQAEELQQKQAAEQERLKQlekerlAAQEQKKQAEEAAKQA------ALKQKQAEEAAAKAAAAAKAKAEAEAK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2077 KAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQAD 2156
Cdd:PRK09510 155 RAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA--------------EAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274923 2157 EEMAKHKKLAEQtlKQKFQVEQELTKVKLQLEETDKQKSLLDD 2199
Cdd:PRK09510 221 AEAKAAAAKAAA--EAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1343-1882 |
3.90e-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: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEKLK---AEEQKKMAEMQAELDK-QKQLAEAHAKAiaKAEKEAQELKLRMQEEVSK----RETAAVDAEK 1414
Cdd:pfam05557 27 RARIELEKKASALKrqlDRESDRNQELQKRIRLlEKREAEAEEAL--REQAELNRLKKKYLEALNKklneKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1415 QKQNIQLELHELKnlseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEdelKQLRDRADAAEKLRKLAQ 1494
Cdd:pfam05557 105 VISCLKNELSELR----RQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE---KQQSSLAEAEQRIKELEF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1495 EEAEKLRKQVSEETQKKRLA-----EEELK-HKSEAERKAANEKQKAL--EDLENLR--------MQAEEAERQVKQAEV 1558
Cdd:pfam05557 178 EIQSQEQDSEIVKNSKSELAripelEKELErLREHNKHLNENIENKLLlkEEVEDLKrklereekYREEAATLELEKEKL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1559 EKERQiqvAHVAAQQSAAAELRS-------------KQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenar 1625
Cdd:pfam05557 258 EQELQ---SWVKLAQDTGLNLRSpedlsrrieqlqqREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK-------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1626 eeaeRELEKWRQKANEALRLRLQ-------AEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQ 1698
Cdd:pfam05557 327 ----IEDLNKKLKRHKALVRRLQrrvllltKERDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1699 RRLAESTA----QQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAqqERKQLEDELSKVRSEMDiliqlksR 1774
Cdd:pfam05557 403 LSVAEEELggykQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEL--ERQRLREQKNELEMELE-------R 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1775 AEKETMSNTEKSKQLleaeatKLRDlaEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAE 1854
Cdd:pfam05557 474 RCLQGDYDPKKTKVL------HLSM--NPAAEAYQQRKNQLEKLQ-AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKE 544
|
570 580
....*....|....*....|....*...
gi 1655274923 1855 IALKEKEAENERLRRQAEDEAYQRKILE 1882
Cdd:pfam05557 545 VLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1478-1715 |
4.15e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.58 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1478 QLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRlaeeelkhKSEAERKAANEKQKaledlenlrmQAEEAERQVKQAE 1557
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLK--------QLEKERLAAQEQKK----------QAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1558 VEKERQIQVAHVAAQQSAAAElrskQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAenareeaerelekwrq 1637
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAE----AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEA---------------- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1638 KANEALRLRLQAEEEAHKKSlaqeeaekqkeeaDREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQE 1715
Cdd:PRK09510 192 AAKAAAEAKKKAEAEAKKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1799-2036 |
4.30e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1799 DLAEEASKLRAIAEEAKHQRQLAEEdAARQRAEAERILKEKLAAISDATRL--KTEAEIALKEKEAE--NERLRRQAEDE 1874
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1875 AYQRKILEDQ-ANQHKLEIEEKIVLLKKSSDA-EMERQKAIVDDTLKQRRVveeeirilklnfekassgkldlelELNKL 1952
Cdd:COG4942 100 EAQKEELAELlRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARRE------------------------QAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1953 KNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKE 2032
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....
gi 1655274923 2033 AEKQ 2036
Cdd:COG4942 236 AAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2198-2378 |
4.45e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2198 DDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmKKDKDNTQKFLVEEAENMKKLAEDAARLSI 2277
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2278 EAQEAARLRQIAE--------DDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRL 2349
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|..
gi 1655274923 2350 DEETEEYQR---SLEAERKRQLEIIAEAEKLK 2378
Cdd:COG3883 174 EAQQAEQEAllaQLSAEEAAAEAQLAELEAEL 205
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1907-2507 |
4.66e-07 |
|
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: 56.30 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1907 MERQKAIVDDTLKQRRVVEEEIRILKlnfekassgkldlelelnklkniaEETQQSKLRAEEEAEKLRRLVLEEEMRRKE 1986
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEEEVRLLR------------------------ETSLQQKMRLEAQAMELDALAVAEKAGQAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1987 AEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQA------ALKCNMAEQQVQSVLAq 2060
Cdd:pfam07111 117 AEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGlekslnSLETKRAGEAKQLAEA- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2061 QKEDSMMQNKLKEEYEKAKALARDAEAAKER-AEREAALLRQQAEEAERQKVAAEQEAANQAKA--QDDAERLRKDAEFE 2137
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRKYvGEQVPPEVHSQTWELERQELLDTMQHLQEDRAdlQATVELLQVRVQSL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2138 AAKLAQAEAAALKQKQQAD----EEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQkslLDDELQRLKDEVDDAMR 2213
Cdd:pfam07111 276 THMLALQEEELTRKIQPSDslepEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQ---LRGQVAELQEQVTSQSQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2214 QKASVEEELFKVKIQME------ELMKLKVRIEEENQRLMKKDKDNTQ---KFLVEEAEN--------MKKLAEDAAR-- 2274
Cdd:pfam07111 353 EQAILQRALQDKAAEVEvermsaKGLQMELSRAQEARRRQQQQTASAEeqlKFVVNAMSStqiwlettMTRVEQAVARip 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2275 -LSIEAQEAAR---------LRQIAEDDLNQQRT--------LAEKMLKEKMQAIQEASRLKAE----AEMLQRQKDLAQ 2332
Cdd:pfam07111 433 sLSNRLSYAVRkvhtikglmARKVALAQLRQESCpppppappVDADLSLELEQLREERNRLDAElqlsAHLIQQEVGRAR 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2333 EQAQklLEDKQLMQ--QRLDEETEEYQRS-------LEAERKRQLEIIAEAEKLKLQVSQlseaqakaeeeakKFKKQAD 2403
Cdd:pfam07111 513 EQGE--AERQQLSEvaQQLEQELQRAQESlasvgqqLEVARQGQQESTEEAASLRQELTQ-------------QQEIYGQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2404 TIAARLHETEIATKEQMTEVKKmefeKLNTSKEadDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVL 2483
Cdd:pfam07111 578 ALQEKVAEVETRLREQLSDTKR----RLNEARR--EQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQRLARRV 651
|
650 660
....*....|....*....|....*.
gi 1655274923 2484 QQTFLTEKEML--LKKEKLIEDEKKK 2507
Cdd:pfam07111 652 QELERDKNLMLatLQQEGLLSRYKQQ 677
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
34-153 |
4.70e-07 |
|
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: 52.35 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 34 ATDGRKDERDRVQKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFH 100
Cdd:cd21323 13 SSEGTQHSYSEEEKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFT 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 101 KLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 153
Cdd:cd21323 93 ISENLNLALNSASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1691-1912 |
4.99e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.61 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1691 AENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIq 1770
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1771 lksRAEKETMSNTEKSKQLLEAEatklrDLAEEASKLRAIAEEAKHQRQL------AEEDAARQRAEAERILKEKLAAIS 1844
Cdd:COG3883 93 ---RALYRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSKIADADADLleelkaDKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1845 DATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKA 1912
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1008-1556 |
5.28e-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: 56.18 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1008 IRKPVEKEPLKECIQKTAE-QAKVQVELEGLKKDLDKVSTKTQDILNSpqpsatapVLRSELELTVQKMDHAYMLSsvyl 1086
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKnIDKFLTEIKKKEKELEKLNNKYNDLKKQ--------KEELENELNLLEKEKLNIQK---- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1087 eKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKE-VETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMS 1165
Cdd:TIGR04523 188 -NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKqNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1166 RVHSERDAELDQHRQHLSSL-------------------QDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWLIRWIAD 1226
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELekqlnqlkseisdlnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1227 AKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEK-NKDKVDECQKYAKAyidiIKDYELQLVAYKAQVEPLTSPLKKtk 1305
Cdd:TIGR04523 347 LKKELTNSE----SENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQ----INDLESKIQNQEKLNQQKDEQIKK-- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1306 LDSASDNIIQEYvtlrTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIA 1385
Cdd:TIGR04523 417 LQQEKELLEKEI----ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1386 KAEKEAQELKlrmqEEVSKRETAAVDAEKQKQNIQLELHELKNlseqQIKDKSQQVDEaLKSRLrIEEEIHLIRIQLETT 1465
Cdd:TIGR04523 493 SKEKELKKLN----EEKKELEEKVKDLTKKISSLKEKIEKLES----EKKEKESKISD-LEDEL-NKDDFELKKENLEKE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1466 VKQKSNAEDELKQLRDRADAA--EKLRKLAQEEAEK--LRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLEN 1541
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKqeEKQELIDQKEKEKkdLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
570
....*....|....*
gi 1655274923 1542 LRMQAEEAERQVKQA 1556
Cdd:TIGR04523 643 LKQEVKQIKETIKEI 657
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1741-2134 |
5.65e-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: 55.80 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1741 KNEVIAAQQERKQLEDELSKVRSEMdiliqlksraeketmsnTEKSKQLLEAEATKLRDLAEEASKLRAIaEEAKH--QR 1818
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEI-----------------PEYKKQSEAAEAAKAQVLEELESTKRLI-EELKLnlER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1819 QLAEEDAARQRAE-AERILKEKLAAISDatrlktEAEIALKEK-EAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKI 1896
Cdd:pfam05701 89 AQTEEAQAKQDSElAKLRVEEMEQGIAD------EASVAAKAQlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1897 VLLKKSSDAEMERQKAivddtlkQRRVVEEEIRILKLNFEKASSGKLDLELELNKLkNIAEETQQSKLR-------AEEE 1969
Cdd:pfam05701 163 IAIKRAEEAVSASKEI-------EKTVEELTIELIATKESLESAHAAHLEAEEHRI-GAALAREQDKLNwekelkqAEEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1970 AEKLR-RLVLEEEMRRK-----------------EAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 2031
Cdd:pfam05701 235 LQRLNqQLLSAKDLKSKletasallldlkaelaaYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2032 EAEKQIVAAqqAALKCNMAEQQVQSVLAQQKED--SMMQNKLKEEYEKAK---ALARDAE-AAKERAEREAALLRQQAEE 2105
Cdd:pfam05701 315 EVNCLRVAA--ASLRSELEKEKAELASLRQREGmaSIAVSSLEAELNRTKseiALVQAKEkEAREKMVELPKQLQQAAQE 392
|
410 420
....*....|....*....|....*....
gi 1655274923 2106 AERQKVAAEQEAANQAKAQDDAERLRKDA 2134
Cdd:pfam05701 393 AEEAKSLAQAAREELRKAKEEAEQAKAAA 421
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
988-1508 |
6.53e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.88 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 988 SEVKDLRLRIEDCEARTVARIRK-PVEKEPLKECIQKtaeQAKVQVELEGLKKDLDKvSTKTQDILNSPQPSATAPV--L 1064
Cdd:pfam05483 254 NKMKDLTFLLEESRDKANQLEEKtKLQDENLKELIEK---KDHLTKELEDIKMSLQR-SMSTQKALEEDLQIATKTIcqL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1065 RSELELTVQKMDHAYMLSSVYLEKLKTVEMVIrntqgaegvlkqyENCLR-EVHTVPNDVKEVETYRTNLKKMRAEAEAE 1143
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSL-------------EELLRtEQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1144 QPVFDSLEEELkkasavsDKMSRVHSERDAELDQHRQH---LSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYDWL 1220
Cdd:pfam05483 397 TKFKNNKEVEL-------EELKKILAEDEKLLDEKKQFekiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1221 IRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEE-------IEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQ 1293
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEasdmtleLKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1294 VEPLTSPLK------KTKLDSASDN---IIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLED---EEKAAEKLKAEEQK 1361
Cdd:pfam05483 550 LESVREEFIqkgdevKCKLDKSEENarsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElhqENKALKKKGSAENK 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1362 KMAEMQAELDK-QKQLAEAHAK---AIAKAEKEAQELKL---RMQEEVSKRETAAVDAEKQKQNIQLEL-HELKNLSEQQ 1433
Cdd:pfam05483 630 QLNAYEIKVNKlELELASAKQKfeeIIDNYQKEIEDKKIseeKLLEEVEKAKAIADEAVKLQKEIDKRCqHKIAEMVALM 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 1434 IKDKsQQVDEALKSRlriEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEET 1508
Cdd:pfam05483 710 EKHK-HQYDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2150-2366 |
7.52e-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: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2150 KQKQ----QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKV 2225
Cdd:COG4942 23 AEAEaeleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2226 KIQMEELMKLKVRIEEENQRLMKKDKDNTQKFlVEEAENMKKLAE-DAARLSIEAQEAARLRQIaEDDLNQQRTLAEKML 2304
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDA-VRRLQYLKYLAPaRREQAEELRADLAELAAL-RAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2305 KEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKR 2366
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2218-2577 |
7.86e-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: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2218 VEEELFKVKIQMEELMKLKVRIEEENQRLMKKDkdntQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQR 2297
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKR----IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2298 TLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQR-SLEAERKRQLEIIAEAEK 2376
Cdd:pfam13868 77 ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEeQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2377 LKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLheteiATKEQMTEVKKMEFEKLNTSKEADDLRkaitelEKEKARLKK 2456
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEEKEREIARL-----RAQQEKAQDEKAERDELRAKLYQEEQE------RKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2457 EAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMllkKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEE 2536
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEE---FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEER 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1655274923 2537 KLKLKAtmdaalnkQKEAEKDILNKQKEMQELERKRLEQER 2577
Cdd:pfam13868 303 EEQRAA--------EREEELEEGERLREEEAERRERIEEER 335
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2173-2603 |
8.72e-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: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2173 KFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEE-LFKVKIQMEELMKLKVRIEEENQR---LMK 2248
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERlkaLTG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2249 KDKDNTQKFLVEEA----ENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRT-LAEKMLKEKMQAIQEASRLKAEAEM 2323
Cdd:pfam12128 369 KHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESeLREQLEAGKLEFNEEEYRLKSRLGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2324 LQRQKDLAQeqaqklLEDKQLMQQRL-DEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEaqakaeeeakkfkkqa 2402
Cdd:pfam12128 449 LKLRLNQAT------ATPELLLQLENfDERIERAREEQEAANAEVERLQSELRQARKRRDQASE---------------- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2403 dtiaaRLHETEIATKEQMT---EVKKMEFEKLNT-----SKEADDLRKAI-----------TELEKEK------------ 2451
Cdd:pfam12128 507 -----ALRQASRRLEERQSaldELELQLFPQAGTllhflRKEAPDWEQSIgkvispellhrTDLDPEVwdgsvggelnly 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2452 -ARLKKEAEEHqnksKEMADAQQkQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQR 2530
Cdd:pfam12128 582 gVKLDLKRIDV----PEWAASEE-ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2531 QqmeeeklklkatmdaaLNKQKEAEKDILNKQKEmqelERKRLEQERV--LADENQKLREKLQQMEEAQKSTLIT 2603
Cdd:pfam12128 657 R----------------LFDEKQSEKDKKNKALA----ERKDSANERLnsLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1702-1916 |
8.87e-07 |
|
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: 55.42 E-value: 8.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1702 AESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEViaaqqerKQLEDELSKVRSEMDILIQLKSRAEK---- 1777
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNEELEKQYKVKKKtldl 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1778 --ETMSNTEKSKQLLEAEATKLRDLAEEASKLRA--IAEEAKHQRQLAE-EDAARQRAEAERILKEKLAAISDATRLKTE 1852
Cdd:pfam05667 396 lpDAEENIAKLQALVDASAQRLVELAGQWEKHRVplIEEYRALKEAKSNkEDESQRKLEEIKELREKIKEVAEEAKQKEE 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1853 AeiaLKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIE-EKIVLLKKSSDAEM-------ERQKAIVDD 1916
Cdd:pfam05667 476 L---YKQLVAEYERLPKDVSRSAYTRRILEIVKNIKKQKEEiTKILSDTKSLQKEInsltgklDRTFTVTDE 544
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1344-1577 |
9.09e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1344 RLEDEEKAAEKLKAEEQKKMAEMQAELdKQKQLAEahakaiakAEKEAQELKLRMQEEvskretaavdaEKQKQNIQlel 1423
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEEL-QQKQAAE--------QERLKQLEKERLAAQ-----------EQKKQAEE--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1424 helknlSEQQIKDKSQQVDEALKSRLRieeeihliriqlettvKQKSNAEDELKQLRDRA-DAAEKLRKLAQEEAEklrK 1502
Cdd:PRK09510 123 ------AAKQAALKQKQAEEAAAKAAA----------------AAKAKAEAEAKRAAAAAkKAAAEAKKKAEAEAA---K 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 1503 QVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAA 1577
Cdd:PRK09510 178 KAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1346-1589 |
9.94e-07 |
|
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: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1346 EDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretAAVDAEKQKQNIQLELHE 1425
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK-------LQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1426 LKN-LSEQQIKDKSQQVDEALKSRLRIEEEIHliRIQLETTVKQKSNaeDELKQLRDRADAAEKLRKLAQEEAEKLRKQV 1504
Cdd:COG3883 88 LGErARALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADA--DLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1505 SEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQM 1584
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....*
gi 1655274923 1585 SFAEN 1589
Cdd:COG3883 244 ASAAG 248
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2290-2564 |
1.12e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 53.76 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2290 EDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSleaeRKRQLE 2369
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDE---LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL----KEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2370 IIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAA--RLHETEIATKEQ----MTEVKKMEfEKLNTSKEADDLRKA 2443
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERleWRQQTEVLSPEEekelVEKIKELE-KELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2444 ITELEKEKARLKKEAEEHQNKSKEMADAQQKqieremTVLQQTFLTEKEMLLKKEkliEDEKKKlesQFEEEIKKAKALK 2523
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQE------LHEEMIELYKEADELRKE---ADELHK---EIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1655274923 2524 DEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE 2564
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2171-2629 |
1.16e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2171 KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEV-------DDAMRQKASVEEELFKVKIQM----EELMKLKVRI 2239
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnnkyNDLKKQKEELENELNLLEKEKlniqKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2240 EEENQRLMK-KDKDNTQKFLVEEAENMKK----LAEDAARLSIEAQEAARLRQIAEDDLNQ---QRTLAEKMLKEKMQAI 2311
Cdd:TIGR04523 197 LKLELLLSNlKKKIQKNKSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKEL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2312 QEASRLKAEAEmlqrqkDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEaERKRQLEI-IAEAEK----LKLQVSQLSE 2386
Cdd:TIGR04523 277 EQNNKKIKELE------KQLNQLKSEISDLNNQKEQDWNKELKSELKNQE-KKLEEIQNqISQNNKiisqLNEQISQLKK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2387 AQAKAeeeakkfkkqadtiaarlhETEIATKEQMTEVKKMEFEKLNtsKEADDLRKAITELEKEKARLKKEAEEHQNKSK 2466
Cdd:TIGR04523 350 ELTNS-------------------ESENSEKQRELEEKQNEIEKLK--KENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2467 EMaDAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKlESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 2546
Cdd:TIGR04523 409 QK-DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2547 ALN--KQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQKSTLitEKHVTVVETVLNGQNAGDVLD 2624
Cdd:TIGR04523 487 KQKelKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL--EDELNKDDFELKKENLEKEID 564
|
....*
gi 1655274923 2625 GVEKR 2629
Cdd:TIGR04523 565 EKNKE 569
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1894-2583 |
1.18e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1894 EKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILK-----------------------LNFEKASSGKLDLELELN 1950
Cdd:pfam12128 182 DKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRqqvehwirdiqaiagimkirpefTKLQQEFNTLESAELRLS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLK-NIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLqkkaDEVRKQKEEA 2029
Cdd:pfam12128 262 HLHfGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL----EDQHGAFLDA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2030 DKEAEKQivAAQQAALKCNMAEQQVQSVLAQQKEdsmmQNKLKEEYEKAKA-----LARDAEAAKERAE--REAALLRQQ 2102
Cdd:pfam12128 338 DIETAAA--DQEQLPSWQSELENLEERLKALTGK----HQDVTAKYNRRRSkikeqNNRDIAGIKDKLAkiREARDRQLA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2103 AEEAERQKVAA---EQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaalKQKQQADEEMAkhkklAEQTLKQKFQVEQE 2179
Cdd:pfam12128 412 VAEDDLQALESelrEQLEAGKLEFNEEEYRLKSRLG--------------ELKLRLNQATA-----TPELLLQLENFDER 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2180 LTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKD----KDNTQ 2255
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEapdwEQSIG 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2256 KFL-------------VEEAENMKKLAEDAARLSIEA----------QEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 2312
Cdd:pfam12128 553 KVIspellhrtdldpeVWDGSVGGELNLYGVKLDLKRidvpewaaseEELRERLDKAEEALQSAREKQAAAEEQLVQANG 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2313 EASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEaERKRQLEiiAEAEKLKLQVSQLSEaqakae 2392
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQLKQLDKKHQAWLE------ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2393 eeakkfkkqadtiaarlheteiATKEQMTEvkkmefeklNTSKEADDLRKAITELEKEKARLKKEAEehqnKSKEMADAQ 2472
Cdd:pfam12128 704 ----------------------EQKEQKRE---------ARTEKQAYWQVVEGALDAQLALLKAAIA----ARRSGAKAE 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2473 QKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE--SQFEEEIKKAkalkdeQDRQRQQMEEEKLKLKATMDAALNK 2550
Cdd:pfam12128 749 LKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIEriAVRRQEVLRY------FDWYQETWLQRRPRLATQLSNIERA 822
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1655274923 2551 QKEAEKDiLNKQKEMQELERKRLEQER-------VLADEN 2583
Cdd:pfam12128 823 ISELQQQ-LARLIADTKLRRAKLEMERkasekqqVRLSEN 861
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2154-2408 |
1.18e-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: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2154 QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM 2233
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2234 klkvrieeenQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLS-IEAQEAARLrqiaeDDLNQQRTLAEKMLKEKMQAIQ 2312
Cdd:COG3883 93 ----------RALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLL-----EELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2313 EASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAE 2392
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|....*.
gi 1655274923 2393 EEAKKFKKQADTIAAR 2408
Cdd:COG3883 238 AAAAAAASAAGAGAAG 253
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
620-712 |
1.40e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.64 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 620 HAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFTA 699
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1655274923 700 ALQTQWSWILQLC 712
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1952-2111 |
1.48e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1952 LKNIAEETQQSKlRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 2031
Cdd:COG2268 191 RRKIAEIIRDAR-IAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2032 EAEkqIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAaKERAEREAALLRQQAE-EAERQK 2110
Cdd:COG2268 270 IAE--ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEA-EAEAEAEAIRAKGLAEaEGKRAL 346
|
.
gi 1655274923 2111 V 2111
Cdd:COG2268 347 A 347
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4122-4150 |
1.52e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 47.32 E-value: 1.52e-06
10 20
....*....|....*....|....*....
gi 1655274923 4122 IVDPETGKEMTVYEAYRKGLIDHQTYIEL 4150
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1124-1550 |
1.57e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1124 KEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKA-SAVSDKMSRVhSERDAELDQHRQHLSSLQDRWKAVFTQIDLRQRE 1202
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEArEAVEDRREEI-EELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1203 LDQLGRQLGYYResydwlirwiadakqrqeniqavpiTDSKTLKEQLAKEKKLLEEieknkDKVDECQKYAK--AYIDII 1280
Cdd:PRK02224 421 RDELREREAELE-------------------------ATLRTARERVEEAEALLEA-----GKCPECGQPVEgsPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1281 KDYELQ---LVAYKAQVEPLTSPLKKtKLDSASDniiqeYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKA 1357
Cdd:PRK02224 471 EEDRERveeLEAELEDLEEEVEEVEE-RLERAED-----LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1358 EEQKKMAEMQ---AELDKQKQLAEAHAKAIAKAEKEAQELKLRMqEEVSKRETAAVDAEKQKQNIQL------ELHELKN 1428
Cdd:PRK02224 545 RAAELEAEAEekrEAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERlrekreALAELND 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1429 LSEQQIKDKSQQVDEalksrlrIEEEIHLIRIqlETTVKQKSNAEDELkqlrdrADAAEKLRKLAQEEAEKLRKQVSEET 1508
Cdd:PRK02224 624 ERRERLAEKRERKRE-------LEAEFDEARI--EEAREDKERAEEYL------EQVEEKLDELREERDDLQAEIGAVEN 688
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1655274923 1509 QKKRLaeEELKHkseaERKAANEKQKALEDLENlrmQAEEAE 1550
Cdd:PRK02224 689 ELEEL--EELRE----RREALENRVEALEALYD---EAEELE 721
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2060-2605 |
1.70e-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: 54.84 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2060 QQKEDSMMQNKLKEEYEkakalARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAA 2139
Cdd:pfam12128 277 RQEERQETSAELNQLLR-----TLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2140 KLAQAEAAALKQKQQADeemaKHKKLAEQTLKQKFQVEQELT--------KVKLQLEETDKQKSLLDDELQRLKDEVDDA 2211
Cdd:pfam12128 352 WQSELENLEERLKALTG----KHQDVTAKYNRRRSKIKEQNNrdiagikdKLAKIREARDRQLAVAEDDLQALESELREQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2212 MRQ---KASVEEELFKVKIQMEELMKLKVRIEEEnqrlMKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAARLRQI 2288
Cdd:pfam12128 428 LEAgklEFNEEEYRLKSRLGELKLRLNQATATPE----LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQ 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2289 AEDDLNQqrtlAEKMLKEKMQAIQEA-SRLKAEA----EMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRS---- 2359
Cdd:pfam12128 504 ASEALRQ----ASRRLEERQSALDELeLQLFPQAgtllHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGgeln 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2360 -----LEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEiatkeqmtevKKMEFEKLNTS 2434
Cdd:pfam12128 580 lygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS----------REETFARTALK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2435 KEADDLRKAITELEKEKARLKKEAEEHQ---NKSKEMADAQQKQIEREMTVL----QQTFLTEKEMLLKKEKLIEDEKKK 2507
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNKALAERKdsaNERLNSLEAQLKQLDKKHQAWleeqKEQKREARTEKQAYWQVVEGALDA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2508 LESQFEEEIKKAKAlkdEQDRQRQQMEEEklklkatMDAALNKQKEAEKDILNKQKEMQELERKrLEQERVLADENQKLR 2587
Cdd:pfam12128 730 QLALLKAAIAARRS---GAKAELKALETW-------YKRDLASLGVDPDVIAKLKREIRTLERK-IERIAVRRQEVLRYF 798
|
570
....*....|....*...
gi 1655274923 2588 EKLQQMEEAQKSTLITEK 2605
Cdd:pfam12128 799 DWYQETWLQRRPRLATQL 816
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2435-2605 |
1.77e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2435 KEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEE 2514
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2515 EIKKAKALKdEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNK-QKEMQELERKRLEQERVLADENQKLREKLQQM 2593
Cdd:COG4717 151 LEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 1655274923 2594 EEAQKSTLITEK 2605
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1243-1566 |
1.88e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1243 KTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQvepltsplkKTKLDSASDNIIQEYVTLRT 1322
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE---------KLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1323 RYSELMTLTSQYiKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAhakaIAKAEKEAQELKlRMQEE 1401
Cdd:TIGR04523 202 LLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtQTQLNQL----KDEQNKIKKQLS-EKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1402 VSKRETAAVDAEKQKQNIQLELHELKNlseqqikDKSQQVDEALKSRLRIEEEihliriQLETTVKQKSNAEDELKQLrd 1481
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNN-------QKEQDWNKELKSELKNQEK------KLEEIQNQISQNNKIISQL-- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1482 radaaeklrklaQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEV--- 1558
Cdd:TIGR04523 341 ------------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKlnq 408
|
....*...
gi 1655274923 1559 EKERQIQV 1566
Cdd:TIGR04523 409 QKDEQIKK 416
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3907-3945 |
1.92e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 46.94 E-value: 1.92e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1655274923 3907 YLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTAFEL 3945
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1806-2598 |
1.96e-06 |
|
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: 54.67 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1806 KLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIAlKEKEAENERLRRQaedeayQRKILEDQA 1885
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKNR------LKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1886 NQHKLEIEekivlLKKSSDAEMERQKAIVDDTLKQRRV---VEEEIRILKLNfeKASSGKLDLELELNKLKNIAEETQQS 1962
Cdd:TIGR00606 263 KIMKLDNE-----IKALKSRKKQMEKDNSELELKMEKVfqgTDEQLNDLYHN--HQRTVREKERELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1963 KLRAEEEAEklrrlvLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 2042
Cdd:TIGR00606 336 RLLNQEKTE------LLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2043 AALkcNMAEQQVQSVLAQQKEDSMMQNKlkeeyekaKALARDAEAAKERAEREAALLR---QQAEEAERQKVAAEQEAAN 2119
Cdd:TIGR00606 410 AAQ--LCADLQSKERLKQEQADEIRDEK--------KGLGRTIELKKEILEKKQEELKfviKELQQLEGSSDRILELDQE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2120 QAKAQDDAERLRKDAEFEAAKLAQAEAAALK-----QKQQADEEMAK---HKKLAEQTL---KQKFQVEQELTKVKLQle 2188
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQNEKadldrKLRKLDQEMEQlnhHTTTRTQMEmltKDKMDKDEQIRKIKSR-- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2189 ETDKQKSLLDD--ELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLveEAENMK 2266
Cdd:TIGR00606 558 HSDELTSLLGYfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF--DVCGSQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2267 KLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASR-LKAEAEMLQRQKDLaqEQAQKLLEDKQlm 2345
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDL--QSKLRLAPDKL-- 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2346 qqrldEETEEYQRSLEAERKRQLEII-AEAEKLKLQVSQLSEAQAKAEEEakkfkkqadtiaarlhETEIATKEQMTEVK 2424
Cdd:TIGR00606 712 -----KSTESELKKKEKRRDEMLGLApGRQSIIDLKEKEIPELRNKLQKV----------------NRDIQRLKNDIEEQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2425 KMEFEKLNTSKE-ADDLRKAITELEkekaRLKKEAEEHQNK-SKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIE 2502
Cdd:TIGR00606 771 ETLLGTIMPEEEsAKVCLTDVTIME----RFQMELKDVERKiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIE 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2503 DEKKKLESQFEE---------EIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRL 2573
Cdd:TIGR00606 847 LNRKLIQDQQEQiqhlksktnELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKE 926
|
810 820
....*....|....*....|....*
gi 1655274923 2574 EQERVLADENQKLREKLQQMEEAQK 2598
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVK 951
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1253-1583 |
2.08e-06 |
|
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: 54.25 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1253 KKLLEEIEKNKDKVDECQKYA--KAYIDIIKDY--ELQLVAYKAQVEpLTSPLKKtKLDSASDniiqeyvtlrtryselm 1328
Cdd:NF033838 68 EKILSEIQKSLDKRKHTQNVAlnKKLSDIKTEYlyELNVLKEKSEAE-LTSKTKK-ELDAAFE----------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1329 tltsqyiKFITDTqrrLEDEEKAAEKlkaeeQKKMAEMQAELDKQKQ-----------------LAEAHAKaIAKAEKE- 1390
Cdd:NF033838 129 -------QFKKDT---LEPGKKVAEA-----TKKVEEAEKKAKDQKEedrrnyptntyktleleIAESDVE-VKKAELEl 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1391 -AQELKLRMQEEVSKRETAAVDAEKQkqniqlELHELKNlseqqIKDKSQQVDEALKSRLRIEEEihliriqlETTVKQK 1469
Cdd:NF033838 193 vKEEAKEPRDEEKIKQAKAKVESKKA------EATRLEK-----IKTDREKAEEEAKRRADAKLK--------EAVEKNV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1470 SNAE-DELKQLRDRADAAEKLRKLAQEEAEKLR-KQVSEET-------QKKRLAEEElKHKSEAERKAANEKQkalEDLE 1540
Cdd:NF033838 254 ATSEqDKPKRRAKRGVLGEPATPDKKENDAKSSdSSVGEETlpspslkPEKKVAEAE-KKVEEAKKKAKDQKE---EDRR 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1541 N--------LRMQAEEAERQVKQAEVE--KERQIQVAHVAAQQSAAAELRSKQ 1583
Cdd:NF033838 330 NyptntyktLELEIAESDVKVKEAELElvKEEAKEPRNEEKIKQAKAKVESKK 382
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3906-3942 |
2.08e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.08e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 3906 KYLEGTSCIAGVYLESNKERLSIYQAMKKNMIRPGTA 3942
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2152-2598 |
2.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2152 KQQADEEMAKHKKLAEQTLKQKfQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEE 2231
Cdd:COG4717 93 LQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2232 LMKLKVRIEEENQRLmkkdkdntqkfLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRtlaekmlkekmqai 2311
Cdd:COG4717 172 LAELQEELEELLEQL-----------SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE-------------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2312 QEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLmqqrldeeteeyqrSLEAERKRQLEIIAE-AEKLKLQVSQLSEAQAK 2390
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALL--------------ALLGLGGSLLSLILTiAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2391 AEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEhqnkskemad 2470
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE---------- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2471 AQQKQIEREMT-VLQQTFLTEKEMLLKKEKL------IEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKlkat 2543
Cdd:COG4717 363 LQLEELEQEIAaLLAEAGVEDEEELRAALEQaeeyqeLKEELEELEEQLEELLGELEELLEALDEEELEEELEELE---- 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2544 mdaalNKQKEAEKDILNKQKEMQELER--KRLEQERVLADENQKLREKLQQMEEAQK 2598
Cdd:COG4717 439 -----EELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
34-154 |
2.58e-06 |
|
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: 50.06 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 34 ATDGRKDERDRVQKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFH 100
Cdd:cd21325 13 SSEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFI 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 101 KLQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 154
Cdd:cd21325 93 IQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2266-2598 |
2.58e-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: 53.00 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2266 KKLAEDAARLSIEAQEAARLRQIAEDDlnQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLM 2345
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEE--RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2346 QQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKK 2425
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2426 MEFEKLNTSKEADDLRKAitelEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFltEKEMLLKKEKLIEDek 2505
Cdd:pfam13868 184 REIARLRAQQEKAQDEKA----ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAR--EEQIELKERRLAEE-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2506 KKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKlkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 2585
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL----------EHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
330
....*....|...
gi 1655274923 2586 LREKLQQMEEAQK 2598
Cdd:pfam13868 326 ERRERIEEERQKK 338
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2498-2686 |
3.16e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.68 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2498 EKLIEdekkKLESQ---FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE--------MQ 2566
Cdd:PRK00409 519 NELIA----SLEELereLEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikeLR 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2567 ELERKRLEQ--ERVLADENQKLREKLQQMEEAQKSTLITEKHVTVVETV--LNGQNAGDVLdgvEKRPDPMA---FDGIR 2639
Cdd:PRK00409 595 QLQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkyLSLGQKGEVL---SIPDDKEAivqAGIMK 671
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1655274923 2640 DKVPASRLLDIGVLPKKEfdllKNGKTTAKELGETENLRKILKGKNS 2686
Cdd:PRK00409 672 MKVPLSDLEKIQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMRY 714
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1461-1884 |
3.35e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 53.37 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1461 QLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLE 1540
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1541 NLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQED 1620
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1621 AENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRR 1700
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1701 LAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDElyrlkNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETM 1780
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAE-----AVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1781 SNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEK 1860
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1655274923 1861 EAENERLRRQAEDEAYQRKILEDQ 1884
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1430-1642 |
3.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1430 SEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVseetq 1509
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1510 KKRLAE--------------------EELKHKSEAERKAANEKQKALEDLENLRMQAEEaerqvKQAEVEKERQIQVAHV 1569
Cdd:COG3883 89 GERARAlyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1570 AAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA 1642
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1577 |
4.29e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1335 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKaIAKAEKEAQELKLRMQEEVSKRETAAVDAE 1413
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNElQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1414 KQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLA 1493
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1494 QEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQ 1573
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
....
gi 1655274923 1574 SAAA 1577
Cdd:COG3883 257 AAAG 260
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1907-2097 |
4.58e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1907 MERQKAIVDDTLKQRRVVEEEiRILKLNFEKASSGKLDLELELNKLKniaeETQQSKLRAEEEAEKLRRLVLEEEMRRKE 1986
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-QAEELQQKQAAEQERLKQLEKERLA----AQEQKKQAEEAAKQAALKQKQAEEAAAKA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1987 AEDKVKKIAAAEEEAARQRKAAQEELDRlQKKADEVRKQKEEADK--EAEKQIVAAQQAALKCNMAEQQVQSVLAQQKED 2064
Cdd:PRK09510 142 AAAAKAKAEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKAAAEAKKkaEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|...
gi 1655274923 2065 SMMQNKLKEEYEKAKALARDAEAAKERAEREAA 2097
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
38-142 |
4.90e-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: 48.81 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 38 RKDERDRVQKKTFTKWVNKHLIKS--QRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKG--RMRFHKLQNVQIALDFLR 113
Cdd:cd21285 3 SWEAENGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLA 82
|
90 100
....*....|....*....|....*....
gi 1655274923 114 HRQVKLVNIRNDDIADGNPKLTLGLIWTI 142
Cdd:cd21285 83 AKGINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2007-2210 |
5.09e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2007 AAQEELDRLQ-KKADEVRKQKEEaDKEAEKQI------VAAQQAALKC----NMAEQQVQSVLAQQKEDSMMQNKLKEEy 2075
Cdd:PRK09510 59 AVVEQYNRQQqQQKSAKRAEEQR-KKKEQQQAeelqqkQAAEQERLKQlekeRLAAQEQKKQAEEAAKQAALKQKQAEE- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2076 EKAKALARDAEAAKERAEREAALLRQQAEEAERQ-KVAAEQEAANQAKAQDDAERLRKDAEfeaaklAQAEAAALKQKQQ 2154
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKaEAEAAKKAAAEAKKKAEAEAAAKAAA------EAKKKAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2155 ADEEmAKHKKLAEqtlkQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDD 2210
Cdd:PRK09510 211 AAAE-AKKKAAAE----AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1938-2195 |
5.35e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1938 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRlvleeemRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQK 2017
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-------QLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2018 KADEVRKQKEEADKEAEKQIVAAQQaalkcnMAEQQVQSVLAQQkeDSMMQNKLKEEYEKAKALARDAEAAKERAEREAa 2097
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYR------LGRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQAEELRADLAE- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2098 lLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDaefeaaklaqaeaaalkqKQQADEEMAKHKKLAEQTLKQKFQVE 2177
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALEALKAE------------------RQKLLARLEKELAELAAELAELQQEA 222
|
250
....*....|....*...
gi 1655274923 2178 QELTKVKLQLEETDKQKS 2195
Cdd:COG4942 223 EELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1089-1561 |
5.76e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1089 LKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKASAVSDKMSRVH 1168
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1169 serdaELDQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLGYYRESYdwlirwIADAKQRQENIQAvpitDSKTLKEQ 1248
Cdd:COG4717 150 -----ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE------LQDLAEELEELQQ----RLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1249 LAKEKKLLEEIEKNKDKVdECQKYAKAYIDIIKDYELQLVAYKAQVEpltsplkktkLDSASDNIIQEYVTLRTRYSELM 1328
Cdd:COG4717 215 LEEAQEELEELEEELEQL-ENELEAAALEERLKEARLLLLIAAALLA----------LLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1329 TLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETA 1408
Cdd:COG4717 284 GLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1409 AVDAEKQKQNIQLELHELKNLSE-QQIKDKSQQVDEALKSRLRIEEEIHLIR--IQLETTVKQKSNAEDELKQLRDRADA 1485
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1486 AEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQ-KALEDLENLRMQAEEAERQVKQAEVEKE 1561
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEwAALKLALELLEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1736-2108 |
6.65e-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: 52.44 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1736 ELYRLKNEVIAAQQERKQLEDELSKVRSEMdiliQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEAS-KLRAIAEEA 1814
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIEL----EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEeALREQAELN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1815 KHQRQLAE------EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE-----AYQRKILED 1883
Cdd:pfam05557 79 RLKKKYLEalnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLkakasEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1884 QANQHKL-EIEEKI--------------VLLKKSSD-----AEMERQKAIVDDTLKQRRVVEEEIRILK----------L 1933
Cdd:pfam05557 159 EKQQSSLaEAEQRIkelefeiqsqeqdsEIVKNSKSelariPELEKELERLREHNKHLNENIENKLLLKeevedlkrklE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1934 NFEKASSGKLDLELELNKL-------KNIAEET-----------------QQSKLRAEEEAEKLRRLVLEEEMRRKEAED 1989
Cdd:pfam05557 239 REEKYREEAATLELEKEKLeqelqswVKLAQDTglnlrspedlsrrieqlQQREIVLKEENSSLTSSARQLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1990 KVKKIAAAEEEAARQRKAAQEELDRLQKKA-------DEVRKQKEEADKEAeKQIVAAQQAALKCNMAEQQVQSVLAQQK 2062
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerDGYRAILESYDKEL-TMSNYSPQLLERIEEAEDMTQKMQAHNE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1655274923 2063 EDSMMQNKLKEEYEKAKALArdaeaakERAEREAALLRQQAEEAER 2108
Cdd:pfam05557 398 EMEAQLSVAEEELGGYKQQA-------QTLERELQALRQQESLADP 436
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2454-2598 |
6.96e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2454 LKKEAEEHQNKSKEMADAQQKQIEREMTVLqqtfltekemllKKEKLIE--DEKKKLESQFEEEIKKAKALKDEQDRQRQ 2531
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAI------------KKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2532 QMEEeklKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLrEKLQQM--EEAQK 2598
Cdd:PRK12704 93 QKEE---NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL-ERISGLtaEEAKE 157
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2278-2598 |
7.36e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2278 EAQEAARLRQiaeddlNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ 2357
Cdd:pfam02029 3 DEEEAARERR------RRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2358 RSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKE-QMTEVKKMEFEKLNTSKE 2436
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREkEYQENKWSTEVRQAEEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2437 ADDLRKAITELEKEKARLKKEAEEHQNKSKEMADA-------QQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 2509
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2510 SQFEEEIKKAKALKDEQDRQRQQMEEEKL-KLKatmdaalNKQKEAEKdilnkqkEMQELERKRLEQERVLADENQKLRE 2588
Cdd:pfam02029 237 EEEAEVFLEAEQKLEELRRRRQEKESEEFeKLR-------QKQQEAEL-------ELEELKKKREERRKLLEEEEQRRKQ 302
|
330
....*....|
gi 1655274923 2589 klqqmEEAQK 2598
Cdd:pfam02029 303 -----EEAER 307
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1413-1846 |
7.71e-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: 51.82 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1413 EKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLEttvkqksNAEDELKQLRDRADAAEKLRKL 1492
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA-------ELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1493 AQEEAEKLRKQVS-----EETQKKRLAEEELKHKSEAERKAANEKqkaleDLENLRMQAEEAERQVKQAEVEKErQIQva 1567
Cdd:pfam07888 106 LSASSEELSEEKDallaqRAAHEARIRELEEDIKTLTQRVLERET-----ELERMKERAKKAGAQRKEEEAERK-QLQ-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1568 hvAAQQSAAAELRSKQMSFAEnvskLEESLKQEHGTVLQLQQDAERLrkqqedaenareeaerelekwRQKANEAlrLRL 1647
Cdd:pfam07888 178 --AKLQQTEEELRSLSKEFQE----LRNSLAQRDTQVLQLQDTITTL---------------------TQKLTTA--HRK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1648 QAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAeeSALKQRDMAENELERQRRLAestAQQKLAAEQELIRLRADFDNAE 1727
Cdd:pfam07888 229 EAENEALLEELRSLQERLNASERKVEGLGEELS--SMAAQRDRTQAELHQARLQA---AQLTLQLADASLALREGRARWA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1728 QQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEmdiliqlksRAEKETMSNTEKSKQLLEAEATKlRDLAEEASKL 1807
Cdd:pfam07888 304 QERETLQQSAEADKDRIEKLSAELQRLEERLQEERME---------REKLEVELGREKDCNRVQLSESR-RELQELKASL 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1655274923 1808 RAIAEEakhQRQLAEEdaARQRAEAERILKEKLAAISDA 1846
Cdd:pfam07888 374 RVAQKE---KEQLQAE--KQELLEYIRQLEQRLETVADA 407
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1739-2485 |
8.64e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1739 RLKNEVIAAQQERKQLEDELSKVRSEM--------DILIQLKSRAEKETMSNTE------KSKQL---LEAEATKLRDLA 1801
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELknkekelkNLDKNLNKDEEKINNSNNKikileqQIKDLndkLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1802 EEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEaeiaLKEKEAENERLRRQAEDEAYQRKIL 1881
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1882 EDQanqhKLEIEEKIvllkkssdaemerqkaivDDTLKQRRVVEEEIRILKLNFEKASSgkldLELELNKLKNiaeetQQ 1961
Cdd:TIGR04523 179 EKE----KLNIQKNI------------------DKIKNKLLKLELLLSNLKKKIQKNKS----LESQISELKK-----QN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1962 SKLraEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAE---KQIV 2038
Cdd:TIGR04523 228 NQL--KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnNQKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2039 AAQQAALKCNMAEQQVQSVLAQQKEDSMMQ--NKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQE 2116
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2117 AANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakHKKLAEQTLKQKFQV---EQELTKVKLQLEETDKQ 2193
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKE---IERLKETIIKNNSEIkdlTNQDSVKELIIKNLDNT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2194 KSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKflVEEAENMKKlaedaa 2273
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK--IEKLESEKK------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2274 rlSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEasrLKAEAEMLQRqkdlAQEQAQKLLEDKQLMQQRLDEET 2353
Cdd:TIGR04523 535 --EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKK----KQEEKQELIDQKEKEKKDLIKEI 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2354 EEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVkkmefeklnt 2433
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI---------- 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2434 skeaDDLRKAITELEKEK-ARLKKEAEEH-QNKSKEMADAQQKQIEREMTVLQQ 2485
Cdd:TIGR04523 676 ----DDIIELMKDWLKELsLHYKKYITRMiRIKDLPKLEEKYKEIEKELKKLDE 725
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1524-1953 |
8.91e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 52.36 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1524 AERKAANEK----QKALEDLENLRMQAeeaeRQVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSfaenvSKLeesLKQ 1599
Cdd:PRK10929 58 EERKGSLERakqyQQVIDNFPKLSAEL----RQQLNNERDEPRSVP----PNMSTDALEQEILQVS-----SQL---LEK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1600 EHgtvlQLQQDAERLRK---------QQEDAEnareeaerelekwRQKANEALRlRLQA-------EEEAHKKSLaqeea 1663
Cdd:PRK10929 122 SR----QAQQEQDRAREisdslsqlpQQQTEA-------------RRQLNEIER-RLQTlgtpntpLAQAQLTAL----- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1664 ekqkeeadreakkrsKAEESALKQRdmaENELErqrrLAESTAQQKlaaeQELIRLRAdfdnaeqqrslledELYrlkne 1743
Cdd:PRK10929 179 ---------------QAESAALKAL---VDELE----LAQLSANNR----QELARLRS--------------ELA----- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1744 viaaQQERKQLEDELSKVRSemdiliQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE 1823
Cdd:PRK10929 214 ----KKRSQQLDAYLQALRN------QLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1824 DAARQRAEAERILKEKLAaisdatrLKTEAEIA--LKEKEAENERLRRQAED--EAYQRKILEDQANQ---HKLEIEEki 1896
Cdd:PRK10929 284 IASQQRQAASQTLQVRQA-------LNTLREQSqwLGVSNALGEALRAQVARlpEMPKPQQLDTEMAQlrvQRLRYED-- 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1897 vLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLK 1953
Cdd:PRK10929 355 -LLNKQPQLRQIRQADGQPLTAEQNRILDAQLRTQRELLNSLLSGGDTLILELTKLK 410
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1735-2321 |
9.22e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1735 DELYRLKNEVIAAQQERKQLEDELSKVRS-------EMDILIQLKSRAEKETMSN-----TEKSKQLLEAEATKLRDLAE 1802
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEEIKKksenyidEIKAQINDLEDVADKAISNddpeeIEKKIENIVTKIDKKKNIYD 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1803 EASKL-RAIAEEAKHQRQLAE-----------------EDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAEN 1864
Cdd:TIGR01612 1191 EIKKLlNEIAEIEKDKTSLEEvkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEM 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1865 ERLRRQ-----AEDEAYQRKILEDQANQHKLEIEEKIvlLKKSSDAEMERQKAIVDDTLkQRRVVEEEIRILKLNFEKAS 1939
Cdd:TIGR01612 1271 DIKAEMetfniSHDDDKDHHIISKKHDENISDIREKS--LKIIEDFSEESDINDIKKEL-QKNLLDAQKHNSDINLYLNE 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1940 SGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLR-RLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKK 2018
Cdd:TIGR01612 1348 IANIYNILKLNKIKKIIDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKEL 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2019 ADEVRKQKEEADKEAEKQIVAAQQAALKCN---MAEQQVQSVLAQQKEDSMMQ-----NKLKEEYEKAKALARDAEAAKE 2090
Cdd:TIGR01612 1428 KNHILSEESNIDTYFKNADENNENVLLLFKnieMADNKSQHILKIKKDNATNDhdfniNELKEHIDKSKGCKDEADKNAK 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2091 RAEREAALLRQQaeeaeRQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKklaeqtl 2170
Cdd:TIGR01612 1508 AIEKNKELFEQY-----KKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIK------- 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2171 KQKFQVEQELTK--------VKLQLEETDKQKSLLddELQRLKDEVDDAMRQKASVEEELFKVKIQMEElMKLKvrieee 2242
Cdd:TIGR01612 1576 KEKFRIEDDAAKndksnkaaIDIQLSLENFENKFL--KISDIKKKINDCLKETESIEKKISSFSIDSQD-TELK------ 1646
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2243 nqrlMKKDKDNTQKFLVEEAENMKKLAEDAARlsiEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEA 2321
Cdd:TIGR01612 1647 ----ENGDNLNSLQEFLESLKDQKKNIEDKKK---ELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIES 1718
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2424-2601 |
9.96e-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: 51.88 E-value: 9.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2424 KKMEFEKLNTSKEADD-LRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTflTEKEMLLKKEKLiE 2502
Cdd:pfam15709 321 SKALLEKREQEKASRDrLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQR--RFEEIRLRKQRL-E 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2503 DEKKKLEsqfEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAalNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 2582
Cdd:pfam15709 398 EERQRQE---EEERKQRLQLQAAQERARQQQEEFRRKLQELQRK--KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMA 472
|
170
....*....|....*....
gi 1655274923 2583 NQKLREKLQQMEEAQKSTL 2601
Cdd:pfam15709 473 EEERLEYQRQKQEAEEKAR 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1058-1480 |
1.18e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.04 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1058 SATAPVLRSELE---LTVQKMDHayMLSSVYLEKLKTVEMVIRNTQGAEGVLKQYENCLREVHTVPNDVKEVETYRTnLK 1134
Cdd:pfam15921 411 SITIDHLRRELDdrnMEVQRLEA--LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELT-AK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1135 KMRAEAeAEQPVFD---SLEEELKKASAVSDKMSRVHSERDAELdQHRQHLSSLQDRWKAVFTQIDLRQRELDQLGRQLG 1211
Cdd:pfam15921 488 KMTLES-SERTVSDltaSLQEKERAIEATNAEITKLRSRVDLKL-QELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIE 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1212 YYRESYDWLIRWIADAKQRQENIQavpiTDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYK 1291
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQ----VEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAG 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1292 AQVEPLTSPLKKTKldsasDNIIQEYVTLRtrySELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELD 1371
Cdd:pfam15921 642 SERLRAVKDIKQER-----DQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1372 KQKQL--AEAHAKAIA-------------------------KAEKEAQELKLRMQEEVSK--RETAAVDAEKQKQNIQLE 1422
Cdd:pfam15921 714 TLKSMegSDGHAMKVAmgmqkqitakrgqidalqskiqfleEAMTNANKEKHFLKEEKNKlsQELSTVATEKNKMAGELE 793
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1423 LheLKNlSEQQIKDKSQQVDEAL-KSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR 1480
Cdd:pfam15921 794 V--LRS-QERRLKEKVANMEVALdKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2187-2623 |
1.28e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2187 LEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEelfkvkiqMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmK 2266
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDE--------LEALIDQWLAELEQVIALRRAGGLEAALALVRSGEG-K 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2267 KLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQ 2346
Cdd:COG5278 149 ALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2347 QRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKM 2426
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2427 EFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKK 2506
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2507 KLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKL 2586
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430
....*....|....*....|....*....|....*..
gi 1655274923 2587 REKLQQMEEAQKSTLITEKHVTVVETVLNGQNAGDVL 2623
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2153-2378 |
1.35e-05 |
|
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: 51.57 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2153 QQADEEMAKHKKLAEQTLKQ-KFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEvddaMRQkasVEEELFKVKIQMEE 2231
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEElQQQREEELEELQEQLEDLESSIQELEKEIKKLESS----IKQ---VEEELEELKEQNEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2232 LmklkvrieEENQRLMKKdkdnTQKFLVEEAENMKKL----AEDAARL-SIEAQ-EAARLRQIAEddlnqQRTLAEKMLK 2305
Cdd:pfam05667 382 L--------EKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHRVPLIEE-----YRALKEAKSN 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2306 EKMqaiqEASRLKAEAEMLQRQ-KDLAQEQAQKLLEDKQLMQQrLDEETEEYQRSleAERKRQLEIIAEAEKLK 2378
Cdd:pfam05667 445 KED----ESQRKLEEIKELREKiKEVAEEAKQKEELYKQLVAE-YERLPKDVSRS--AYTRRILEIVKNIKKQK 511
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1818-2042 |
1.37e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1818 RQLAEEDAARQRAEAERILKEklaAISDATRLKTEAEIALKEkeaENERLRRQAEDEAYQR----KILEDQANQHKLEIE 1893
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERrnelQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1894 EKIVLLKKSsDAEMERQKAIVDDTLKQRRVVEEEIRILKLNfekassgkldlelELNKLKNIAEETQqsklraeEEAEKL 1973
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEE-------------QLQELERISGLTA-------EEAKEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1974 RRLVLEEEMRRkEAEDKVKKIaaaeeeaarqrkaaqEEldrlqkkadevrKQKEEADKEAEKQIVAAQQ 2042
Cdd:PRK12704 159 LLEKVEEEARH-EAAVLIKEI---------------EE------------EAKEEADKKAKEILAQAIQ 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1790-2042 |
1.37e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1790 LEAEATKLRDLAEEASKLRAIAEEAKHQR-QLAEEDAARQRAEAERILKEKLAAISDATRLKTeAEIALKEKEAENERLR 1868
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIeLLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1869 RQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERqkaivddtlkqrrvVEEEIRilklnfekassgklDLELE 1948
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ--------------LEREIE--------------RLERE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1949 LNKLKNiaeetqqsklRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLqkKADEVRKQKEE 2028
Cdd:COG4913 354 LEERER----------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEA--EAALRDLRREL 421
|
250
....*....|....
gi 1655274923 2029 ADKEAEKQIVAAQQ 2042
Cdd:COG4913 422 RELEAEIASLERRK 435
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1636-2024 |
1.55e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.02 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1636 RQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAK---KRSKAEESALKQRdMAENELERQRRLAESTAQQKLaa 1712
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgQGGLDEEEAFLDR-TAKREERRQKRLQEALERQKE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1713 eqelirlradfdnaeqqrsllEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMSNTEKSKQLLEa 1792
Cdd:pfam02029 89 ---------------------FDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1793 eaTKLRDLAEEASKLRAIAEEAKHQRqlaEEDAARQRAEAERILKEKlaaisdatRLKTEAEIALKEKEAENERLRRQAE 1872
Cdd:pfam02029 147 --TEVRQAEEEGEEEEDKSEEAEEVP---TENFAKEEVKDEKIKKEK--------KVKYESKVFLDQKRGHPEVKSQNGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1873 DEAYQRKILEDQANQHKLEIEEKivllKKSSDAEMERQKAIvdDTLKQRRVVEEEirilkLNFEKASSGKLDLELELNKL 1952
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQER----EEEAEVFLEAEQKL--EELRRRRQEKES-----EEFEKLRQKQQEAELELEEL 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1953 KNIAEEtqqsklraeeeaeklRRLVLEEEMRRKEAEDKVKKIaaAEEEAARQRKaaqEELDRLQKKADEVRK 2024
Cdd:pfam02029 283 KKKREE---------------RRKLLEEEEQRRKQEEAERKL--REEEEKRRMK---EEIERRRAEAAEKRQ 334
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1478-1734 |
1.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1478 QLRDRADAAEKLRKLAQEEAEKLRKQVSE-ETQKKRLAEEELKHKSEAERKAANEKQKALED-LENLRMQAEEAERQVKQ 1555
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEaEAALEEFRQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1556 AEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRkqqedaenareeaerelekw 1635
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALR-------------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1636 RQKANEALRLRLQAEeeahkkslaqeeaekqkeeadreakkrskAEESALKQRdmaENELERQRRLAESTAQQKLAAEQE 1715
Cdd:COG3206 305 AQLQQEAQRILASLE-----------------------------AELEALQAR---EASLQAQLAQLEARLAELPELEAE 352
|
250 260
....*....|....*....|
gi 1655274923 1716 LIRLRADFDNAEQQ-RSLLE 1734
Cdd:COG3206 353 LRRLEREVEVARELyESLLQ 372
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1686-1879 |
1.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRDMAENELERQRRLAESTA--QQKLAAEQEliRLRADfdnaEQQRslledelyrlknevIAAQQERKQLEDELSKVRS 1763
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEelQQKQAAEQE--RLKQL----EKER--------------LAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1764 EmdiliqlKSRAEKETMSNTEKSKQLLEAEATKLRDLA---EEASKLRAIAEEAKHQRQLAEEDA-----------ARQR 1829
Cdd:PRK09510 130 K-------QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAkkaAAEAKKKAEAEAAKKAAAEAKKKAeaeaaakaaaeAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1830 AEAERilKEKLAAISD---ATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1879
Cdd:PRK09510 203 AEAEA--KKKAAAEAKkkaAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1473-1840 |
1.70e-05 |
|
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: 50.30 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1473 EDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAE----EELKHKSEAERKAANEKQKALEDLENLRMQAEE 1548
Cdd:pfam13868 5 SDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEmmeeERERALEEEEEKEEERKEERKRYRQELEEQIEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1549 AERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQehgtvLQLQQDAERLRKQQEDAENAREEA 1628
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEF-----NEEQAEWKELEKEEEREEDERILE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1629 ERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEaekqkeeadrEAKKRSKAEESALKQRDMAENELERQRRLAESTAQQ 1708
Cdd:pfam13868 160 YLKEKAEREEEREAEREEIEEEKEREIARLRAQQ----------EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1709 KLAAEQELIRLRadfdnaeqqrslleDELYRLKNEVIAAQQERKQLEDELskvrsemdiLIQLKSRAEKETMSNTEKSKQ 1788
Cdd:pfam13868 230 KARQRQELQQAR--------------EEQIELKERRLAEEAEREEEEFER---------MLRKQAEDEEIEQEEAEKRRM 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1789 LLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKL 1840
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3705-3741 |
2.00e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 2.00e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 3705 LNLLETQAATGFIIDPIKNETLTVDEAVRKGVVGPEI 3741
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2186-2575 |
2.01e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2186 QLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELfkvKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENM 2265
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQW---ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2266 KKLAEDAARLSIEAQEAARLRQIAEDdlnqQRTLAEKMLKEKMqaiqEASRLKAEAEMLQRQKdlAQEQAQKllEDKQLM 2345
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKERAKKAGAQR--KEEEAER--KQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2346 QQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAkaeeeakkfkkqadtiAARLHETEI-ATKEQMTEVK 2424
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT----------------TAHRKEAENeALLEELRSLQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2425 kmefEKLNTSKEA-----DDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQ------QKQIEREMTVLQQTFLTEKEM 2493
Cdd:pfam07888 244 ----ERLNASERKveglgEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASlalregRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2494 LLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELerKRL 2573
Cdd:pfam07888 320 IEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYI--RQL 397
|
..
gi 1655274923 2574 EQ 2575
Cdd:pfam07888 398 EQ 399
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1686-2021 |
2.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM 1765
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1766 DILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ----LAEEDAARQRAEAERILKEKLA 1841
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEelaaLEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1842 AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQR 1921
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1922 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEA 2001
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1655274923 2002 ARQRKAAQEELDRLQKKADE 2021
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1795-2110 |
2.05e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1795 TKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDE 1874
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1875 AYQRKILEDQANQHK---LEIEEKIVLLKKSS---DAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELE 1948
Cdd:pfam07888 114 SEEKDALLAQRAAHEariRELEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1949 LNKLKNIAEETQQSKLRAEEEAEKLRRLVleEEMRRKEAEDKVKKiaaaeeeaaRQRKAAQEELDRLQKKADEVRKQKEE 2028
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKL--TTAHRKEAENEALL---------EELRSLQERLNASERKVEGLGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2029 ADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEeyekakALARDAEAAKERAEREAALLRQ-----QA 2103
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERE------TLQQSAEADKDRIEKLSAELQRleerlQE 336
|
....*..
gi 1655274923 2104 EEAERQK 2110
Cdd:pfam07888 337 ERMEREK 343
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1119-1293 |
2.07e-05 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 48.98 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1119 VPNDVKEVETYRTNLKKMRAEAEAEQPVFDSLEEElkkasavSDKMSRVHSErdaELDQHRQHLSSLQDRWKAVFTQIDL 1198
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNEL-------GEQLIEEGHP---DAEEIQERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1199 RQRELDQLGRQLGYYRESYDwLIRWIADAKQRQENIQavPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYID 1278
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1655274923 1279 IIKDYELQLVAYKAQ 1293
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2293-2615 |
2.15e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.12 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2293 LNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLqrqKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERK--RQLEI 2370
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLL---TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltQKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2371 IAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIAT-KEQMTEVKKMEFEKLNTSKEADDLRKAIteLEK 2449
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAhIKAVTQIEQQAQRIHTELQSKMRSRAKL--LMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2450 EKARLKKEAEEHQNKS---------KEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAK 2520
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRllqtlhsqeIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2521 ALKDEQDRQRQQMEEEKLKLKATMDAalnKQKEAEKDILNKQKEMQELERKRLEQERVladeNQKLREKLQQMEEAQKST 2600
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTAQCEKLEKIHLQES----AQSLKEREQQLQTKEQIH 482
|
330
....*....|....*
gi 1655274923 2601 LITEKHVTVVETVLN 2615
Cdd:TIGR00618 483 LQETRKKAVVLARLL 497
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
183-260 |
2.19e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.14 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 183 DNFTTSWRDGKLFNAVIHK------NYPRLIdmgkvyRQTNLENLEQAFNvAEKDLGVTRLLDPEDVDVPHPDEKSIITY 256
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNAlggsvpGWPNLD------PEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAY 92
|
....
gi 1655274923 257 VSSL 260
Cdd:cd21185 93 AAQL 96
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1496-2107 |
2.20e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1496 EAEKLRKQVSEETQKKRLAEEELKHKS---EAERKAANEKQKAledlenlrmqAEEAERQvkqaeveKERQIQVAHVAAQ 1572
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRariELEKKASALKRQL----------DRESDRN-------QELQKRIRLLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1573 QSAAAELRSKQMsfaenvskleeslkqehgtvlqlqqdaerlrkqqedaenareeaerelekwrqkanEALRLRLQAEEE 1652
Cdd:pfam05557 64 EAEAEEALREQA--------------------------------------------------------ELNRLKKKYLEA 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1653 AHKKslaqEEAEKQKEEADREAKKRSKAEESALKQrdmaenELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSL 1732
Cdd:pfam05557 88 LNKK----LNEKESQLADAREVISCLKNELSELRR------QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1733 LEDELYRLKneviAAQQERKQLEDELSKvrSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRaiAE 1812
Cdd:pfam05557 158 LEKQQSSLA----EAEQRIKELEFEIQS--QEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLK--EE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1813 EAKHQRQLAEEDAARQRAEAERILKEKLAA-------ISDATRLKTEAEIALKEK--EAENERLRRQAEDEAYQRKILED 1883
Cdd:pfam05557 230 VEDLKRKLEREEKYREEAATLELEKEKLEQelqswvkLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQL 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1884 QANQHKLEIeEKIVLLKKSSDAEM--ERQKAIVDDTLKQRRVVEEEIRILK---------LNFEKASSGKLDLELELNKL 1952
Cdd:pfam05557 310 EKARRELEQ-ELAQYLKKIEDLNKklKRHKALVRRLQRRVLLLTKERDGYRailesydkeLTMSNYSPQLLERIEEAEDM 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1953 ------KNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKaaqeELDRLQKKADEVRKQK 2026
Cdd:pfam05557 389 tqkmqaHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRR----KLETLELERQRLREQK 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2027 EEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKER-----------AERE 2095
Cdd:pfam05557 465 NELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQvlrlpettstmNFKE 544
|
650
....*....|..
gi 1655274923 2096 AALLRQQAEEAE 2107
Cdd:pfam05557 545 VLDLRKELESAE 556
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2167-2524 |
2.21e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2167 EQTLKQKFQVEQELTKVKLQLEETDKQK-----SLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEE 2241
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2242 ENQRLMKKDKDNTQKFLVEEAENMKKLaEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEA 2321
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2322 EMLQRQ-KDLAQEQAQKLLEDKQL------MQQRLDEETEEY---QRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKA 2391
Cdd:TIGR04523 436 IKNNSEiKDLTNQDSVKELIIKNLdntresLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2392 EEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFE--KLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 2469
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKE 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2470 DAQQ---KQIEREMTVL----QQTFLTEKE----------MLLKKEKL------IEDEKKKLESQFEEEIKKAKALKD 2524
Cdd:TIGR04523 596 KEKKdliKEIEEKEKKIssleKELEKAKKEneklssiiknIKSKKNKLkqevkqIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2422-2590 |
2.43e-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: 48.77 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2422 EVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQI--EREMTVLQQtfltEKEMLLKKEK 2499
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVrnNKEYEALQK----EIESLKRRIS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2500 LIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEeklklkatmdaalnKQKEAEKDILNKQKEMQELERKRLEQERVL 2579
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEE--------------KKAELDEELAELEAELEELEAEREELAAKI 172
|
170
....*....|.
gi 1655274923 2580 ADENQKLREKL 2590
Cdd:COG1579 173 PPELLALYERI 183
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
41-149 |
2.50e-05 |
|
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: 46.52 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSqrHVTDLYEDLRDGHNLISLLEV---------LSGDTLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNP--YVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 112 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1420-1756 |
2.62e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1420 QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAeklrklaQEEAEK 1499
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL-------EEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1500 LRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAEL 1579
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1580 RSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAHKKSLA 1659
Cdd:COG4372 165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1660 QEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYR 1739
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
330
....*....|....*..
gi 1655274923 1740 LKNEVIAAQQERKQLED 1756
Cdd:COG4372 325 AKKLELALAILLAELAD 341
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1343-1446 |
2.66e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1343 RRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHA-KAIAKAEKEAQELKLRMQEevSKRETAAVDAEKQKQNIQL 1421
Cdd:PRK00409 537 EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAqQAIKEAKKEADEIIKELRQ--LQKGGYASVKAHELIEARK 614
|
90 100
....*....|....*....|....*
gi 1655274923 1422 ELHElKNLSEQQIKDKSQQVDEALK 1446
Cdd:PRK00409 615 RLNK-ANEKKEKKKKKQKEKQEELK 638
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
45-146 |
2.72e-05 |
|
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: 46.64 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRF----HKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHF 146
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2185-2367 |
2.81e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 50.37 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2185 LQLEETDKqkSLLDDELQRLKDEVDDAMRQKASveeelfkvkiqmeelmklkvriEEENQRLMKKDKDNTQKFLVEEAEN 2264
Cdd:pfam13779 477 LRIEDGDL--SDAERRLRAAQERLSEALERGAS----------------------DEEIAKLMQELREALDDYMQALAEQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2265 MKKLAEDAARLSIEAQeaarlRQIAEDDLnqqrtlaEKMlkekMQAIQEASRL--KAEA-EML---------------QR 2326
Cdd:pfam13779 533 AQQNPQDLQQPDDPNA-----QEMTQQDL-------QRM----LDRIEELARSgrRAEAqQMLsqlqqmlenlqagqpQQ 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1655274923 2327 QKDLAQEQAQKLLEDKQLM---QQRLDEETeeyQRSLEAERKRQ 2367
Cdd:pfam13779 597 QQQQGQSEMQQAMDELGDLlreQQQLLDET---FRQLQQQGGQQ 637
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1342-1582 |
2.87e-05 |
|
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: 49.53 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAEKLKA--EEQKKMAEMQAELDKQ-KQLAEAHAKAIAKAEKEAQELKLRMQEEVSK---RETAAVDAEKQ 1415
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKLEKQRQLREeidEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1416 KQNIQLELHELKNLseQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQE 1495
Cdd:pfam13868 145 LEKEEEREEDERIL--EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1496 EAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQvkqaEVEKERQIQVAHVAAQQSA 1575
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE----EAEKRRMKRLEHRRELEKQ 298
|
....*..
gi 1655274923 1576 AAELRSK 1582
Cdd:pfam13868 299 IEEREEQ 305
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4115-4143 |
2.88e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 2.88e-05
10 20
....*....|....*....|....*....
gi 1655274923 4115 VRKRRVVIVDPETGKEMTVYEAYRKGLID 4143
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1591-1915 |
2.93e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.28 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1591 SKLEESLkQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKwrqkaneALRLRLQAEEEAHKKSLAQEEAEKQKEEA 1670
Cdd:pfam07888 34 NRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWERQRR-------ELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1671 DREAKKRSKAEESALKqrDMAENELERQRRLAE---STAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAA 1747
Cdd:pfam07888 106 LSASSEELSEEKDALL--AQRAAHEARIRELEEdikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1748 QQERKQLEDELSKVRSEMD----ILIQLKSRAEKETMSNTEKSKQLLEAEATK--LRDLAEEASKLRAIAEEAKhqRQLA 1821
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLeeLRSLQERLNASERKVEGLG--EELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1822 EEDAARQRAEAErILKEKLAAISDATRLkTEAEIALKEKEA----ENERLRRQAEDEayQRKILEDQANQHKLEieekiv 1897
Cdd:pfam07888 262 SMAAQRDRTQAE-LHQARLQAAQLTLQL-ADASLALREGRArwaqERETLQQSAEAD--KDRIEKLSAELQRLE------ 331
|
330
....*....|....*...
gi 1655274923 1898 llKKSSDAEMERQKAIVD 1915
Cdd:pfam07888 332 --ERLQEERMEREKLEVE 347
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1546-1976 |
3.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1546 AEEAERQVKQA-EVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQ--EHgtvLQLQQDAERLRKQQEDAE 1622
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasDH---LNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1623 NAREeaerelekwrqKANEALRLRLQAEEEAHkkslaqeeaekqKEEADREAKKRSkAEESAlkqrDMAENEL-ERQRRL 1701
Cdd:PRK04863 355 ADLE-----------ELEERLEEQNEVVEEAD------------EQQEENEARAEA-AEEEV----DELKSQLaDYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1702 aesTAQQKLA-----AEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS---KVRSEMDILIQLKS 1773
Cdd:PRK04863 407 ---DVQQTRAiqyqqAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSvaqAAHSQFEQAYQLVR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1774 RAEKETMSNT--EKSKQLLEaEATKLRDLAEEASKLRAIAEEAKhQRQLAEEDAARQRAEAERILKEKLAAISDATRLkt 1851
Cdd:PRK04863 484 KIAGEVSRSEawDVARELLR-RLREQRHLAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1852 eaeiaLKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEkivLLKKS-----SDAEMERQKAIVDDTLKQRRVVEE 1926
Cdd:PRK04863 560 -----QEELEARLESLSESVSEARERRMALRQQLEQLQARIQR---LAARApawlaAQDALARLREQSGEEFEDSQDVTE 631
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1927 EIRILKLNFEKASSGKLDLELELNKLKNIAEETQQsklRAEEEAEKLRRL 1976
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNAL 678
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1891-2207 |
3.13e-05 |
|
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: 49.53 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1891 EIEEKIVLLKKSSDAEMERQKAIVDDTLKQR-RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLR-AEE 1968
Cdd:pfam13868 23 ERDAQIAEKKRIKAEEKEEERRLDEMMEEEReRALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1969 EAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE------VRKQKEEADKEAEKQIVAAQQ 2042
Cdd:pfam13868 103 MDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDErileylKEKAEREEEREAEREEIEEEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2043 AALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEkAKALARDAEAAKERAEREAALLRQQAEEAERQKvaaeqEAANQAK 2122
Cdd:pfam13868 183 EREIARLRAQQEKAQDEKAERDELRAKLYQEEQE-RKERQKEREEAEKKARQRQELQQAREEQIELKE-----RRLAEEA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2123 AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQ 2202
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
....*
gi 1655274923 2203 RLKDE 2207
Cdd:pfam13868 337 KKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2505-2614 |
3.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2505 KKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLkLKATmDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQ 2584
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|
gi 1655274923 2585 KLREKLQQMEEAQKSTLITEKHVTVVETVL 2614
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEEL 133
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
46-153 |
3.46e-05 |
|
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: 46.93 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1655274923 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 153
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1334-1910 |
3.47e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1334 YIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKqlaeaHAKAIAKAEKEAQELKLRMQEEVSKretaavdAE 1413
Cdd:PRK01156 195 SNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESEIKT-------AE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1414 KQKQNIQLELHELKNLSEQQIKDKSqqvDEALKSRLRIEEEIHLIRiQLETTVKQKSNAEDELKQLRDradaaeklrklA 1493
Cdd:PRK01156 263 SDLSMELEKNNYYKELEERHMKIIN---DPVYKNRNYINDYFKYKN-DIENKKQILSNIDAEINKYHA-----------I 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1494 QEEAEKLRKQVSEETQKKRlAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQ--AEVEKERQIQVAHVAA 1571
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKS-RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsAFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1572 QQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEAL-RLRLQAE 1650
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKsRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1651 EEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRA--------- 1721
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkledldsk 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1722 --DFDNAEQQRSLLEDELYRLKNEVIAAQQerKQLEDELSKVRSEMDiliqlksraekETMSNTEKSKQLLEAEATKLRD 1799
Cdd:PRK01156 567 rtSWLNALAVISLIDIETNRSRSNEIKKQL--NDLESRLQEIEIGFP-----------DDKSYIDKSIREIENEANNLNN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1800 LAEEASKLRAIAEEAKHQRQLAEEDAARQRaEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRK 1879
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
570 580 590
....*....|....*....|....*....|.
gi 1655274923 1880 ILEDQANQHKLEIEEKIVLLKKSSDAEMERQ 1910
Cdd:PRK01156 713 ELSDRINDINETLESMKKIKKAIGDLKRLRE 743
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2004-2592 |
3.88e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.18 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2004 QRKAAQEELDRLQKKADEVRKQKEE----------ADKEAEKQIVAAQQAalkcnmaEQQVQSVLAQQKEdsmmqnkLKE 2073
Cdd:PRK10246 192 QHKSARTELEKLQAQASGVALLTPEqvqsltaslqVLTDEEKQLLTAQQQ-------QQQSLNWLTRLDE-------LQQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2074 EYEKAKALARDAEAAKERAEREAALL--------------RQQAEEAE----RQKVAAEQEAANQAKAQddAERLRKDAE 2135
Cdd:PRK10246 258 EASRRQQALQQALAAEEKAQPQLAALslaqparqlrphweRIQEQSAAlahtRQQIEEVNTRLQSTMAL--RARIRHHAA 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2136 FEAAKLAQAEAAALKQKQQADEEMAKHKKLA--EQTLKQKFQVEQELTKVKLQL-EETDKQKSLLDDELQRLKDEVDDAM 2212
Cdd:PRK10246 336 KQSAELQAQQQSLNTWLAEHDRFRQWNNELAgwRAQFSQQTSDREQLRQWQQQLtHAEQKLNALPAITLTLTADEVAAAL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2213 RQKAS---VEEELFKVKIQMEELMKLKVRIEEENQRL-------------MKKD-KDNTQKF-----LVEEAENMKKLAE 2270
Cdd:PRK10246 416 AQHAEqrpLRQRLVALHGQIVPQQKRLAQLQVAIQNVtqeqtqrnaalneMRQRyKEKTQQLadvktICEQEARIKDLEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2271 DAARL---------------SIEAQEAARLrqiaedDLNQQRTLAekMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQA 2335
Cdd:PRK10246 496 QRAQLqagqpcplcgstshpAVEAYQALEP------GVNQSRLDA--LEKEVKKLGEEGAALRGQLDALTKQLQRDESEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2336 QKLLEDkqlmQQRLDEETEEYQRSLEAERKRQLEI---IAEAEKLKLQVSQLSEAQAKAEeeakkfkkqadTIAArlHET 2412
Cdd:PRK10246 568 QSLRQE----EQALTQQWQAVCASLNITLQPQDDIqpwLDAQEEHERQLRLLSQRHELQG-----------QIAA--HNQ 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2413 EIATKEQMTEVKKMEFEKlntskEADDLRKAITELEKEKARL---KKEAEEHQNKSKEMADAQQK--QIEREMTVLQQTF 2487
Cdd:PRK10246 631 QIIQYQQQIEQRQQQLLT-----ALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRiqQLTPLLETLPQSD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2488 LTEKE---MLLKKEKLIEDEKKKLESQFEeeikkakALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEA-------EKD 2557
Cdd:PRK10246 706 DLPHSeetVALDNWRQVHEQCLSLHSQLQ-------TLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAflaalldEET 778
|
650 660 670
....*....|....*....|....*....|....*
gi 1655274923 2558 ILNKQKEMQELERKRLEQERVLADENQKLREKLQQ 2592
Cdd:PRK10246 779 LTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1526-1770 |
4.23e-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: 49.07 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1526 RKAANEKQKALEDLENLRMQAEEAERQvKQAEVEKERQIQVAHVAAQQSAAAELRSKQmsfAENVSKLEESLKQehgtvl 1605
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQ-RAAEQARQKELEQRAAAEKAAKQAEQAAKQ---AEEKQKQAEEAKA------ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1606 qlQQDAERLRKQQEDAEnareeaerelekwRQKANEALRlrlQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESAL 1685
Cdd:TIGR02794 127 --KQAAEAKAKAEAEAE-------------RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1686 KQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEM 1765
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAII 268
|
....*
gi 1655274923 1766 DILIQ 1770
Cdd:TIGR02794 269 QQAIQ 273
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1325-1535 |
4.36e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1325 SELMTLTSQYIKFITD---TQRRLEDEEKAAE---KLKAEEQKKMAEM---QAELDKQKQLA-----EAHAKAIaKAEKE 1390
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAEAdrqRLEQEKQQQLAAIsgsQSQLESTDQNAletngQAQRDAI-LEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1391 A--QELKLRMQ--EEVSKRETAAVD---------AEKQKQNIQLELHELKNLS-------EQQIKDKSQQVDEALKsrlr 1450
Cdd:NF012221 1617 AvtKELTTLAQglDALDSQATYAGEsgdqwrnpfAGGLLDRVQEQLDDAKKISgkqladaKQRHVDNQQKVKDAVA---- 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1451 ieeeihliriQLETTVKQ----KSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEelKHKSEAER 1526
Cdd:NF012221 1693 ----------KSEAGVAQgeqnQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGE--QDASAAEN 1760
|
....*....
gi 1655274923 1527 KAANEKQKA 1535
Cdd:NF012221 1761 KANQAQADA 1769
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3982-4013 |
4.52e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.52e-05
10 20 30
....*....|....*....|....*....|..
gi 1655274923 3982 KLLSAERAVTGYRDPYTGKTISLFQAMKKGLI 4013
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3081-3117 |
4.70e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.70e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 3081 KLLSAERAVTGYRDPYTGKTVSLFQAMKKDLIPKEQG 3117
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1283-1762 |
5.03e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 49.58 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1283 YELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKK 1362
Cdd:COG4995 6 LLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1363 MAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVD 1442
Cdd:COG4995 86 ALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1443 EALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKS 1522
Cdd:COG4995 166 LALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1523 EAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHG 1602
Cdd:COG4995 246 AAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1603 TVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEEEAhkkslaqeeaekqkeEADREAKKRSKAEE 1682
Cdd:COG4995 326 LLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLA---------------LLLEALLLLLLALL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1683 SALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELY---RLKNEVIAaqqerkQLEDELS 1759
Cdd:COG4995 391 AALLLLAAALLALAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYafvQLYQLLIA------PIEAELP 464
|
...
gi 1655274923 1760 KVR 1762
Cdd:COG4995 465 GIK 467
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
46-143 |
5.20e-05 |
|
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: 46.12 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVN---------KHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPR----EKGRMRFHKLQNVQIALDFL 112
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1655274923 113 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1713-2106 |
5.56e-05 |
|
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: 49.44 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1713 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDiliqlksraEKETMSNtEKSKQLLE- 1791
Cdd:pfam10174 302 ESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLE---------EKESFLN-KKTKQLQDl 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1792 --------AEATKLRDLAEeaSKLRAIAEEAKHQRQLAEE--DAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKE 1861
Cdd:pfam10174 372 teekstlaGEIRDLKDMLD--VKERKINVLQKKIENLQEQlrDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1862 AENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLL------KKSSDAEM-ERQKAIVDDTLKQrrvvEEEIRILKLN 1934
Cdd:pfam10174 450 RIIERLKEQREREDRERLEELESLKKENKDLKEKVSALqpelteKESSLIDLkEHASSLASSGLKK----DSKLKSLEIA 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1935 FEKASSGKLDLELELNKLKNIAEETQQSklraEEEAEKLRRLVLE-----EEMRRKEAE----------------DKVKK 1993
Cdd:pfam10174 526 VEQKKEECSKLENQLKKAHNAEEAVRTN----PEINDRIRLLEQEvarykEESGKAQAEverllgilreveneknDKDKK 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1994 IAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMmqnKLKE 2073
Cdd:pfam10174 602 IAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDAT---KARL 678
|
410 420 430
....*....|....*....|....*....|...
gi 1655274923 2074 EYEKAKALARDAEAAKERAEReaallRQQAEEA 2106
Cdd:pfam10174 679 SSTQQSLAEKDGHLTNLRAER-----RKQLEEI 706
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2430-2567 |
5.70e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.44 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2430 KLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKskemadaqqkqieremtvLQQTFLTEKEMLLKKEKLIEdEKKKLE 2509
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEAL------------------LKEAEKLKEELEEKKEKLQE-EEDKLL 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2510 SQFEEEIKKA-KALKDEQD------RQRQQMEEEKLKLKATMDA--ALNKQKEAEKDILNKQKEMQE 2567
Cdd:PRK00409 569 EEAEKEAQQAiKEAKKEADeiikelRQLQKGGYASVKAHELIEArkRLNKANEKKEKKKKKQKEKQE 635
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1848-2341 |
5.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1848 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKivllkKSSDAEMERQKAIVDDTLKQRRVVEEE 1927
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1928 IRILKLNFEKASsgkldLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKA 2007
Cdd:COG4717 125 LQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2008 AQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQ---------SVLAQQKEDSMMQNKLKEEYEKA 2078
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2079 KALARDAEAAKERAEREAALLRQQAEEAERQkvaAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEE 2158
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQAL---PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2159 MAKHKKLAEQTLKQKFQveQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELfKVKIQMEELMKLKVR 2238
Cdd:COG4717 357 EELEEELQLEELEQEIA--ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGEL-EELLEALDEEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2239 IEEENQRLMkkdkdntqkflvEEAENMKKLAEDAARLSieaqeaARLRQIAEDDLNQQRTLAEKMLKEKMQ-AIQEASRL 2317
Cdd:COG4717 434 LEELEEELE------------ELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAAL 495
|
490 500
....*....|....*....|....*
gi 1655274923 2318 KAEAEMLQR-QKDLAQEQAQKLLED 2341
Cdd:COG4717 496 KLALELLEEaREEYREERLPPVLER 520
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1342-1578 |
6.00e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAaeklKAEEQKKMAEMQAELDKQkqlAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQL 1421
Cdd:PRK05035 459 QARLEREKAA----REARHKKAAEARAAKDKD---AVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1422 ELHELKNLSEqQIKDKSQQVDEALKsrlrieeeihliRIQLETTVKQKSNAEDELKQLRDRADAAEklrKLAQEEAEKLR 1501
Cdd:PRK05035 532 ARQAEKQAAA-AADPKKAAVAAAIA------------RAKAKKAAQQAANAEAEEEVDPKKAAVAA---AIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1502 KQVSEETQKKRLAEEELKhksEAERKAANEKQKALEdLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 1578
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPK---KAAVAAAIARAKAKK-AEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAE 668
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1405-1746 |
6.65e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1405 RETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRAD 1484
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1485 AAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQI 1564
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1565 QVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEA-L 1643
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEViL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1644 RLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADF 1723
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
330 340
....*....|....*....|...
gi 1655274923 1724 DNAEQQRSLLEDELYRLKNEVIA 1746
Cdd:COG4372 338 ELADLLQLLLVGLLDNDVLELLS 360
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1150-1583 |
7.03e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1150 LEEELKKASAVSDKmSRVHSERDAELDQHRQHLSS-LQD----RWKAVFTQIDLRQrELDQLGRQLGYYRESYDWLIRWI 1224
Cdd:pfam05483 263 LEESRDKANQLEEK-TKLQDENLKELIEKKDHLTKeLEDikmsLQRSMSTQKALEE-DLQIATKTICQLTEEKEAQMEEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1225 ADAKQRQENIQAVPITDSKTLKEQLAKEKKLLE-----------EIEKNKDKVDECQKYAKAyidiiKDYELQ------- 1286
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEknedqlkiitmELQKKSSELEEMTKFKNN-----KEVELEelkkila 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1287 ----LVAYKAQVEPLTSPLKKTKldsasdniiQEYV-TLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQK 1361
Cdd:pfam05483 416 edekLLDEKKQFEKIAEELKGKE---------QELIfLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLK 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1362 KMaEMQAELDKqkqLAEAHAKAIAKAEKEAQELKlRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQV 1441
Cdd:pfam05483 487 NI-ELTAHCDK---LLLENKELTQEASDMTLELK-KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1442 DEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETqkKRLAEEELK-H 1520
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN--KQLNAYEIKvN 639
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 1521 KSEAERKAANEK--------QKALEDL----ENLRMQAEEAERQVKQA-EVEKERQIQVAHVAAQQSAAAELRSKQ 1583
Cdd:pfam05483 640 KLELELASAKQKfeeiidnyQKEIEDKkiseEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2152-2416 |
7.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2152 KQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAmrqkasvEEELFKVKIQMEE 2231
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2232 LMklkvrieeenqRLMKKDKDNTQKF-----------LVEEAENMKKLAEDAARLsIEAQEAARlrqiaeDDLNQQRTLA 2300
Cdd:COG3883 91 RA-----------RALYRSGGSVSYLdvllgsesfsdFLDRLSALSKIADADADL-LEELKADK------AELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEASRLKAEaemLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 2380
Cdd:COG3883 153 EAKLAELEALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274923 2381 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIAT 2416
Cdd:COG3883 230 AAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2214-2474 |
7.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2214 QKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKfLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDL 2293
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2294 NQQRTLAEKMLKeKMQAIQEASRLKaeaeMLQRQKDLAQeqAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAE 2373
Cdd:COG4942 100 EAQKEELAELLR-ALYRLGRQPPLA----LLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2374 AEKLKLQVSQLseaqakaeeeakkfkkqadtiAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKAR 2453
Cdd:COG4942 173 RAELEALLAEL---------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250 260
....*....|....*....|.
gi 1655274923 2454 LKKEAEEHQNKSKEMADAQQK 2474
Cdd:COG4942 232 LEAEAAAAAERTPAAGFAALK 252
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2070-2277 |
7.68e-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: 48.85 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2070 KLKEEYEKAKALARDAEAAKERAEREAALLRQQ-AEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaa 2148
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQlKEELDKKQIDADKAQQKADFAQDNADKQRDEVR------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2149 lkQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKqksllDDELQRLKDEVDDAMRQKASVEEelfkvkiQ 2228
Cdd:pfam05262 252 --QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEIKKN-----DEEALKAKDHKAFDLKQESKASE-------K 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1655274923 2229 MEElmklkvRIEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLSI 2277
Cdd:pfam05262 318 EAE------DKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1672-1877 |
8.67e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 49.06 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAEN-----ELERQRRLA---------ESTAQQKLAAeqelirlradfdNAEQQRSLLEDEL 1737
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEAdrqrlEQEKQQQLAaisgsqsqlESTDQNALET------------NGQAQRDAILEES 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1738 YRLKNEVIAAQQERKQLEDE-------------------LSKVRSEMDiliqlksRAEKETMSNTEKSKQLLEAEATKLR 1798
Cdd:NF012221 1616 RAVTKELTTLAQGLDALDSQatyagesgdqwrnpfagglLDRVQEQLD-------DAKKISGKQLADAKQRHVDNQQKVK 1688
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1799 DlaeEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQ 1877
Cdd:NF012221 1689 D---AVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQ 1764
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3375-3408 |
9.08e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 9.08e-05
10 20 30
....*....|....*....|....*....|....
gi 1655274923 3375 LLEAQAASGFIVDPVKNQCLSVDEAVKSGVVGPE 3408
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1905-2359 |
9.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1905 AEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELnKLKNIAEETQQSKLRAEEEAEKLRRLvleeEMRR 1984
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEEL----EERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1985 KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAqQKED 2064
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE-QLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2065 SMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQA 2144
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2145 EAAALKQKQQADEEMAKhKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKsllddELQRLKDEVDDAMRQ-KASVEEELF 2223
Cdd:COG4717 315 ELEEEELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEEL-----QLEELEQEIAALLAEaGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2224 KVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAENmkkLAEDAARLSIEAQEAARLRqiaeDDLNQQRTLAEKM 2303
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---LEEELEELEEELEELEEEL----EELREELAELEAE 461
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 2304 LKEkMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLledkQLMQQRLDEETEEYQRS 2359
Cdd:COG4717 462 LEQ-LEEDGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREE 512
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1338-1831 |
9.64e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1338 ITDTQRRLEDEEKAAEKLKAEEqkkMAEMQAELDKQK----QLAEAHAKAIAKAEKEAQ--ELKLRMQEEVSKRETAAVD 1411
Cdd:PRK10246 389 LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQRplrqRLVALHGQIVPQQKRLAQlqVAIQNVTQEQTQRNAALNE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1412 AEKQKQNIQLELHELKNLSEQQIKDKSQqvdEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRdrADAAEKLRK 1491
Cdd:PRK10246 466 MRQRYKEKTQQLADVKTICEQEARIKDL---EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSR--LDALEKEVK 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1492 LAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAER----------KAANEKQKALEDLENLRMQAEEAERQVKQAEVEKE 1561
Cdd:PRK10246 541 KLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQaltqqwqavcASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHE 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1562 RQIQVA-HVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRkqqedaenareeaereleKWRQKAN 1640
Cdd:PRK10246 621 LQGQIAaHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQ------------------SWQQRQN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1641 EALRLRLQAEEEAHKKSLAQEEAEKQKEEAD------REAKKRSKAEESALKQrdMAENELERQRRLAESTAQQKLAAEQ 1714
Cdd:PRK10246 683 ELTALQNRIQQLTPLLETLPQSDDLPHSEETvaldnwRQVHEQCLSLHSQLQT--LQQQDVLEAQRLQKAQAQFDTALQA 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1715 ELIRLRADFDNA---EQQRSLLEDELYRLKNEVIAAQ----QERKQLEDELSKVRSEMDiliqlksraekeTMSNTEKSK 1787
Cdd:PRK10246 761 SVFDDQQAFLAAlldEETLTQLEQLKQNLENQRQQAQtlvtQTAQALAQHQQHRPDGLD------------LTVTVEQIQ 828
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1655274923 1788 QLLEAEATKLRDLA----EEASKLRAIAEEAKHQRQL-AEEDAARQRAE 1831
Cdd:PRK10246 829 QELAQLAQQLRENTtrqgEIRQQLKQDADNRQQQQALmQQIAQATQQVE 877
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1713-1863 |
9.73e-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: 47.23 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1713 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQL--L 1790
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEYeaL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1791 EAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRlKTEAEIALKEKEAE 1863
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA-ELEAELEELEAERE 166
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1441-1557 |
9.90e-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: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1441 VDEALkSRLRIEeeihliriqLETTVKQKSNAEDELKQLRDRADAAEKLRKLA-QEEAEKLRKQvsEETQKKRLaeEELK 1519
Cdd:COG0542 395 IDEAA-ARVRME---------IDSKPEELDELERRLEQLEIEKEALKKEQDEAsFERLAELRDE--LAELEEEL--EALK 460
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274923 1520 HKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAE 1557
Cdd:COG0542 461 ARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELE 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2269-2521 |
9.91e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2269 AEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQR 2348
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2349 LDEETEEYqrsleAERKRQLEIIAEAEKLKLQVSQlseaqakaeeeakKFKKQADTIAARLHETEIATKEQMTEVKkmef 2428
Cdd:COG4942 99 LEAQKEEL-----AELLRALYRLGRQPPLALLLSP-------------EDFLDAVRRLQYLKYLAPARREQAEELR---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2429 eklntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKL 2508
Cdd:COG4942 157 ------ADLAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|...
gi 1655274923 2509 ESQFEEEIKKAKA 2521
Cdd:COG4942 230 ARLEAEAAAAAER 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2005-2384 |
9.99e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2005 RKAAQEELDRLQKKADEVRK--QKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEYEKAKALA 2082
Cdd:PRK10929 60 RKGSLERAKQYQQVIDNFPKlsAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKS---RQAQQEQDRAREIS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2083 rDAeaakeraereAALLRQQAEEAERQkvaaeqeaanqakaQDDAERLRKdaefEAAKLAQAEAAALKQKQQAdeEMAKH 2162
Cdd:PRK10929 137 -DS----------LSQLPQQQTEARRQ--------------LNEIERRLQ----TLGTPNTPLAQAQLTALQA--ESAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2163 K-KLAEQTLKQ-KFQVEQELTKVKLQLEEtdKQKSLLDDELQRLKDEVDDAMRQKAsvEEELfkvkiqmeelmklkvrie 2240
Cdd:PRK10929 186 KaLVDELELAQlSANNRQELARLRSELAK--KRSQQLDAYLQALRNQLNSQRQREA--ERAL------------------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2241 eENQRLMKKDKDNTQKFLVEEAENMKKLAEDaarLSIEAQE----AARLRQIAEDDLNQQRTLAekMLKEKMQ------A 2310
Cdd:PRK10929 244 -ESTELLAEQSGDLPKSIVAQFKINRELSQA---LNQQAQRmdliASQQRQAASQTLQVRQALN--TLREQSQwlgvsnA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2311 IQEASRLKAE--AEMLQRQK---DLAQEQAQKLLEDKQLMQQRLDEE---------TEEYQRSLEAERKRQLEI------ 2370
Cdd:PRK10929 318 LGEALRAQVArlPEMPKPQQldtEMAQLRVQRLRYEDLLNKQPQLRQirqadgqplTAEQNRILDAQLRTQRELlnslls 397
|
410
....*....|....*....
gi 1655274923 2371 -----IAEAEKLKLQVSQL 2384
Cdd:PRK10929 398 ggdtlILELTKLKVANSQL 416
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2435-2595 |
1.01e-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: 47.23 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2435 KEADDLRKAITELEKEKARLKKEAEEHQNKSKEmADAQQKQIEREMTVLQQtfltekemllkkekLIEDEKKKLESqfee 2514
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEA--------------RIKKYEEQLGN---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2515 eIKKAKALK------DEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLRE 2588
Cdd:COG1579 85 -VRNNKEYEalqkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*..
gi 1655274923 2589 KLQQMEE 2595
Cdd:COG1579 164 EREELAA 170
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1246-1894 |
1.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1246 KEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKK-----TKLDSASDNIIQEyvtl 1320
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdkiNKLNSDLSKINSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1321 rtryselmtltsqyIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQEL---KLR 1397
Cdd:TIGR04523 112 --------------IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELeneLNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1398 MQEEVSKRETAAVDAEKQKQNIQLELHELKNLsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELK 1477
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKLELLLSNLKKK-IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1478 QLRDRADAAEKLRKLAQEEAEKLRKQVSE-ETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQA 1556
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKElEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1557 EVEKERQIqvahvaaqqsaaAELRSKQMSFAENVSKLEESLKQEhgtvlqlQQDAERLRKQQEDAENAREEAERELEKWR 1636
Cdd:TIGR04523 337 ISQLNEQI------------SQLKKELTNSESENSEKQRELEEK-------QNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1637 QKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEAdREAKKRSKAEESALKQRDMA-ENELERQRRLAESTAQQKLAAEQE 1715
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL-KETIIKNNSEIKDLTNQDSVkELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1716 LIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMS--------NTEKSK 1787
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkdDFELKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1788 QLLEAEatkLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIAlkekEAENERL 1867
Cdd:TIGR04523 557 ENLEKE---IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA----KKENEKL 629
|
650 660
....*....|....*....|....*..
gi 1655274923 1868 RRQAEDEAYQRKILEDQANQHKLEIEE 1894
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2069-2598 |
1.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2069 NKLKEEYEKAKALARDAEAAKERAEREAAlLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAefeaaklaqaeaaA 2148
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRRLEL-------------L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2149 LKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDkqksllDDELQRLKDEVDDAMRQKASVEEELfkvKIQ 2228
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRR---ARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2229 MEELMKLKVRIEEEnqrlmkkdkdntqkflveeaenmkklAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEkmlKEKM 2308
Cdd:COG4913 365 EALLAALGLPLPAS--------------------------AEEFAALRAEAAALLEALEEELEALEEALAEAE---AALR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2309 QAIQEASRLKAEAEMLQRQK---DLAQEQAQKLLEDK------------QLMQQRLDEET-----EEYQRSL------EA 2362
Cdd:COG4913 416 DLRRELRELEAEIASLERRKsniPARLLALRDALAEAlgldeaelpfvgELIEVRPEEERwrgaiERVLGGFaltllvPP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2363 ERKRQLEIIAEAEKLKLQVSqlSEAQAKAEEEAKKFKKQADTIAARL--HETEIAT--KEQMTEvkKMEFEKLNTSKEAD 2438
Cdd:COG4913 496 EHYAAALRWVNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLdfKPHPFRAwlEAELGR--RFDYVCVDSPEELR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2439 DLRKAIT-----------------------------------ELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMT-- 2481
Cdd:COG4913 572 RHPRAITragqvkgngtrhekddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERLEALEAELDALQERREAlq 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2482 VLQQTFLTEKEMLLKKEKL--IEDEKKKLES------QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKE 2553
Cdd:COG4913 652 RLAEYSWDEIDVASAEREIaeLEAELERLDAssddlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE 731
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1655274923 2554 AEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQK 2598
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERID 776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1195-1448 |
1.12e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1195 QIDLRQRELDQLgrqlgyyresydwlirwiadakqrQENIQAVpitdSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAK 1274
Cdd:COG4942 21 AAAEAEAELEQL------------------------QQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1275 AYIDIIKDYELQLVAYKAQVEPLTSPLKKTKlDSASDNIIQEYVTlrTRYSELMTLTSQyiKFITDTQRRLEDEEKAAEK 1354
Cdd:COG4942 73 ALEQELAALEAELAELEKEIAELRAELEAQK-EELAELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1355 LKaEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNlSEQQI 1434
Cdd:COG4942 148 RR-EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEEL 225
|
250
....*....|....
gi 1655274923 1435 KDKSQQVDEALKSR 1448
Cdd:COG4942 226 EALIARLEAEAAAA 239
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1902-2109 |
1.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1902 SSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLvLEEE 1981
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREE-LGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1982 MRRK--------------EAED---------KVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIV 2038
Cdd:COG3883 92 ARALyrsggsvsyldvllGSESfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2039 AAQQAalkcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQ 2109
Cdd:COG3883 172 ELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1955-2281 |
1.18e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1955 IAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKV---KKIAAAEEEAARQRKAAQEE----LDRLQKKADEVRKQKE 2027
Cdd:pfam02029 1 IEDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEpneHNSYEEDSELKPSGQGGLDEeeafLDRTAKREERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2028 EADKEAEKQIVAAQQAAL-----KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYE-KAKALARDAEAAKERAEREaallrQ 2101
Cdd:pfam02029 81 EALERQKEFDPTIADEKEsvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEiREKEYQENKWSTEVRQAEE-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2102 QAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQK---QQADEEMAKHKKLAEQTLKQKFQVEQ 2178
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEvksQNGEEEVTKLKVTTKRRQGGLSQSQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2179 ELTKVKLQLeETDKQKSLLDDELQRLKDEVDDAMRQK-ASVEEELFKVKIQMEElmKLKVRIEEENQRlmkkdKDNTQKF 2257
Cdd:pfam02029 236 REEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLRQKqQEAELELEELKKKREE--RRKLLEEEEQRR-----KQEEAER 307
|
330 340
....*....|....*....|....
gi 1655274923 2258 LVEEAENMKKLAEDAARLSIEAQE 2281
Cdd:pfam02029 308 KLREEEEKRRMKEEIERRRAEAAE 331
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1373-1528 |
1.20e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1373 QKQLAEAHAKA---IAKAEKEAQELKlrmqeevskretaavdaEKQKQNIQLELHELKNLSEQQIKDKSQQVDEaLKSRL 1449
Cdd:PRK12704 30 EAKIKEAEEEAkriLEEAKKEAEAIK-----------------KEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1450 RIEEEIhlIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQV------SEETQKKRL---AEEELKH 1520
Cdd:PRK12704 92 LQKEEN--LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisglTAEEAKEILlekVEEEARH 169
|
170 180
....*....|....*....|.
gi 1655274923 1521 -------------KSEAERKA 1528
Cdd:PRK12704 170 eaavlikeieeeaKEEADKKA 190
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1678-2102 |
1.22e-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: 48.47 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1678 SKAEESALKQRDMAENELER-----QRRLAESTAQQKLAAEQELIRLRAD-FDNAEQQRSLLEDEL-YRLKNEVIAAQQE 1750
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEyLYELNVLKEKSEAELtSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1751 RKQLEDELSKVRSEMDILI---QLKSRAEKET-----MSNTEKSKQLLEAEAtklrDLAEEASKLRAIAEEAKHQRQLAE 1822
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVeeaEKKAKDQKEEdrrnyPTNTYKTLELEIAES----DVEVKKAELELVKEEAKEPRDEEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1823 EDAARQRAEAERILKEKLAAI-SDATRLKTEAE--IALKEKEAENERLRRQAEDEA---YQRKILEDQANQHKLEIEEKi 1896
Cdd:NF033838 206 IKQAKAKVESKKAEATRLEKIkTDREKAEEEAKrrADAKLKEAVEKNVATSEQDKPkrrAKRGVLGEPATPDKKENDAK- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1897 vllkkSSDAEMERQKAIVDDTLKQRRVVEEEIRILKlnFEKASSGKLDLE---LELNKLKNIAEETQQSKLRAEEEAEKL 1973
Cdd:NF033838 285 -----SSDSSVGEETLPSPSLKPEKKVAEAEKKVEE--AKKKAKDQKEEDrrnYPTNTYKTLELEIAESDVKVKEAELEL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1974 rrlvLEEEMRRKEAEDKVKKiaaaEEEAARQRKAAQEELDRLQ---KKADEVRKQK-EEADKEAEKQIVAAQQAAlkcnm 2049
Cdd:NF033838 358 ----VKEEAKEPRNEEKIKQ----AKAKVESKKAEATRLEKIKtdrKKAEEEAKRKaAEEDKVKEKPAEQPQPAP----- 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2050 aeqqvqsvlAQQKEDSmmQNKLKEEYEKAKALARDAEAAKE----RAEREAALLRQQ 2102
Cdd:NF033838 425 ---------APQPEKP--APKPEKPAEQPKAEKPADQQAEEdyarRSEEEYNRLTQQ 470
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1682-1872 |
1.29e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1682 ESALKQRDMAENELERQR-RLAESTAQ-QKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS 1759
Cdd:COG3206 171 EEARKALEFLEEQLPELRkELEEAEAAlEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1760 KVRSEMDILIQlksraeKETMSNTEKSKQLLEAE-ATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAE---RI 1835
Cdd:COG3206 251 SGPDALPELLQ------SPVIQQLRAQLAELEAElAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEaelEA 324
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655274923 1836 LKEKLAAISDA-TRLKTEAEiALKEKEAENERLRRQAE 1872
Cdd:COG3206 325 LQAREASLQAQlAQLEARLA-ELPELEAELRRLEREVE 361
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1243-1720 |
1.31e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1243 KTLKEQLAKEKKLLEEIEKNKDKVDECQkyakAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRT 1322
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYA----ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1323 RYSELMTLtsqyIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEV 1402
Cdd:COG4717 140 ELAELPER----LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1403 SKRETAAVDAEKQKQNIQLELHELKNlsEQQIKDKSQ------------QVDEALKSRLRIEEEIHLIRIQLETTVKQ-K 1469
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAAL--EERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLLALLFLlL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1470 SNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKqvseetqkkrlaeeELKHKSEAERKAANEKQKALEDLENLRMQAEEA 1549
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLA--------------ALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1550 ERQVKQAEVEKERQIQVAhvAAQQSAAAELRSKQMSFAENVSKLEEslkqehgtvlqLQQDAERLRKQQEDAENAREEAE 1629
Cdd:COG4717 360 EEELQLEELEQEIAALLA--EAGVEDEEELRAALEQAEEYQELKEE-----------LEELEEQLEELLGELEELLEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1630 RELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAkkrskaeESALKQRDMAENELER--QRRLAESTAQ 1707
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL-------AELLQELEELKAELRElaEEWAALKLAL 499
|
490
....*....|...
gi 1655274923 1708 QKLAAEQELIRLR 1720
Cdd:COG4717 500 ELLEEAREEYREE 512
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2189-2595 |
1.31e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2189 ETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELmklkvrieEENQRLMKKDKDNTQKFLVEEAENMKKL 2268
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERREEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2269 A---EDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDlaqeqaqklledkqlm 2345
Cdd:PRK02224 254 EtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE---------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2346 qqRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqakaEEEAKKFKKQADTIAARLHETEIATKEQMTEVkk 2425
Cdd:PRK02224 318 --ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEI-- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2426 mefeklntskeaDDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREmTVLQQTFLTEKEMLLKKEKLIEDEK 2505
Cdd:PRK02224 387 ------------EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2506 KKLESQFEEEIKKAKALkDEQDRQRQQMEEEKLKLKATMDaALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQK 2585
Cdd:PRK02224 454 CPECGQPVEGSPHVETI-EEDRERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRET 531
|
410
....*....|
gi 1655274923 2586 LREKLQQMEE 2595
Cdd:PRK02224 532 IEEKRERAEE 541
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2007-2222 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2007 AAQEELDRLQKKADEVRKQKEEADKEAEKQivAAQQAALKCNMAEQQVQSVLAQQKedsmmQNKLKEEYEKAKalARDAE 2086
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAAL--KKEEKALLKQLAALERRIAALARR-----IRALEQELAALE--AELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2087 AAKERAEREAALLRQQAEEAERQKVAAEQEAANQAK---AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQAdEEMAKHK 2163
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2164 KLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEEL 2222
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2071-2480 |
1.35e-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: 47.61 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2071 LKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKvaaeqeaaNQAKAQDDAERLRKDAEfeaaklaqaeaaalk 2150
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKE--------EERRLDEMMEEERERAL--------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2151 qKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQME 2230
Cdd:pfam13868 58 -EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2231 ELMKLKVRIEEENQRLmkkdkdntqkflvEEAENMKKLAEDAARLsiEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQA 2310
Cdd:pfam13868 137 EEQAEWKELEKEEERE-------------EDERILEYLKEKAERE--EEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2311 IQEASRLK-AEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRqleiiAEAEKLKLQVSQLseaqa 2389
Cdd:pfam13868 202 ERDELRAKlYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAER-----EEEEFERMLRKQA----- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2390 kaeeeakkfkkqadtiaarlhetEIATKEQMTEVKKMEFEKlntsKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 2469
Cdd:pfam13868 272 -----------------------EDEEIEQEEAEKRRMKRL----EHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
410
....*....|.
gi 1655274923 2470 DAQQKQIEREM 2480
Cdd:pfam13868 325 AERRERIEEER 335
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1342-1567 |
1.35e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.45 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAEKLK----AEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEevskretaavdAEKQKQ 1417
Cdd:pfam09787 17 ARILQSKEKLIASLKegsgVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE-----------LEAQQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1418 NIQLELHELKNLSEQQIkdksqqvdeALKSRLRIEEEIHLIRIQLEttvkQKSNAEDelkQLRDRADAAEKLRKLAQeEA 1497
Cdd:pfam09787 86 EEAESSREQLQELEEQL---------ATERSARREAEAELERLQEE----LRYLEEE---LRRSKATLQSRIKDREA-EI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 1498 EKLRKQVSEETQKKrLAEEELKHKSEAERKAANEKQKALEDLE----NLRMQAEEAERQVKQAEVEKERQIQVA 1567
Cdd:pfam09787 149 EKLRNQLTSKSQSS-SSQSELENRLHQLTETLIQKQTMLEALSteknSLVLQLERMEQQIKELQGEGSNGTSIN 221
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4256-4292 |
1.36e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.36e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 4256 DPSEETVPIAGILDTETLEKVSVTEAMHRNLVDNITG 4292
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1698-1880 |
1.45e-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: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1698 QRRLAESTAQQKLAAeqelirlradfdnAEQQRslledelyrlKNEVIAAQQERKQledELSKVRSEMDILIQLKSRAEK 1777
Cdd:COG2268 191 RRKIAEIIRDARIAE-------------AEAER----------ETEIAIAQANREA---EEAELEQEREIETARIAEAEA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1778 ETmsntEKSKQLLEAEATKLRDLAEEASKLRAI---------AEEAKHQRQ--LAEEDAARQRAEAERILKEKLAAisDA 1846
Cdd:COG2268 245 EL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAEREREieLQEKEAEREEAELEADVRKPAEA--EK 318
|
170 180 190
....*....|....*....|....*....|....
gi 1655274923 1847 TRLKTEAeialkEKEAENERLRRQAEDEAYQRKI 1880
Cdd:COG2268 319 QAAEAEA-----EAEAEAIRAKGLAEAEGKRALA 347
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
150-263 |
1.57e-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: 44.03 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 150 DIQVNGQSEDMSAKEKLLLWSQrmtDGYQGIRCDNFTTSWRDGKLFNAVIHKNYPRLI-DMGKVYRQTNLENLEQAFNVA 228
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQ---NKLPQLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274923 229 EKDLGVTRLLDPEDVDVPHPDEKSIITYVSSLYDA 263
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4369-4406 |
1.70e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 4369 QRFLEVQYLTGGLIEPEAQGRVSLDESIRKGTIDARTA 4406
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2419-2598 |
1.86e-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: 47.59 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2419 QMTEvkKMEFEKLNTSKEADDLRkaiTELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKE 2498
Cdd:pfam15964 342 QMTE--EANFEKTKALIQCEQLK---SELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2499 KLIED---EKKKLESQFEEEIKKAKAlkdeqdrqrQQMEEEKL--KLKATMDAALNKQKEAEKDILN-KQKEMQELERKR 2572
Cdd:pfam15964 417 AQVEKvtrEKNSLVSQLEEAQKQLAS---------QEMDVTKVcgEMRYQLNQTKMKKDEAEKEHREyRTKTGRQLEIKD 487
|
170 180
....*....|....*....|....*.
gi 1655274923 2573 LEQERVladeNQKLREKLQQMEEAQK 2598
Cdd:pfam15964 488 QEIEKL----GLELSESKQRLEQAQQ 509
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1314-2012 |
1.90e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1314 IQEYVTLRTRYSELMTLTSQYIK---FITDTQRRLEDEEK--------AAEKLKAEEQKKMAEMQAELDKQK-------- 1374
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAEQYRLVEMARELAELNeaesdleq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1375 ------------QLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAA---VDAEKQKQNIQLELHELKN-LSE-QQIKDK 1437
Cdd:PRK04863 329 dyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQNEVVEEADeqqEENEARAEAAEEEVDELKSqLADyQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1438 SQ----QVDEALKSRLRIEEEIHLIRIQLEttvkqksNAEDELKQLRDRADAA-EKLRKLAQeeaeKLRKQVSEETQKKR 1512
Cdd:PRK04863 409 QQtraiQYQQAVQALERAKQLCGLPDLTAD-------NAEDWLEEFQAKEQEAtEELLSLEQ----KLSVAQAAHSQFEQ 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1513 LAEEELKHKSEAERKAANEK-QKALEDLENLRMQAEEAE-RQVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSFAENV 1590
Cdd:PRK04863 478 AYQLVRKIAGEVSRSEAWDVaRELLRRLREQRHLAEQLQqLRMRLSELEQRLRQQ----QRAERLLAEFCKRLGKNLDDE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1591 SKLEEsLKQEHGTVL--------QLQQDAERLRKQQEDAENAREEAERELEKWRQkANEAL-RLRLQAEE---------E 1652
Cdd:PRK04863 554 DELEQ-LQEELEARLeslsesvsEARERRMALRQQLEQLQARIQRLAARAPAWLA-AQDALaRLREQSGEefedsqdvtE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1653 AHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAEneLERQRRLAESTAQQKLAAEQELIRLR------------ 1720
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSE--DPRLNALAERFGGVLLSEIYDDVSLEdapyfsalygpa 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1721 ------ADFDNAEQQRSLLED---ELY-------RLKNEVIAAQQERKQLEDEL-------SKVRSE------------- 1764
Cdd:PRK04863 710 rhaivvPDLSDAAEQLAGLEDcpeDLYliegdpdSFDDSVFSVEELEKAVVVKIadrqwrySRFPEVplfgraarekrie 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1765 -MDILIQLKSRAEKETMSNTEKSKQLLEA-----------------EATkLRDLAEEASKL-RAIAE-EAKHQRQLAEED 1824
Cdd:PRK04863 790 qLRAEREELAERYATLSFDVQKLQRLHQAfsrfigshlavafeadpEAE-LRQLNRRRVELeRALADhESQEQQQRSQLE 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1825 AARQRAEA-----------------ERI--LKEKLAAISDATRL-----KTEAEI-----ALKEKEAENERLRRQAEDEA 1875
Cdd:PRK04863 869 QAKEGLSAlnrllprlnlladetlaDRVeeIREQLDEAEEAKRFvqqhgNALAQLepivsVLQSDPEQFEQLKQDYQQAQ 948
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1876 YQRKILEDQA--------NQHKLEIEEKIVLLKKSSDAEmERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLEL 1947
Cdd:PRK04863 949 QTQRDAKQQAfaltevvqRRAHFSYEDAAEMLAKNSDLN-EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1948 ELNK----LKNIAEETQQSKLRAEEEAEK---LRRLVLEEEM-----RRKEAEDKVKKIAAAEEEAARQRKAAQEEL 2012
Cdd:PRK04863 1028 SYDAkrqmLQELKQELQDLGVPADSGAEErarARRDELHARLsanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERDY 1104
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1438-1779 |
1.93e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1438 SQQVDEALKSRL-RIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEE 1516
Cdd:COG5185 206 SIKESETGNLGSeSTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENAN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1517 ELKHKSEAERKAANEKQKALEDLENLrmqaEEAERQVKQAEVEKERQIQVAHV-AAQQSAAAELRSKQMSFAENVSKLEE 1595
Cdd:COG5185 286 NLIKQFENTKEKIAEYTKSIDIKKAT----ESLEEQLAAAEAEQELEESKRETeTGIQNLTAEIEQGQESLTENLEAIKE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1596 SLKQEHGTVlQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALrlrlqaeeEAHKKSLAQEEAEKQKEEADREAK 1675
Cdd:COG5185 362 EIENIVGEV-ELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEIL--------ATLEDTLKAADRQIEELQRQIEQA 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1676 KRSKAEESalKQRDMAENELERQRRLAESTAQQKLAAEQELI--RLRADFDNAEQQRSLLEDELYRLKNEViaaQQERKQ 1753
Cdd:COG5185 433 TSSNEEVS--KLLNELISELNKVMREADEESQSRLEEAYDEInrSVRSKKEDLNEELTQIESRVSTLKATL---EKLRAK 507
|
330 340
....*....|....*....|....*.
gi 1655274923 1754 LEDELSKVRSEMDILIQLKSRAEKET 1779
Cdd:COG5185 508 LERQLEGVRSKLDQVAESLKDFMRAR 533
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1481-1824 |
1.98e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1481 DRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENL--RMQAEEAERQVKQAEv 1558
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldRTAKREERRQKRLQE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1559 EKERQIQVAHVAAQQSAAAELRSKQMSFAENVS-------KLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERE 1631
Cdd:pfam02029 82 ALERQKEFDPTIADEKESVAERKENNEEEENSSwekeekrDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1632 LEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKA----EESALKQRDMAENELERQRRLAESTAQ 1707
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQngeeEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1708 QKLAAEQELIRLRADFDNAEQQrslledELYRLKNEviaaQQERKQLEDELSKVRSEmdiliQLKSRAEKETMSNTEKSK 1787
Cdd:pfam02029 242 VFLEAEQKLEELRRRRQEKESE------EFEKLRQK----QQEAELELEELKKKREE-----RRKLLEEEEQRRKQEEAE 306
|
330 340 350
....*....|....*....|....*....|....*..
gi 1655274923 1788 QLLEAEATKlRDLAEEASKLRAiaeEAKHQRQLAEED 1824
Cdd:pfam02029 307 RKLREEEEK-RRMKEEIERRRA---EAAEKRQKLPED 339
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1742-1863 |
2.01e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1742 NEVIAA-QQERKQLEDELSKVRSemdiliqLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQ--R 1818
Cdd:PRK00409 519 NELIASlEELERELEQKAEEAEA-------LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEiiK 591
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1655274923 1819 QLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAE 1863
Cdd:PRK00409 592 ELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1533-2044 |
2.12e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1533 QKALEDLENLRMQAEEAERQVKQAEVEK-----ERQIQVAHVAAQQSAAAELRSKQMSFAENVSK----LEESLKQEHGT 1603
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYlagrfEEAEALLERALAARALAALAALRHGNPPASARayanLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1604 VLQLQQDAERL--RKQQEDAENAREEAERELEKWRQKANEALRLRLQAEE--EAHKKSLAQEEAEKQKEEADREAKKRSK 1679
Cdd:COG3899 809 AYEFGELALALaeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEagLETGDAALALLALAAAAAAAAAAAALAA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1680 AEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELS 1759
Cdd:COG3899 889 AAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAA 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1760 KVRSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEK 1839
Cdd:COG3899 969 AAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAA 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1840 LAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLK 1919
Cdd:COG3899 1049 LAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAA 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1920 QRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEdkvkkiaaaEE 1999
Cdd:COG3899 1129 ARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLA---------AL 1199
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1655274923 2000 EAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAA 2044
Cdd:COG3899 1200 LALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1340-1562 |
2.12e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.17 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1340 DTQRRLEDEEKAAEKLKAEEQKKMAEMQaELDKQKQLAEAHAKAIAKAEKEAQElklrmqEEVSKRETAAVDAEKQKQNI 1419
Cdd:pfam02029 140 YQENKWSTEVRQAEEEGEEEEDKSEEAE-EVPTENFAKEEVKDEKIKKEKKVKY------ESKVFLDQKRGHPEVKSQNG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1420 QLELHELKNLSEQQIKDKSQQVDEALKSRLRIEeeihliriqlettvkqksnAEDELKQLRDRADAAEklrklaQEEAEK 1499
Cdd:pfam02029 213 EEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-------------------AEQKLEELRRRRQEKE------SEEFEK 267
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 1500 LRkqvseetQKKRLAE---EELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKER 1562
Cdd:pfam02029 268 LR-------QKQQEAElelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1476-1656 |
2.28e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.17 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1476 LKQLRDRADA--AEKLRKLAQ--EEAEKLRKQVSEETQKKrlaeeelkhKSEAERKAANEKQKALEDLENLRMQAEEAER 1551
Cdd:COG2268 176 ITDLEDENNYldALGRRKIAEiiRDARIAEAEAERETEIA---------IAQANREAEEAELEQEREIETARIAEAEAEL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1552 QVKQAEVEKERQIQvahvAAQQSAAAELRSKQMSfaENVSKLEESLKQEHGTVLQlQQDAERLRKQQEDAENAREEAERE 1631
Cdd:COG2268 247 AKKKAEERREAETA----RAEAEAAYEIAEANAE--REVQRQLEIAEREREIELQ-EKEAEREEAELEADVRKPAEAEKQ 319
|
170 180
....*....|....*....|....*.
gi 1655274923 1632 LEKWRQKAN-EALRLRLQAEEEAHKK 1656
Cdd:COG2268 320 AAEAEAEAEaEAIRAKGLAEAEGKRA 345
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2003-2284 |
2.33e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEV---------RKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNklke 2073
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAkarfearqaRLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV---- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2074 eyEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAerlRKDAEFEAAKLAQAEAAALKQKQ 2153
Cdd:PRK05035 508 --IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKA---KKAAQQAANAEAEEEVDPKKAAV 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2154 QADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETD----KQKSLLDDELQRLKDEVDDamrQKASVEEELFKVKIqm 2229
Cdd:PRK05035 583 AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAiaraKAKKAEQQANAEPEEPVDP---RKAAVAAAIARAKA-- 657
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2230 eelmklkvrieeenqrlmKKDKDNTQKFLVEEAENMKKLAEDAARLSIEAQEAAR 2284
Cdd:PRK05035 658 ------------------RKAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2298-2597 |
2.48e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2298 TLAEKMLKEKMQAIQEASRLKAEA---EMLQRQKDLAQEQAQKLLEDKQLMQQRldEETEEYQRSLEAERKRQLEIIAEA 2374
Cdd:TIGR00618 119 RILAAKKSETEEVIHDLLKLDYKTftrVVLLPQGEFAQFLKAKSKEKKELLMNL--FPLDQYTQLALMEFAKKKSLHGKA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2375 EKLKLQVSQLSEAQAKAEeeakkfkkqaDTIAARLhETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARL 2454
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMP----------DTYHERK-QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2455 KKEAEEHQNKSKEMADaQQKQIEREMTVLQqtFLTEKEMLLKKEKLIEDEKKKLESQFEEEIK----KAKALKDEQDRQR 2530
Cdd:TIGR00618 266 RARIEELRAQEAVLEE-TQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKllmkRAAHVKQQSSIEE 342
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 2531 QQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADENQKLREKLQQMEEAQ 2597
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQ 409
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1432-1598 |
2.49e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1432 QQIKDKSQQvdEALKSRLRIEEeihliriQLETTVKQKSNAEDE-LKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQK 1510
Cdd:PRK09510 67 QQQQQKSAK--RAEEQRKKKEQ-------QQAEELQQKQAAEQErLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1511 KRLAEEELKHKSEAERKAANE-KQKALEDlenlrMQAEEAERQVKQAEVEKERQiqvAHVAAQQSAAAELRSKQMSFAEN 1589
Cdd:PRK09510 138 AAKAAAAAKAKAEAEAKRAAAaAKKAAAE-----AKKKAEAEAAKKAAAEAKKK---AEAEAAAKAAAEAKKKAEAEAKK 209
|
....*....
gi 1655274923 1590 VSKLEESLK 1598
Cdd:PRK09510 210 KAAAEAKKK 218
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1746-1919 |
2.85e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.32 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1746 AAQQERKQLEDElskVRSEMDILIqLKSRAEKEtmsntEKSKQLLEAEAtklRDLAEEASKlRAIAEeakhqrqlaeeda 1825
Cdd:PTZ00491 667 AARHQAELLEQE---ARGRLERQK-MHDKAKAE-----EQRTKLLELQA---ESAAVESSG-QSRAE------------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1826 ARQRAEAERIlkeKLAAISDATRLKTEAEIALKEKEAENERLRRQAEdeayqrkiLEDQANQHKLEIEEKivllKKSSDA 1905
Cdd:PTZ00491 721 ALAEAEARLI---EAEAEVEQAELRAKALRIEAEAELEKLRKRQELE--------LEYEQAQNELEIAKA----KELADI 785
|
170
....*....|....*...
gi 1655274923 1906 EMERQKAIVD----DTLK 1919
Cdd:PTZ00491 786 EATKFERIVEalgrETLI 803
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
47-112 |
3.03e-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: 43.03 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 47 KKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREK----GRMRFHKLQNVQIALDFL 112
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1726-1896 |
3.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1726 AEQQRSLLEdeLYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQLLEAEATKLRDLAEEAS 1805
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1806 KLRAIAEEAKHQRQLAEE--DAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILED 1883
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|...
gi 1655274923 1884 QANQHKLEIEEKI 1896
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1919-2109 |
3.39e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1919 KQRRVVEEEIRILKLNFEKASSGKLDLELELNKlknIAEETQQSKLRAEEEaeklrRLVLEEEMRRKEAEDKVKKiaaae 1998
Cdd:pfam15709 352 RKRREQEEQRRLQQEQLERAEKMREELELEQQR---RFEEIRLRKQRLEEE-----RQRQEEEERKQRLQLQAAQ----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1999 EEAARQRKAAQEELDRLQKKadevrKQKEEADK-EAEKQivaaQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEK 2077
Cdd:pfam15709 419 ERARQQQEEFRRKLQELQRK-----KQQEEAERaEAEKQ----RQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEK 489
|
170 180 190
....*....|....*....|....*....|...
gi 1655274923 2078 AKALARDAEAAKERAEREA-ALLRQQAEEAERQ 2109
Cdd:pfam15709 490 ARLEAEERRQKEEEAARLAlEEAMKQAQEQARQ 522
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2336-2595 |
3.47e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2336 QKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIA 2415
Cdd:COG5185 214 NLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFEN 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2416 TKEQMTEVKKMEFEKLNTSKEADDLRKAitELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTF--LTEKEM 2493
Cdd:COG5185 294 TKEKIAEYTKSIDIKKATESLEEQLAAA--EAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIenIVGEVE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2494 LLKKEKLIEDEKKKLESQFEEEIKKAKALKD--------------EQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDIL 2559
Cdd:COG5185 372 LSKSSEELDSFKDTIESTKESLDEIPQNQRGyaqeilatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNELISELN 451
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1655274923 2560 NKQKEMQELERKRLEQE-----RVLADENQKLREKLQQMEE 2595
Cdd:COG5185 452 KVMREADEESQSRLEEAydeinRSVRSKKEDLNEELTQIES 492
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1682-1992 |
3.49e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1682 ESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKV 1761
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1762 RSEMDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLA 1841
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1842 AISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQR 1921
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 1922 RVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVK 1992
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2403-2546 |
3.51e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.00 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2403 DTIAARLHeTEIATKEQmtevkkmefeklntskEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTV 2482
Cdd:COG0542 396 DEAAARVR-MEIDSKPE----------------ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEA 458
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2483 LQQTFLTEKEMLlkkeklieDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA 2546
Cdd:COG0542 459 LKARWEAEKELI--------EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| SH3_and_anchor |
TIGR04211 |
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ... |
2175-2264 |
3.68e-04 |
|
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.
Pssm-ID: 275056 [Multi-domain] Cd Length: 198 Bit Score: 45.00 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2175 QVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKiqmeELMKLKVRIEEENQRLMKKDKDNT 2254
Cdd:TIGR04211 70 ELQQELAELQEELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIK----QISANAIELDEENRELREELAELK 145
|
90
....*....|
gi 1655274923 2255 QKFLVEEAEN 2264
Cdd:TIGR04211 146 QENEALEAEN 155
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2301-2588 |
3.73e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEaSRLKAEAEMLQRQKDLAQEQAqkllEDKQLMQQRLDEETEEYQRSLEAERKRQLEI----IAEAEK 2376
Cdd:pfam02029 61 EEAFLDRTAKREE-RRQKRLQEALERQKEFDPTIA----DEKESVAERKENNEEEENSSWEKEEKRDSRLgrykEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2377 LKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVK-KMEFEKLNTSKEADDLRKAITELEKEKARLK 2455
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKiKKEKKVKYESKVFLDQKRGHPEVKSQNGEEE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2456 KEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKL-ESQFEEEIKKAKaLKDEQDRQRQQME 2534
Cdd:pfam02029 216 VTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrQKQQEAELELEE-LKKKREERRKLLE 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2535 EEKLKLKAtmDAALNKQKEAEKdilnKQKEMQELERKRLEQervlADENQKLRE 2588
Cdd:pfam02029 295 EEEQRRKQ--EEAERKLREEEE----KRRMKEEIERRRAEA----AEKRQKLPE 338
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
523-617 |
3.75e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.70 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 523 LRYVQDLLEWVQENQRRIDEAEWGSDLPSVESQLGSHRGLHQTVEDFRSKIERAKADENQL---SPISRGKYREYLGRLD 599
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1655274923 600 LQYAKLLNSSKSRLRNLD 617
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1446-2007 |
4.01e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1446 KSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKlAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAE 1525
Cdd:PRK01156 149 AQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKS-SNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1526 RKAANEKQKALEDLENLRMQAEEAER------------QVKQAEVEKERQIQVAHVAAQQSAAAELRS------------ 1581
Cdd:PRK01156 228 NNAMDDYNNLKSALNELSSLEDMKNRyeseiktaesdlSMELEKNNYYKELEERHMKIINDPVYKNRNyindyfkykndi 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1582 ---KQM---------SFAENVSKLEEsLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELekwrqKANEALRLRLQA 1649
Cdd:PRK01156 308 enkKQIlsnidaeinKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL-----KSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1650 EEEAHKKSLAQEEAEKQKEEADREAKKRSKAE--------ESAL-----KQRDMAENELERQRRLAESTAQQKLA----- 1711
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDPDAIKKELNEinvklqdiSSKVsslnqRIRALRENLDELSRNMEMLNGQSVCPvcgtt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1712 -AEQELIRLRADFDNaeqQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSE-------------------MDILIQL 1771
Cdd:PRK01156 462 lGEEKSNHIINHYNE---KKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksineynkiesaradlEDIKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1772 KSRAEKETMSNTEKSkqllEAEATKLRDL-AEEASKLRAIAeeakhQRQLAEEDAARQRAEaerilkEKLAAISDATRLK 1850
Cdd:PRK01156 539 NELKDKHDKYEEIKN----RYKSLKLEDLdSKRTSWLNALA-----VISLIDIETNRSRSN------EIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1851 TEAEIALKEKEAENERLRRQAEDEA--YQRKILEDQANQHKLE-IEEKIVLLKKSSDAEMERQKaivddtlkqrrvveee 1927
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEAnnLNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIP---------------- 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1928 irilklNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMR---RKEAEDKVKKIAAAEEEAARQ 2004
Cdd:PRK01156 668 ------DLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRindINETLESMKKIKKAIGDLKRL 741
|
...
gi 1655274923 2005 RKA 2007
Cdd:PRK01156 742 REA 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1938-2155 |
4.09e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1938 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLrrlvlEEEMRRKEAEdkvkkiaaaeeeaarqRKAAQEELDRLQK 2017
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-----NEEYNELQAE----------------LEALQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2018 KADEVRKQKEEADKEAEKQIVAAQQAALKCNMAE---------------QQVQSVLAQQKEDSMMQNKLKEEYEKAKAla 2082
Cdd:COG3883 73 EIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKA-- 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2083 rDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQA 2155
Cdd:COG3883 151 -ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3412-3443 |
4.12e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.12e-04
10 20 30
....*....|....*....|....*....|..
gi 1655274923 3412 KLLSAEKAVTGYKDPFTGKTISLFEAMQKDLI 3443
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1417-1572 |
4.21e-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: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1417 QNIQLELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLA--- 1493
Cdd:COG1579 13 QELDSELDRL----EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1494 ------QEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLR--MQAEEAERQVKQAEVEKERQIQ 1565
Cdd:COG1579 89 keyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKaeLDEELAELEAELEELEAEREEL 168
|
....*..
gi 1655274923 1566 VAHVAAQ 1572
Cdd:COG1579 169 AAKIPPE 175
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2336-2609 |
4.57e-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: 46.22 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2336 QKLLEDKQLMQQRLDEEteEYQRSLEAERKRQLeiIAEAEKLKLQVSQLSEAQAKaeeeakkfkkqaDTIAARLHETEIA 2415
Cdd:pfam05622 3 SEAQEEKDELAQRCHEL--DQQVSLLQEEKNSL--QQENKKLQERLDQLESGDDS------------GTPGGKKYLLLQK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2416 TKEQMTEvkkmEFEKLNTSKeaDDLRKAITELEKEKARLKKEAEEHQNKSKEMAdaqqkQIEREMTVLQQTflteKEMLL 2495
Cdd:pfam05622 67 QLEQLQE----ENFRLETAR--DDYRIKCEELEKEVLELQHRNEELTSLAEEAQ-----ALKDEMDILRES----SDKVK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2496 KKEKLIEDEKKKLES-----------------------QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALN--- 2549
Cdd:pfam05622 132 KLEATVETYKKKLEDlgdlrrqvklleernaeymqrtlQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKlef 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2550 --KQKEAEKDILNKQKEmqelerkRLEQER-VLADENQKLR-EKLQQMEEAQKSTLITEKHVTV 2609
Cdd:pfam05622 212 eyKKLEEKLEALQKEKE-------RLIIERdTLRETNEELRcAQLQQAELSQADALLSPSSDPG 268
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2431-2600 |
4.60e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2431 LNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEkemLLKKEKLIEDEKKKLES 2510
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2511 QFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQ---------ELERKRLEQERVLAD 2581
Cdd:COG3206 285 RYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEarlaelpelEAELRRLEREVEVAR 364
|
170 180
....*....|....*....|
gi 1655274923 2582 EN-QKLREKLQQMEEAQKST 2600
Cdd:COG3206 365 ELyESLLQRLEEARLAEALT 384
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2717-2750 |
4.97e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.97e-04
10 20 30
....*....|....*....|....*....|....
gi 1655274923 2717 LLEAQAATGYMLDPINNHKLSVNEAVKEGLIGPE 2750
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2358-2602 |
5.06e-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: 46.37 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2358 RSLEAERKRQLEIIAEAEK-LKLQVSQLSEAQAKAEEEAKKFKKQAD-TIAARLHETEIAtkeqmtEVKKMEFEKLNTSK 2435
Cdd:pfam12128 268 KSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEAL------EDQHGAFLDADIET 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2436 EADDLRKA---ITELEKEKARLKKEAEEHQNKSKEMADAQQK---QIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLE 2509
Cdd:pfam12128 342 AAADQEQLpswQSELENLEERLKALTGKHQDVTAKYNRRRSKikeQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2510 SQFEEEIKKAKA-LKDEQDRQRQQMEEEKLKLKAT----------------MDAALNKQKEAEKDILNKQKEMQELERKR 2572
Cdd:pfam12128 422 SELREQLEAGKLeFNEEEYRLKSRLGELKLRLNQAtatpelllqlenfderIERAREEQEAANAEVERLQSELRQARKRR 501
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274923 2573 LEQERVLADENQKLRE------KLQQMEEAQKSTLI 2602
Cdd:pfam12128 502 DQASEALRQASRRLEErqsaldELELQLFPQAGTLL 537
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2411-2569 |
5.52e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.02 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2411 ETEIATKEQMTEVKKMEFEKlNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQqkQIEREMTVLQQTFLTE 2490
Cdd:COG2268 211 ETEIAIAQANREAEEAELEQ-EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIA--EANAEREVQRQLEIAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2491 KEmllKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDA-ALNKQKEAEKDILNKQKEMQELE 2569
Cdd:COG2268 288 RE---REIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIE 364
|
|
| PTZ00332 |
PTZ00332 |
paraflagellar rod protein; Provisional |
2181-2555 |
5.64e-04 |
|
paraflagellar rod protein; Provisional
Pssm-ID: 240364 [Multi-domain] Cd Length: 589 Bit Score: 46.11 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2181 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQ-KASVEEELFKVKIQMEE----LMKLKVRI----EEENQRLmkKDK 2251
Cdd:PTZ00332 174 TQIQNALASTDDQIKTQLAQLEKTNEIQNVAMHDgEMQVAEEQMWTKVQLQErlieLVADKFRLigkcEEENKSF--SKI 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2252 DNTQKFLVEEAENMKklaeDAARlsieaqeaaRLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLA 2331
Cdd:PTZ00332 252 HEVQKQANQETSQMK----DAKR---------RLKQRCETDLKHIHDAIQKADLEDAEAMKRYATNKEKSERFIRENEDR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2332 QEQAQKLLEDKQLMQQRLDEETEEyqrsleaERKRQLEIIAEAEKLKLQVSQLseaqakaeeeakkfkkqadtiaarlhe 2411
Cdd:PTZ00332 319 QEEAWNKIQDLERQLQRLGTERFE-------EVKRRIEENDREEKRRVEYQQF--------------------------- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2412 TEIATKEQmtevKKMEFEKLNTSKeADDLRKAITELEKEKARLKKEaeEHQNKSKEMADAQQKQIEREMTVLQQTFLTEK 2491
Cdd:PTZ00332 365 LEVAGQHK----KLLELTVYNCDL-ALRCTGLVEELVSEGCAAVKA--RHDKTNQDLAALRLQVHKEHLEYFRMLYLTLG 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2492 EMLLKKEKLIEDEKKKLESQ----------FEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAE 2555
Cdd:PTZ00332 438 SLIYKKEKRLEEIDRNIRTThiqlefcvetFDPNAKKHADMKKELYKLRQGVEEELAMLKEKQAQALEMFKESE 511
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1855-2128 |
6.28e-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: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1855 IALKEKEAENERLRRQAEDEAYQRKILEDQ----ANQHKLEiEEKIVLLK--KSSDAEMER--QKAIVDDTLKQRRVVEE 1926
Cdd:NF012221 1535 VATSESSQQADAVSKHAKQDDAAQNALADKeraeADRQRLE-QEKQQQLAaiSGSQSQLEStdQNALETNGQAQRDAILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1927 EIRILKLNFEKASSGkldleleLNKLKNIAEETQQSKLRAEEE-AEKLRRLVleeemrrKEAEDKVKKIAAAEEEAARQR 2005
Cdd:NF012221 1614 ESRAVTKELTTLAQG-------LDALDSQATYAGESGDQWRNPfAGGLLDRV-------QEQLDDAKKISGKQLADAKQR 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2006 KAaqeelDRLQKKADEVRK------QKEEADKEAEKQIVAAQqaalkcNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAK 2079
Cdd:NF012221 1680 HV-----DNQQKVKDAVAKseagvaQGEQNQANAEQDIDDAK------ADAEKRKDDALAKQNEAQQAESDANAAANDAQ 1748
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 2080 ALA-RDAEAAK---ERAEREAALLRQQA-EEAERQKVAAEQEAANQAKAQDDAE 2128
Cdd:NF012221 1749 SRGeQDASAAEnkaNQAQADAKGAKQDEsDKPNRQGAAGSGLSGKAYSVEGVAE 1802
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2484-2596 |
6.54e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 44.31 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2484 QQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKaKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNK-- 2561
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQR-KARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQew 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 1655274923 2562 -QKEMQELERKRLEQERVLADENQKLREKLQQMEEA 2596
Cdd:pfam13904 148 eRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1689-2028 |
6.56e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1689 DMAENELERQRRlaestaqqklaAEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDIL 1768
Cdd:pfam02029 3 DEEEAARERRRR-----------AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1769 IQLKSRAEKETMsntEKSKQLLEAEATKLRDLAEEASKL-RAIAEEAKHQRQLAEEDAARQRAEAERILKEklaaisDAT 1847
Cdd:pfam02029 72 EERRQKRLQEAL---ERQKEFDPTIADEKESVAERKENNeEEENSSWEKEEKRDSRLGRYKEEETEIREKE------YQE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1848 RLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQH-----KLEIEEKIVLLKKSSDAEMERQKAiVDDTLKQRR 1922
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKikkekKVKYESKVFLDQKRGHPEVKSQNG-EEEVTKLKV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1923 VVEEEIRILKLNFEKASSGKLDLELElNKLKNIAEETQQSklrAEEEAEKLRR------LVLEEEMRRKEAEDKVKKiaa 1996
Cdd:pfam02029 222 TTKRRQGGLSQSQEREEEAEVFLEAE-QKLEELRRRRQEK---ESEEFEKLRQkqqeaeLELEELKKKREERRKLLE--- 294
|
330 340 350
....*....|....*....|....*....|..
gi 1655274923 1997 aeeEAARQRKaaQEELDRLQKKADEVRKQKEE 2028
Cdd:pfam02029 295 ---EEEQRRK--QEEAERKLREEEEKRRMKEE 321
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2286-2601 |
6.73e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2286 RQIAEDDLNQQRTLAEKM-LKEKMQAIQEasrLKAEAEMLQRQKDLAQEQAQKLLEDkqlMQQRLDEEtEEYQRSLEAER 2364
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNaLQEQLQAETE---LCAEAEEMRARLAARKQELEEILHE---LESRLEEE-EERSQQLQNEK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2365 KRQLEIIAEAEklklqvSQLSEAQakaeeeakkfkkqadtiAARLH-ETEIATKEqmTEVKKMEFEKLNTSKEADDLRKA 2443
Cdd:pfam01576 99 KKMQQHIQDLE------EQLDEEE-----------------AARQKlQLEKVTTE--AKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2444 ITELEKEKARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQQTFLTEKEMLLKKEKLiedeKKKLE---SQFEEEIKKAK 2520
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKSLSKLKNKH-EAMISDLEERLKKEEKGRQELEKA----KRKLEgesTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2521 ALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKrLEQERVLADENQKLREKLQQMEEAQKST 2600
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED-LESERAARNKAEKQRRDLGEELEALKTE 307
|
.
gi 1655274923 2601 L 2601
Cdd:pfam01576 308 L 308
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1360-1911 |
7.85e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1360 QKKMAEMQAELDKQKQLAEAHAKAI-------------AKAEKEAQELKLRMQE-EVSKRETAAVDAEKQKQNIQL--EL 1423
Cdd:pfam10174 136 RKTLEEMELRIETQKQTLGARDESIkkllemlqskglpKKSGEEDWERTRRIAEaEMQLGHLEVLLDQKEKENIHLreEL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1424 HELKNLSEQQIKDKS-QQVDEALKSRL-RIEEEIHLIRIQLETTvkqKSNA-------EDELKQL---RDRAD-AAEKLR 1490
Cdd:pfam10174 216 HRRNQLQPDPAKTKAlQTVIEMKDTKIsSLERNIRDLEDEVQML---KTNGllhtedrEEEIKQMevyKSHSKfMKNKID 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1491 KLAQEEAEK-------------LRKQVSEETQKKRLAEEELKHKSE---------------AERKAA--NEKQKALEDLE 1540
Cdd:pfam10174 293 QLKQELSKKesellalqtkletLTNQNSDCKQHIEVLKESLTAKEQraailqtevdalrlrLEEKESflNKKTKQLQDLT 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1541 NLRMQAEEAERQVKQAEVEKERQIQVAHvAAQQSAAAELRSKQMSFAEN-----------------VSKLEESLKQEHGT 1603
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKINVLQ-KKIENLQEQLRDKDKQLAGLkervkslqtdssntdtaLTTLEEALSEKERI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1604 VlqlqqdaERLRKQQEDAENAREEAERELEKWRQKANEalRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRS--KAE 1681
Cdd:pfam10174 452 I-------ERLKEQREREDRERLEELESLKKENKDLKE--KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSklKSL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1682 ESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRLRadfdnaeqqrsLLEDELYRLKNEVIAAQQERKQLEDELSKV 1761
Cdd:pfam10174 523 EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIR-----------LLEQEVARYKEESGKAQAEVERLLGILREV 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1762 RSE-------MDILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAER 1834
Cdd:pfam10174 592 ENEkndkdkkIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1835 ilkeklaaisDATRLK-TEAEIALKEKEAENERL----RRQAED------EAYQRKILEDQANQHKLEI--------EEK 1895
Cdd:pfam10174 672 ----------DATKARlSSTQQSLAEKDGHLTNLraerRKQLEEilemkqEALLAAISEKDANIALLELssskkkktQEE 741
|
650
....*....|....*.
gi 1655274923 1896 IVLLKKSSDAEMERQK 1911
Cdd:pfam10174 742 VMALKREKDRLVHQLK 757
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2417-2527 |
8.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2417 KEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEkemllK 2496
Cdd:PRK00409 530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS-----V 604
|
90 100 110
....*....|....*....|....*....|.
gi 1655274923 2497 KEKLIEDEKKKLESQFEEEIKKAKALKDEQD 2527
Cdd:PRK00409 605 KAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1945-2353 |
9.12e-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: 45.03 E-value: 9.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1945 LELELNKLKNiAEETQQSKLRAEEEAEKLRRLvlEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRK 2024
Cdd:pfam15558 10 AALMLARHKE-EQRMRELQQQAALAWEELRRR--DQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2025 QKEEADKEAEKQIVAAQQAALKCNMAEQQVQsvlAQQKEDSMMQN-KLKEEYEKAKAlardaeaakeraEREAALLRQQA 2103
Cdd:pfam15558 87 KQVIEKESRWREQAEDQENQRQEKLERARQE---AEQRKQCQEQRlKEKEEELQALR------------EQNSLQLQERL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2104 EEAERQKVAAEQEAANQAKAQDDAERLRKDAefeaaklaqaEAAALKQKQQADEEMAKhkklaeQTLKQKFQVEQELTkv 2183
Cdd:pfam15558 152 EEACHKRQLKEREEQKKVQENNLSELLNHQA----------RKVLVDCQAKAEELLRR------LSLEQSLQRSQENY-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2184 klqleetdkqksllddelQRLKDEVDDAMRQKASVEEELFKvkiqmeelmKLKVRIEEENQRLMKKdkdntQKFLVEEAE 2263
Cdd:pfam15558 214 ------------------EQLVEERHRELREKAQKEEEQFQ---------RAKWRAEEKEEERQEH-----KEALAELAD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2264 NMKKLAEDAARLSIEaQEAARLRQIAEDDLNQQRTLAEKMLKE---KMQAIQEASRLKAE-AEMLQRQKDLAQEQAQKLL 2339
Cdd:pfam15558 262 RKIQQARQVAHKTVQ-DKAQRARELNLEREKNHHILKLKVEKEekcHREGIKEAIKKKEQrSEQISREKEATLEEARKTA 340
|
410
....*....|....
gi 1655274923 2340 EDKQLMQQRLDEET 2353
Cdd:pfam15558 341 RASFHMREKVREET 354
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2354-2540 |
9.28e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.32 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2354 EEYQRSLEAERKRQLEIIAEaEKLKLQVSQLseaqakaeeeaKKFKKQADTIAARlhETEIATKEQM---TEVKKMEFEK 2430
Cdd:COG4487 25 KQRRAEFEKELAERLADAAK-REAALELAEA-----------KAKAQLQEQVAEK--DAEIAELRARleaEERKKALAVA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2431 LNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQK---QIEREmtvLQQTFLTEKEMLLKKEKLIEDEKKK 2507
Cdd:COG4487 91 EEKEKELAALQEALAEKDAKLAELQAKELELLKKERELEDAKREaelTVEKE---RDEELDELKEKLKKEEEEKQLAEKS 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1655274923 2508 L-ESQFEEEIKKAK----ALKDEQDRQRQQMEEEKLKL 2540
Cdd:COG4487 168 LkVAEYEKQLKDMQeqieELKRKKEQGSTQLQGEVLEL 205
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1501-1708 |
9.43e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1501 RKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEaERQVKQAEVEKERQIQVAHVAAQQSAAAELR 1580
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEE-QRRLQQEQLERAEKMREELELEQQRRFEEIR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1581 SKQMSFAENVSKLEESLKQEHgtvLQLQQDAERLRKQQEDAENAREEAERELEKWRQKANEALRLRLQAEE----EAHKK 1656
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQR---LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEmqlaEEQKR 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 1657 SLAQEEAEK---QKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQ 1708
Cdd:pfam15709 468 LMEMAEEERleyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1345-1617 |
9.71e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1345 LEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDA---EKQKQNIQ 1420
Cdd:PLN03229 413 VDPERKVNMKKREAVKTPVRELEGEVEKlKEQILKAKESSSKPSELALNEMIEKLKKEIDLEYTEAVIAmglQERLENLR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1421 LELheLKNLSEQQ-----IKDKSQQVDE-------------ALKSRLRIEEEIHLIRIQLETTVKQ---KSNAEDELKQL 1479
Cdd:PLN03229 493 EEF--SKANSQDQlmhpvLMEKIEKLKDefnkrlsrapnylSLKYKLDMLNEFSRAKALSEKKSKAeklKAEINKKFKEV 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1480 RDRADAAEKLRKLAQEEAEKlrKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVK----Q 1555
Cdd:PLN03229 571 MDRPEIKEKMEALKAEVASS--GASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPppnlQ 648
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 1556 AEVEK---------ERQIQVAHVAA-----QQSAAAELRSKQMSFAENVSKLEESLKQEHGTVL---QLQQDAERLRKQ 1617
Cdd:PLN03229 649 EKIESlneeinkkiERVIRSSDLKSkiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALnssELKEKFEELEAE 727
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1952-2106 |
9.77e-04 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 43.93 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1952 LKNIAEETQQSKLRAEEEAEKLRRlvlEEEMRRKEAEDKVKkiaaaeeeaarqrkaaqeelDRLQKKADEVRKQKEEADK 2031
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKEEQ---EAELRKRLAKEKYQ--------------------EWLQRKARQQTKKREESHK 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2032 EaekqiVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARdaeaAKERAEREAALLRQQAEEA 2106
Cdd:pfam13904 118 Q-----KAAESASKSLAKPERKVSQEEAKEVLQEWERKKLEQQQRKREEEQR----EQLKKEEEEQERKQLAEKA 183
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2003-2109 |
9.99e-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: 44.99 E-value: 9.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvlAQQKEDSMMQNKLKEEYEKA-KAL 2081
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADT--SSPKEDKQVAENQKREIEKAqIEI 290
|
90 100
....*....|....*....|....*...
gi 1655274923 2082 ARDAEAAKERAEREAALLRQQAEEAERQ 2109
Cdd:pfam05262 291 KKNDEEALKAKDHKAFDLKQESKASEKE 318
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2756-2786 |
1.01e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|.
gi 1655274923 2756 LSAEKAVVGYKDPYSGGKISVFEAMKKGLMD 2786
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1672-2133 |
1.03e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1672 REAKKRSKAEESALKQRDMAEnelERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLEDELyRLKNEVIAAQQER 1751
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAE---AEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEA-EQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1752 KQLEDElskvrsemdiliqlKSRAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKhqrqlAEEDAARQRAE 1831
Cdd:COG3064 78 KLAEAE--------------KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKR-----KAEEEAKRKAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1832 AERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQK 1911
Cdd:COG3064 139 EERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1912 AIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKV 1991
Cdd:COG3064 219 LAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1992 KKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKL 2071
Cdd:COG3064 299 DSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2072 KEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKD 2133
Cdd:COG3064 379 KLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKL 440
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
52-142 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 52 KWVNKHLIKSQR---HVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRM---RFHKLQNVQIALDFLRhrQVKLVN-IRN 124
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 1655274923 125 DDIADGNPKLTLGLIWTI 142
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4264-4295 |
1.06e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.06e-03
10 20 30
....*....|....*....|....*....|..
gi 1655274923 4264 IAGILDTETLEKVSVTEAMHRNLVDNITGQRL 4295
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
40-143 |
1.06e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 42.05 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 40 DERDRVQkktFTKWVNK---------HLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTL-------PREKGRM--RFHK 101
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQM 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1655274923 102 LQNVQIALDFLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21294 81 IENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1224-1440 |
1.08e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1224 IADAKQRQENIQAvpitdskTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEpltsplkk 1303
Cdd:COG3883 25 LSELQAELEAAQA-------ELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1304 tkldsasDNIIQEYVTLRTRYSELMTLTSQ----------YIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQ 1373
Cdd:COG3883 90 -------ERARALYRSGGSVSYLDVLLGSEsfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1374 KQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQ 1440
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2161-2511 |
1.08e-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: 44.56 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2161 KHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIE 2240
Cdd:pfam09728 1 KAARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2241 EENQRLMkkdkdntqkflvEEAENMKKlAEDAARLSIEAQEAARLRQIaEDDLNQQRTLAEKMLKEKMQAiqeASRLKAe 2320
Cdd:pfam09728 81 KQNKKLK------------EESKKLAK-EEEEKRKELSEKFQSTLKDI-QDKMEEKSEKNNKLREENEEL---REKLKS- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2321 aemLQRQKDLAQEQAQKLLEDKQLMQQRLdeETEEYQRSLEAERKRQLEIIAEAEKLKLQVSQLSeaqakaeeeakkfkk 2400
Cdd:pfam09728 143 ---LIEQYELRELHFEKLLKTKELEVQLA--EAKLQQATEEEEKKAQEKEVAKARELKAQVQTLS--------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2401 qadtiaarlhETEIATKEQMTE-VKKM-EFEK---------LNTSKEADDLRKAITELEKEKARLKKEAEEHQNKSKEMA 2469
Cdd:pfam09728 203 ----------ETEKELREQLNLyVEKFeEFQDtlnksnevfTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMA 272
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1655274923 2470 DAQQKQIEremtvlqqtfltEKEMLLKKEKLIEDEKKKLESQ 2511
Cdd:pfam09728 273 EERQKLKE------------ELEKLQKKLEKLENLCRALQAE 302
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3045-3077 |
1.12e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|...
gi 1655274923 3045 LEAQAGTGYVVDPVHNQHYTVDEAVKAGVVGPE 3077
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1713-2351 |
1.14e-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: 45.40 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1713 EQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKEtMSNTEKSKQLLEA 1792
Cdd:TIGR04523 60 DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVE-LNKLEKQKKENKK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1793 EATK----LRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIaLKEKEAENERLR 1868
Cdd:TIGR04523 139 NIDKflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN-LKKKIQKNKSLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1869 RQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSsdaemerQKAIVDDTLKQRRVVEE-EIRILKLnfEKASSGKLDLEL 1947
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNT-------QTQLNQLKDEQNKIKKQlSEKQKEL--EQNNKKIKELEK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1948 ELNKLKNIAEETQQSKlrAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKE 2027
Cdd:TIGR04523 289 QLNQLKSEISDLNNQK--EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2028 EADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMMQNKLKEEYEKAKalardaEAAKERAEREAALLRQQAEEAE 2107
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEKLNQQKDEQIKKL------QQEKELLEKEIERLKETIIKNN 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2108 RQKVAAEQEAANQAKAQDDAERLRKDaefeaaklaqaeaaalkQKQQADEEMAKHKKLaEQTLKQKfqvEQELTKVKLQL 2187
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRES-----------------LETQLKVLSRSINKI-KQNLEQK---QKELKSKEKEL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2188 EETDKQKSLLDDELQRLKDEVDdamrQKASVEEELFKVKIQME-ELMKLKVRIEEENQRLmkkDKDNTQKFLVEEAENMK 2266
Cdd:TIGR04523 499 KKLNEEKKELEEKVKDLTKKIS----SLKEKIEKLESEKKEKEsKISDLEDELNKDDFEL---KKENLEKEIDEKNKEIE 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2267 KLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQ 2346
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
....*
gi 1655274923 2347 QRLDE 2351
Cdd:TIGR04523 652 ETIKE 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1247-1764 |
1.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1247 EQLAKEKKLLEEIeknkdkVDECQKYAKAYIDIikdyeLQLVAYKAQVEPLTSPLKKTKLDSASDNIIQEYVTLRTRYSE 1326
Cdd:COG4913 245 EDAREQIELLEPI------RELAERYAAARERL-----AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1327 LMTLTSQYIKFITDTQRRLE----DEEKAAEKLKAEEQKKMAEMQAELDKQKQLAE-------AHAKAIAKAEKEAQELK 1395
Cdd:COG4913 314 LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1396 LRMQEEVSKRETAAVDAEKQKQNIQLELHELknlsEQQIkdksqqvdEALKSR-LRIEEEIHLIRIQLETTVKqksNAED 1474
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELREL----EAEI--------ASLERRkSNIPARLLALRDALAEALG---LDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1475 ELK------QLRDRA----DAAEK-LRKLA----------------------------QEEAEKLRKQVSEETQKKRLAE 1515
Cdd:COG4913 459 ELPfvgeliEVRPEEerwrGAIERvLGGFAltllvppehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1516 -----------------------------EELKH-----------KSEAERKAANEKQKALED----------LENLRMQ 1545
Cdd:COG4913 539 kldfkphpfrawleaelgrrfdyvcvdspEELRRhpraitragqvKGNGTRHEKDDRRRIRSRyvlgfdnrakLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1546 AEEAERQVKQAEvEKERQIQVAHVAAQQSAAAELRSKQMSFAEnvskleESLKQEHGTVLQLQQDAERLRkqqedaenar 1625
Cdd:COG4913 619 LAELEEELAEAE-ERLEALEAELDALQERREALQRLAEYSWDE------IDVASAEREIAELEAELERLD---------- 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1626 eeaerelekwrqKANEALRlRLQAEEEAHKKSLaqeeaekqkEEADREAKKRSKAEESALKQRDMAENELER-QRRLAES 1704
Cdd:COG4913 682 ------------ASSDDLA-ALEEQLEELEAEL---------EELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAA 739
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1705 TAQQKLAAEQELIRLRADFDNAEQQRSLLEdelyRLKNEVIAAQQERKQLEDELSKVRSE 1764
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1825-2060 |
1.17e-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: 44.75 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1825 AARQRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANqhklEIEEKIVLLKKSSD 1904
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1905 AEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQqsklraeEEAEKLRRlvleeemRR 1984
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR-------EQAEELRA-------DL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 1985 KEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKadevRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQ 2060
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1684-1990 |
1.19e-03 |
|
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: 45.28 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1684 ALKQRDMAENELERQRRLAE---STAQQKLAAEQELIR--LRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDEL 1758
Cdd:pfam15964 354 ALIQCEQLKSELERQKERLEkelASQQEKRAQEKEALRkeMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1759 SKVRS-----EMD---ILIQLKSRAEKETMSNTEKSKQLLEAEATKLRDLA---EEASKLRAIAEEAKHQRQLAEEDAAR 1827
Cdd:pfam15964 434 EEAQKqlasqEMDvtkVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAAR 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1828 QRAEAERIlkeklaaisdaTRLKTEAEIALKEKEAENERLRRQAEDEAyqrKILEDQANQHKLEIEEKIVLLKKSSDAEM 1907
Cdd:pfam15964 514 AREECLKL-----------TELLGESEHQLHLTRLEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTV 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKASsgkldlelelNKLKNIAEETQQSKLRAEEEAEKLRRlvleeemRRKEA 1987
Cdd:pfam15964 580 NEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT----------QKSRSEVEQLSQEKEYLQDRLEKLQK-------RNEEL 642
|
...
gi 1655274923 1988 EDK 1990
Cdd:pfam15964 643 EEQ 645
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1453-1563 |
1.29e-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: 44.99 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1453 EEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQ----------------KKRLAEE 1516
Cdd:pfam05262 199 DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQeaknlpkpadtsspkeDKQVAEN 278
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655274923 1517 ElkhKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQ 1563
Cdd:pfam05262 279 Q---KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK 322
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1891-2256 |
1.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1891 EIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEA 1970
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1971 EKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMA 2050
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2051 EQQVQSVLA--QQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAE 2128
Cdd:COG4372 163 QEELAALEQelQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2129 RLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEV 2208
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1655274923 2209 DDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQK 2256
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1671-2373 |
1.36e-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: 44.81 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1671 DREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAEQELIRL--------RADFDNAEQQRSLLEDELYRLkn 1742
Cdd:pfam10174 44 ERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLlqqdfttsPVDGEDKFSTPELTEENFRRL-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1743 eviaaQQERKQLEDELSKVRSEMDILiQLKSRAEKETMSNTEKS-KQLLEAEATKlrdlaeeasKLRAIAEEAKHQRQLA 1821
Cdd:pfam10174 122 -----QSEHERQAKELFLLRKTLEEM-ELRIETQKQTLGARDESiKKLLEMLQSK---------GLPKKSGEEDWERTRR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1822 EEDAARQRAEAERILKEKlaaisdatrlKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLE-----IEEKI 1896
Cdd:pfam10174 187 IAEAEMQLGHLEVLLDQK----------EKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLErnirdLEDEV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1897 VLLKKSSDAEMERQKaivdDTLKQRRVV-------EEEIRILKLNFEKASSGKLDLELELNKLKNiaeetQQSKLRAEEE 1969
Cdd:pfam10174 257 QMLKTNGLLHTEDRE----EEIKQMEVYkshskfmKNKIDQLKQELSKKESELLALQTKLETLTN-----QNSDCKQHIE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1970 aeklrrlVLEEEMRRKEaedkvkkiaaaeeeaarQRKAA-QEELDRLQKKADE-----VRKQKEEADKEAEKQIVAAQQA 2043
Cdd:pfam10174 328 -------VLKESLTAKE-----------------QRAAIlQTEVDALRLRLEEkesflNKKTKQLQDLTEEKSTLAGEIR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2044 ALKcNMAEQQVQSVLAQQKEDSMMQNKLKEE-------YEKAKALARDA----------EAAKERAEREAALLRQQAEEA 2106
Cdd:pfam10174 384 DLK-DMLDVKERKINVLQKKIENLQEQLRDKdkqlaglKERVKSLQTDSsntdtalttlEEALSEKERIIERLKEQRERE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2107 ERQKVAAEQEAANQAK-AQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLaEQTLKQKFQ----VEQELT 2181
Cdd:pfam10174 463 DRERLEELESLKKENKdLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-EIAVEQKKEecskLENQLK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2182 KVKlQLEETDKQKSLLDDELQRLKDEV----DDAMRQKASVEEELFKVK-IQMEELMKLKvRIEEENQRLMKKDKDNTQK 2256
Cdd:pfam10174 542 KAH-NAEEAVRTNPEINDRIRLLEQEVarykEESGKAQAEVERLLGILReVENEKNDKDK-KIAELESLTLRQMKEQNKK 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2257 flveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMlkekmqaiqeasrlkaeaEMLQRQKDLAQEQAQ 2336
Cdd:pfam10174 620 -----VANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM------------------GALEKTRQELDATKA 676
|
730 740 750
....*....|....*....|....*....|....*..
gi 1655274923 2337 KLLEdkqlMQQRLdEETEEYQRSLEAERKRQLEIIAE 2373
Cdd:pfam10174 677 RLSS----TQQSL-AEKDGHLTNLRAERRKQLEEILE 708
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1740-2041 |
1.48e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1740 LKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETmsntEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQ 1819
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEEL----EQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1820 LAEEDAARQRAEAERILKEKLAAISDATRLK---TEAEIALKEKEAENERLRRQAEDEayQRKILEDQANQHKLEIEEKI 1896
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEaqiAELQSEIAEREEELKELEEQLESL--QEELAALEQELQALSEAEAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1897 VLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRL 1976
Cdd:COG4372 183 QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEE 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 1977 VLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQ 2041
Cdd:COG4372 263 LELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKK 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1224-1450 |
1.54e-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: 44.37 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1224 IADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPLTSPLKK 1303
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1304 TK------LDSASDNIIQEYVTLR---------TRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQA 1368
Cdd:COG4942 102 QKeelaelLRALYRLGRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1369 ELDKQKQlaeahakAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSR 1448
Cdd:COG4942 182 ELEEERA-------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
..
gi 1655274923 1449 LR 1450
Cdd:COG4942 255 LP 256
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1420-1617 |
1.55e-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: 44.65 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1420 QLELHELKNLSEQQIKdKSQQVDEAlksrlrIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADA-AEKLRKlAQEEAE 1498
Cdd:pfam10168 535 QLLSRATQVFREEYLK-KHDLAREE------IQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKlAEKYEE-IKDKQE 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1499 KLRKQVSEETQkkrLAEEELKHKSEAERKAANEkqkaledLENLRMQAEEAERQVKQAEVEKERQIQvaHVAAQQSAAae 1578
Cdd:pfam10168 607 KLMRRCKKVLQ---RLNSQLPVLSDAEREMKKE-------LETINEQLKHLANAIKQAKKKMNYQRY--QIAKSQSIR-- 672
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655274923 1579 lRSKQMSFAENVSK-LEESLKQEHGTVLQLQQDAERLRKQ 1617
Cdd:pfam10168 673 -KKSSLSLSEKQRKtIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1554-1781 |
1.56e-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: 44.37 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1554 KQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERELE 1633
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1634 KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMAENELERQRRLAESTAQQKLAAE 1713
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1714 QELIRLRADFDNAEQQRsllEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILIQLKSRAEKETMS 1781
Cdd:COG4942 181 AELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2154-2383 |
1.62e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2154 QADEEMAKHKKLAEQTL---KQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQ---KASVEEELFKVKI 2227
Cdd:PRK11281 53 LLEAEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlsTLSLRQLESRLAQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2228 QMEELMKLKVRIEEENQRLMkkdkdnTQKFLVEEA-----ENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEK 2302
Cdd:PRK11281 133 TLDQLQNAQNDLAEYNSQLV------SLQTQPERAqaalyANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2303 MLKEKMQAIQEASRLKaeaEMLQRQKDLAQEQAQKLLEDKQLMQ-----QRLD--EET-EEYQRSLEAERKRQLEIIAEA 2374
Cdd:PRK11281 207 QNDLQRKSLEGNTQLQ---DLLQKQRDYLTARIQRLEHQLQLLQeainsKRLTlsEKTvQEAQSQDEAARIQANPLVAQE 283
|
....*....
gi 1655274923 2375 EKLKLQVSQ 2383
Cdd:PRK11281 284 LEINLQLSQ 292
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1122-1261 |
1.64e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1122 DVKEVETYRTNLKKMRAEAEAEQPVFDSLEEELKKAsavsdkmsrvhserDAELDQHRQHLSSLQDRWKAVFTQIDLRQR 1201
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEEL--------------EAELEELEEELDELKGEIGRLEKELEQAEE 727
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1202 ELDQLGRQLGYYRESYDWLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEK 1261
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEE 787
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1858-2102 |
1.68e-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: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1858 KEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVllkkssdAEMERQKAivddtLKQRRVVEEEIRilklNFEK 1937
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRA-------AEQARQKE-----LEQRAAAEKAAK----QAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1938 ASSGKLDLELELNKLKNIAEETQQSKLRAEEEAEKLRRLV--LEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEEldRL 2015
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAkqAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA--EA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2016 QKKADEVRKQKEEADKEAEKQIVA-AQQAALKCNMAEqqvqsvlAQQKEDSMMQNK---LKEEYEKAKALARDAEAAKER 2091
Cdd:TIGR02794 188 KAKAEEAKAKAEAAKAKAAAEAAAkAEAEAAAAAAAE-------AERKADEAELGDifgLASGSNAEKQGGARGAAAGSE 260
|
250
....*....|.
gi 1655274923 2092 AEREAALLRQQ 2102
Cdd:TIGR02794 261 VDKYAAIIQQA 271
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2791-2827 |
1.70e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.70e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 2791 IRVLEAQLATGGIIDPLNSHRVPNEIAYKQGQYDAEM 2827
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2513-2627 |
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 1655274923 2513 EEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKrleqervLADENQKLREKLQQ 2592
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------IAEAEAEIEERREE 87
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274923 2593 MEEAQKSTLITEKHVTVVETVLNGQNAGDVLDGVE 2627
Cdd:COG3883 88 LGERARALYRSGGSVSYLDVLLGSESFSDFLDRLS 122
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1948-2358 |
1.86e-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: 44.62 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1948 ELNKLKNIAEETQQSKLRAEEEA--EKLRRLVLEEEMRRKEAEDKVKKiaaaeeeaARQRKAAQEELDRlqkkadevRKQ 2025
Cdd:NF033838 103 ELNVLKEKSEAELTSKTKKELDAafEQFKKDTLEPGKKVAEATKKVEE--------AEKKAKDQKEEDR--------RNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2026 KEEADKEAEKQIVaaqQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKerAEREAAllrqqAEE 2105
Cdd:NF033838 167 PTNTYKTLELEIA---ESDVEVKKAELELVKEEAKEPRDEEKIKQAKAKVESKKAEATRLEKIK--TDREKA-----EEE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2106 AERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEmakhkkLAEQTLKQ-KFQVEQELTKVK 2184
Cdd:NF033838 237 AKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSS------VGEETLPSpSLKPEKKVAEAE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2185 LQLEETDKqksllddelqRLKDEVDDAMRQKASVEEELFKVkiqmeELMKLKVRIEEENQRLMKKDKdntqkflvEEAEN 2264
Cdd:NF033838 311 KKVEEAKK----------KAKDQKEEDRRNYPTNTYKTLEL-----EIAESDVKVKEAELELVKEEA--------KEPRN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2265 MKKLAEDAARLSIEAQEAARLRQI------AEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKl 2338
Cdd:NF033838 368 EEKIKQAKAKVESKKAEATRLEKIktdrkkAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK- 446
|
410 420
....*....|....*....|
gi 1655274923 2339 LEDKQLMQQRLDEETEEYQR 2358
Cdd:NF033838 447 PADQQAEEDYARRSEEEYNR 466
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1567-1814 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1567 AHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQQEDAENAREEAERelekwRQKANEALRLR 1646
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-----ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1647 LQAEEEAHKKSLAQEEAEKQKEEADREAKKRSKAEESALKQRDMaeNELERQRRLAESTAQqklAAEQELIRLRADFDNA 1726
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAP---ARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1727 EQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRsemDILIQLKSRAEKEtmsntEKSKQLLEAEATKLRDLAEEASK 1806
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQ---KLLARLEKELAEL-----AAELAELQQEAEELEALIARLEA 234
|
....*...
gi 1655274923 1807 LRAIAEEA 1814
Cdd:COG4942 235 EAAAAAER 242
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1335-1423 |
1.87e-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: 41.70 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1335 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKR-ETAAVDA 1412
Cdd:COG0711 26 LKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEaRAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIiAQAEAEI 105
|
90
....*....|.
gi 1655274923 1413 EKQKQNIQLEL 1423
Cdd:COG0711 106 EQERAKALAEL 116
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1346-1615 |
1.96e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1346 EDEEKAAEKLKAEEqkKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNiqlELHE 1425
Cdd:PRK07735 36 KLEEENREKEKALP--KNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA---ALAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1426 LKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETT--VKQKSNAEDELKQLRDRADAAE-KLRKLAQEEAEKLRK 1502
Cdd:PRK07735 111 QKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTeeVTEEEEETDKEKAKAKAAAAAKaKAAALAKQKAAEAGE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1503 QVSEETQKKRLAEEELKHKSEAERKAANEKQKALEDlenlrmqaeeaerqvkQAEVEKERQIQVAHVAAQQSAAAELRSK 1582
Cdd:PRK07735 191 GTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG----------------NGDSGDEDAKAKAIAAAKAKAAAAARAK 254
|
250 260 270
....*....|....*....|....*....|....*
gi 1655274923 1583 QMSfaeNVSKLEESLKQEHGTVLQ--LQQDAERLR 1615
Cdd:PRK07735 255 TKG---AEGKKEEEPKQEEPSVNQpyLNKYVEVIK 286
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1330-1889 |
1.97e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.41 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1330 LTSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKM------AEMQAELDKQKQLAEAHAKAIAKAEKEAQEL-------KL 1396
Cdd:PRK10246 213 LTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLnwltrlDELQQEASRRQQALQQALAAEEKAQPQLAALslaqparQL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1397 RMQEEVSKRETAAVDAekqkqniqlelhelknlSEQQIKDKSQQVDEALKSRLRIEeeihliriqlETTVKQKSNAEDEL 1476
Cdd:PRK10246 293 RPHWERIQEQSAALAH-----------------TRQQIEEVNTRLQSTMALRARIR----------HHAAKQSAELQAQQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1477 KQLRDRADAAEKLRKLAQEEA---EKLRKQVSEETQKKRLAEEELkhkseaerkAANEKQKALEDLeNLRMQAEEaerqv 1553
Cdd:PRK10246 346 QSLNTWLAEHDRFRQWNNELAgwrAQFSQQTSDREQLRQWQQQLT---------HAEQKLNALPAI-TLTLTADE----- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1554 kqaevekerqiqVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedaenareeAERELE 1633
Cdd:PRK10246 411 ------------VAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAA----------LNEMRQ 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1634 KWRQKANEALRLRLQAEEEAHKKSLAQEEAEKqkeeadrEAKKR----SKAEESALKQRDMAENELERQRRLAESTAQQK 1709
Cdd:PRK10246 469 RYKEKTQQLADVKTICEQEARIKDLEAQRAQL-------QAGQPcplcGSTSHPAVEAYQALEPGVNQSRLDALEKEVKK 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1710 LAAEQELIRLRADFDNAEQQR------SLLEDE--LYRLKNEVIA-----------------AQQERKQLEDELSKvRSE 1764
Cdd:PRK10246 542 LGEEGAALRGQLDALTKQLQRdeseaqSLRQEEqaLTQQWQAVCAslnitlqpqddiqpwldAQEEHERQLRLLSQ-RHE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1765 MDILIQLKSRAEKETMSNTEKSKQLLEAE----ATKLRDLAEEASKLRAIAEEAKH-QRQLAEEDAARQRAEAERILKEK 1839
Cdd:PRK10246 621 LQGQIAAHNQQIIQYQQQIEQRQQQLLTAlagyALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTPLLET 700
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1840 LAAiSDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHK 1889
Cdd:PRK10246 701 LPQ-SDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQK 749
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2413-2604 |
2.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2413 EIATKEQMTEVKKMEFEKLNTSKE-ADDLRKAITELEKEKARLKKEaeehQNKSKEMADAQQKQIEREMTVL---QQTFL 2488
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEEnIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELlkeKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2489 TEKEMLLKKEKLIEDEKKKLESQFEEEIK----KAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKE 2564
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKrleeIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274923 2565 MQELERKRLEQE---RVLADENQKLREKLQQmEEAQKSTLITE 2604
Cdd:TIGR02169 317 LEDAEERLAKLEaeiDKLLAEIEELEREIEE-ERKRRDKLTEE 358
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1951-2158 |
2.05e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQS---KLRAE--------EEAEKLRRLVLEEEMRRKEAEDKV---------KKIAAAEEEAARQRK---- 2006
Cdd:PRK05035 437 EIRAIEQEKKKAeeaKARFEarqarlerEKAAREARHKKAAEARAAKDKDAVaaalarvkaKKAAATQPIVIKAGArpdn 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2007 ---AAQEELDRLQKKADEVRKQKEEADkEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSmmqNKLKEEYEKAKALAR 2083
Cdd:PRK05035 517 savIAAREARKAQARARQAEKQAAAAA-DPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDP---KKAAVAAAIARAKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2084 --------------DAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEfeaaklaqaeaaal 2149
Cdd:PRK05035 593 kaaqqaasaepeeqVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKAR-------------- 658
|
....*....
gi 1655274923 2150 KQKQQADEE 2158
Cdd:PRK05035 659 KAAQQQANA 667
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1953-2096 |
2.09e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1953 KNIAEETQQSKLRAEEEAEKLRRLVLEE-EMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEVRKQKEEADK 2031
Cdd:PRK12704 49 KEAEAIKKEALLEAKEEIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2032 EAE--KQIVAAQQAALkcnmaeqQVQSVLAQQKEDSMMQNKLKEEYEKAKA-LARDAEA-AKERAEREA 2096
Cdd:PRK12704 129 KEEelEELIEEQLQEL-------ERISGLTAEEAKEILLEKVEEEARHEAAvLIKEIEEeAKEEADKKA 190
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2166-2352 |
2.15e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2166 AEQTLkQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQM-------------EEL 2232
Cdd:COG3206 194 AEAAL-EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALpellqspviqqlrAQL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2233 MKLKVRIEEENQRLMKKDKDntqkflVEEAENmkKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQ 2312
Cdd:COG3206 273 AELEAELAELSARYTPNHPD------VIALRA--QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLA 344
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1655274923 2313 EASRLKAEAEMLQRQKDLAQEQAQKLLedKQLMQQRLDEE 2352
Cdd:COG3206 345 ELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEA 382
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2301-2592 |
2.26e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2301 EKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLEAERKRQLEIIAEAEKLKLQ 2380
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2381 VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEE 2460
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2461 HQNkSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEdEKKKLESQFEEEIKKAKALKDE-----QDRQRQQMEE 2535
Cdd:pfam07888 197 LRN-SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-ELRSLQERLNASERKVEGLGEElssmaAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2536 EKLKLKAT------MDAAL--------------NKQKEAEKD---ILNKQKEMQELErKRLEQERVladENQKLREKLQQ 2592
Cdd:pfam07888 275 HQARLQAAqltlqlADASLalregrarwaqereTLQQSAEADkdrIEKLSAELQRLE-ERLQEERM---EREKLEVELGR 350
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1473-1563 |
2.28e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1473 EDELKQLRDRADAAEKLRKlaqeEAEKLRKQVSEetQKKRLAEEELKHKSEAERKA----ANEKQKALEDLENLRMQAEE 1548
Cdd:PRK00409 526 EELERELEQKAEEAEALLK----EAEKLKEELEE--KKEKLQEEEDKLLEEAEKEAqqaiKEAKKEADEIIKELRQLQKG 599
|
90
....*....|....*
gi 1655274923 1549 AERQVKQAEVEKERQ 1563
Cdd:PRK00409 600 GYASVKAHELIEARK 614
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2006-2108 |
2.35e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2006 KAAQEELDRLQKKADEVRKQK-EEADKEAEKQIV----AAQQAALKCNMAEQQ-----VQSVLA--QQKEDSMMQNKLKE 2073
Cdd:PRK11637 166 QARQETIAELKQTREELAAQKaELEEKQSQQKTLlyeqQAQQQKLEQARNERKktltgLESSLQkdQQQLSELRANESRL 245
|
90 100 110
....*....|....*....|....*....|....*
gi 1655274923 2074 EYEKAKAlARDAEAAKERAEREAALLRQQAEEAER 2108
Cdd:PRK11637 246 RDSIARA-EREAKARAEREAREAARVRDKQKQAKR 279
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1322-1559 |
2.46e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 43.33 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1322 TRYSELMtltSQYIKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEahakaiaKAEKEAQELKLRMQEE 1401
Cdd:cd16269 44 AHYEEQM---EQRVQLPTETLQELLDLHAACEKEALEVFMKRSFKDEDQKFQKKLME-------QLEEKKEEFCKQNEEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1402 VSKRETAAVDA------EKQKQNI-------QLELHELKNLSE--QQIKDKSQQVDEALKSRLR----IEEEIHLiriql 1462
Cdd:cd16269 114 SSKRCQALLQElsapleEKISQGSysvpggyQLYLEDREKLVEkyRQVPRKGVKAEEVLQEFLQskeaEAEAILQ----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1463 etTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVseETQKKRLAE--EELKHKSEAERK-AANEKQKALEDL 1539
Cdd:cd16269 189 --ADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKL--EDQERSYEEhlRQLKEKMEEEREnLLKEQERALESK 264
|
250 260
....*....|....*....|..
gi 1655274923 1540 --ENLRMQAEEAERQVKQAEVE 1559
Cdd:cd16269 265 lkEQEALLEEGFKEQAELLQEE 286
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1342-1552 |
2.65e-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: 43.79 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAE-----KLKAEEQKKMAEMQAELDKQKQlaeahakaiakaeKEAQELKLRMQEEVSKRETAAvdAEKQK 1416
Cdd:pfam15709 345 MRRLEVERKRREqeeqrRLQQEQLERAEKMREELELEQQ-------------RRFEEIRLRKQRLEEERQRQE--EEERK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1417 QNIQlelhelknlsEQQIKDKSQQVDEALKSRLRieeEIHLIRIQLETtvkQKSNAEDE-LKQLRDR-ADAAEKLRKLAQ 1494
Cdd:pfam15709 410 QRLQ----------LQAAQERARQQQEEFRRKLQ---ELQRKKQQEEA---ERAEAEKQrQKELEMQlAEEQKRLMEMAE 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1495 EEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAAnekqkaledLENLRMQAEEAERQ 1552
Cdd:pfam15709 474 EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA---------LEEAMKQAQEQARQ 522
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1712-2109 |
2.74e-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: 43.79 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1712 AEQELIRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSemdilIQLKSRAEKETMSNTEKSKQLLE 1791
Cdd:COG5185 168 LTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES-----TLLEKAKEIINIEEALKGFQDPE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1792 AEATKLRDLAEEASKLRAIAEEAKhqrqlaeEDAARQRAEAERilkeklaaisdatRLKTEAEIALKEKEAENERLRRQA 1871
Cdd:COG5185 243 SELEDLAQTSDKLEKLVEQNTDLR-------LEKLGENAESSK-------------RLNENANNLIKQFENTKEKIAEYT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1872 EDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIR----------ILKLNFEKASSG 1941
Cdd:COG5185 303 KSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienivgevELSKSSEELDSF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1942 KLDLElelNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADE 2021
Cdd:COG5185 383 KDTIE---STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2022 VRKQKEEadkeaEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQ 2101
Cdd:COG5185 460 ESQSRLE-----EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
....*...
gi 1655274923 2102 QAEEAERQ 2109
Cdd:COG5185 535 YAHILALE 542
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1273-1505 |
2.87e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1273 AKAYIDIIKDYELQLVAYKAQVEPLTSPLKKTKldSASDNIIQEYVTLRTRYSELMTL---TSQYIKFITDTQRRLEDEE 1349
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALK--KEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1350 KAAEKLKAEEQKKMAEMQAELdkQKQLAEAHAKAIAKAEKEAQELK-LRMQEEVSKRETAAVDAEKQKQNiqlELHELKN 1428
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRrLQYLKYLAPARREQAEELRADLA---ELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1429 LSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLR---DRADAAekLRKLAQEEAEKLRKQVS 1505
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaEELEAL--IARLEAEAAAAAERTPA 245
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
2405-2611 |
2.91e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 43.69 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2405 IAARLHETEIATKEQMTEVKKMEFEklNTSKEADDLRKAITEL----EKEKaRLKKEAEEHQNKSKEM---ADAQQKQIE 2477
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLELD--EAEEALEEIEERIDQLydllEKEV-DAKKYVEKNLPEIEDYlehAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2478 REMTVLQQTF-LTEKEmlLKKEKLIEDEKKKLESQFEEEIKKAK-------ALKDEQDRQRQQM---EEEKLKLKATMDA 2546
Cdd:pfam06160 312 EELERVQQSYtLNENE--LERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILEQLeeiEEEQEEFKESLQS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2547 ALNKQKEAEKDILNKQKEMQELERkRLEQER-------------VLADENQKLREKLQQ----MEEAQKSTLITEKHVTV 2609
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKR-LVEKSNlpglpesyldyffDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDT 468
|
..
gi 1655274923 2610 VE 2611
Cdd:pfam06160 469 LY 470
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1385-1656 |
2.93e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1385 AKAEKEAQELKlRMQEEVSKRETAAvdAEKQKQNIQLeLHELKNlSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLET 1464
Cdd:PRK11637 40 AHASDNRDQLK-SIQQDIAAKEKSV--RQQQQQRASL-LAQLKK-QEEAISQASRKLRETQNTLNQLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1465 TVKQKSNAEDEL-KQLrdraDAAEKlrklaQEEAEKLRKQVS-EETQKKRLAEEELKHKSEAERKAANEKQKALEDLenl 1542
Cdd:PRK11637 115 LEQQQAAQERLLaAQL----DAAFR-----QGEHTGLQLILSgEESQRGERILAYFGYLNQARQETIAELKQTREEL--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1543 rmQAEEAERQVKQAEvekerqiQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQEHGTVLQLQQDAERLRKQqedae 1622
Cdd:PRK11637 183 --AAQKAELEEKQSQ-------QKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDS----- 248
|
250 260 270
....*....|....*....|....*....|....*.
gi 1655274923 1623 narEEAERELEKWR--QKANEALRLRlQAEEEAHKK 1656
Cdd:PRK11637 249 ---IARAEREAKARaeREAREAARVR-DKQKQAKRK 280
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1957-2261 |
3.12e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.56 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1957 EETQQSKLRAEEEAEKLRRL--VLEEEMRRKEAedKVKKIAAAEEEAARQRKAAQEELdrlQKKADEVRKQKEEADKEAE 2034
Cdd:pfam03528 4 EDLQQRVAELEKENAEFYRLkqQLEAEFNQKRA--KFKELYLAKEEDLKRQNAVLQEA---QVELDALQNQLALARAEME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2035 kQIVAAqqAALKCNMAEQQVQSVLAQ-QKEDSMMQNKLKE---EYEKAKALARDAEAA-----KERAEREAALLRQQAEE 2105
Cdd:pfam03528 79 -NIKAV--ATVSENTKQEAIDEVKSQwQEEVASLQAIMKEtvrEYEVQFHRRLEQERAqwnqyRESAEREIADLRRRLSE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2106 AERQKvaaeQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADE-EMAKHKKL-----AEQTLKQKFQ---- 2175
Cdd:pfam03528 156 GQEEE----NLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKElEASKMKELnhyleAEKSCRTDLEmyva 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2176 ---------------VEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDA----MRQKASVEEELFKVKIQMEELMKLK 2236
Cdd:pfam03528 232 vlntqksvlqedaekLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESqrllMRDMQRMESVLTSEQLRQVEEIKKK 311
|
330 340
....*....|....*....|....*
gi 1655274923 2237 VRIEEENQRlMKKDKDNTQKFLVEE 2261
Cdd:pfam03528 312 DQEEHKRAR-THKEKETLKSDREHT 335
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2308-2511 |
3.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2308 MQAIQE--ASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQR---SLEAERKRQLEIIAEAEKLKLQVS 2382
Cdd:COG4717 40 LAFIRAmlLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAElqeELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2383 QLSEAQAKAEEEAKKFKKQA--DTIAARLHETEiatkEQMTEVKKMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEE 2460
Cdd:COG4717 120 KLEKLLQLLPLYQELEALEAelAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2461 HQNKSKEMADAQQKQIEREMTVLQQT--FLTEKEMLLKKEKLIEDEKKKLESQ 2511
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEEleELEEELEQLENELEAAALEERLKEA 248
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1404-1610 |
3.17e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1404 KRETAAVDAEKQKQNIQLELH-----ELKNLSEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQ 1478
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTYnknieEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1479 LRD-RADAAEKLRKLAQEEA----------------------EKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKA 1535
Cdd:PHA02562 260 LNTaAAKIKSKIEQFQKVIKmyekggvcptctqqisegpdriTKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1536 LE---DLENLRMQAEEAERQVKQAEVEKERqIQVAHVaaqqSAAAELRSKQMSFAENVSKLEESLKQ--EHGTVLQLQQD 1610
Cdd:PHA02562 340 LElknKISTNKQSLITLVDKAKKVKAAIEE-LQAEFV----DNAEELAKLQDELDKIVKTKSELVKEkyHRGIVTDLLKD 414
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1347-1565 |
3.50e-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: 43.40 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1347 DEEKAAEKLKAEEQKKMAEMQAELDKQKqlaeahakaiakaekeaQELKLRMQEEVSKRetaavdAEKQKQNIQLELHEL 1426
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVERKRRE-----------------QEEQRRLQQEQLER------AEKMREELELEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1427 KnlseQQIKDKSQQVDEalkSRLRIEEEIHLIRIQLETTVKQKSNAEDELkqlrdRADAAEKLRKLAQEEAEKL----RK 1502
Cdd:pfam15709 386 F----EEIRLRKQRLEE---ERQRQEEEERKQRLQLQAAQERARQQQEEF-----RRKLQELQRKKQQEEAERAeaekQR 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1503 QVSEETQ----KKRLAEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERqVKQAEVEKERQIQ 1565
Cdd:pfam15709 454 QKELEMQlaeeQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAAR-LALEEAMKQAQEQ 519
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2003-2367 |
3.56e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKaaqeeldrlQKKADEVRKQKEEADKEAE-KQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKAL 2081
Cdd:pfam02029 9 RERR---------RRAREERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2082 ARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAK 2161
Cdd:pfam02029 80 QEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2162 HKKLAEQTLKQK---FQVEQELTKVKLQLEETDKQKSLLDdelqrlkdevddamrQKASVEEelfkVKIQMEELMKLKVR 2238
Cdd:pfam02029 160 EDKSEEAEEVPTenfAKEEVKDEKIKKEKKVKYESKVFLD---------------QKRGHPE----VKSQNGEEEVTKLK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2239 IEEENQRLMKKDKDNTQKFLVEEAENMKKLAEDAARLS-IEAQEAARLRQiaeddlNQQRTLAE-KMLKEKMqaiQEASR 2316
Cdd:pfam02029 221 VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQeKESEEFEKLRQ------KQQEAELElEELKKKR---EERRK 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2317 LKAEAEmlQRQKDLAQEQAQKLLEDKqlmqQRLDEETEeyQRSLEAERKRQ 2367
Cdd:pfam02029 292 LLEEEE--QRRKQEEAERKLREEEEK----RRMKEEIE--RRRAEAAEKRQ 334
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2153-2285 |
3.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2153 QQADEEMAKHKKLAEQTLKQKF-----QVEQELT--KVKLQ-LEETDKQK-SLLDDELQRLKDEVDDAMRQKASVEEELF 2223
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIhklrnEFEKELRerRNELQkLEKRLLQKeENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 2224 KVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVEEAEnmKKLAEDAARLSIEAQEAARL 2285
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE--EEARHEAAVLIKEIEEEAKE 184
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1749-2110 |
3.74e-03 |
|
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: 42.98 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1749 QERKQLEDELSKVRSEMDILIQLKS-RAEKETMSNTEKSKQLLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEEDAAR 1827
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEEReRALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1828 QRAEAERILKEKLAAISDATRLKTEAEIALKEKEAENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdaem 1907
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK------ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 erqkaivddtlkqrrvveeeirilklnfekassgkldlELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEA 1987
Cdd:pfam13868 183 --------------------------------------EREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1988 EDKVKKIaaaeeeaaRQRKAAQEELdRLQKKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSvLAQQKEDSMM 2067
Cdd:pfam13868 225 EEAEKKA--------RQRQELQQAR-EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR-RMKRLEHRRE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1655274923 2068 QNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQK 2110
Cdd:pfam13868 295 LEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1470-1882 |
3.85e-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: 43.13 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1470 SNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAAN---EKQKALEDLENLRMQA 1546
Cdd:pfam19220 13 GEMADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGltrRLSAAEGELEELVARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1547 EEAERQVKQAEVEKERQiqvahvaaqqsaAAELRSKQmSFAENvskLEESLKQEHGTVLQLQQDaerlrkqqedaenare 1626
Cdd:pfam19220 93 AKLEAALREAEAAKEEL------------RIELRDKT-AQAEA---LERQLAAETEQNRALEEE---------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1627 eaerelekwrqkaNEALRLRLQAEEEAhkkslaqeeaekqkeeadreaKKRSKAEESALKQR-DMAENELERQRRLAEST 1705
Cdd:pfam19220 141 -------------NKALREEAQAAEKA---------------------LQRAEGELATARERlALLEQENRRLQALSEEQ 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1706 AQQKLAAEQeliRLRADFDNAEQQRSLLEDELYRLKNEVIAAQQERKQLEDELSKVRSEMDILiqlksRAEKETMSN-TE 1784
Cdd:pfam19220 187 AAELAELTR---RLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASL-----RMKLEALTArAA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1785 KSKQLLEAEATKLRDLAE----------EASKLRAIAE------EAKHQRQLAE-EDAARQRAEAE-------RILKEKL 1840
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEairaaerrlkEASIERDTLErrlaglEADLERRTQQfQEMQRARAELEeraemltKALAAKD 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 1841 AAISDAT--------RLKTEAEIALKEK---EAENERLRRQAEDEAYQRKILE 1882
Cdd:pfam19220 339 AALERAEeriaslsdRIAELTKRFEVERaalEQANRRLKEELQRERAERALAQ 391
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
2489-2599 |
3.86e-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: 42.70 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2489 TEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKdeqdrqrqQMEEEKLKLKAT-MDAALNKQKEAEKDILNKQKEMQE 2567
Cdd:smart00787 158 EDYKLLMKELELLNSIKPKLRDRKDALEEELRQLK--------QLEDELEDCDPTeLDRAKEKLKKLLQEIMIKVKKLEE 229
|
90 100 110
....*....|....*....|....*....|..
gi 1655274923 2568 LERKRLEQERVLADENQKLREKLQQMEEAQKS 2599
Cdd:smart00787 230 LEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1770-1913 |
3.91e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1770 QLKSRAEKETmSNTEKSKQLLEAEATKLRDLAEEASKlRAIAEeakhqRQLAEEDAARQRAEAErilkekLAAISDATRL 1849
Cdd:COG2268 196 EIIRDARIAE-AEAERETEIAIAQANREAEEAELEQE-REIET-----ARIAEAEAELAKKKAE------ERREAETARA 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 1850 KTEAEIALKEKEAENErLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKssdAEMERQKAI 1913
Cdd:COG2268 263 EAEAAYEIAEANAERE-VQRQLEIAEREREIELQEKEAEREEAELEADVRKP---AEAEKQAAE 322
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1546-1735 |
3.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1546 AEEAERQVKQAEVEKERQIQVAHVAAQQsaAAELRSKQMSFAENVSKLE-ESLKQEHGTVLQLQQDAERLRKQQEDAENA 1624
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQ--AEELQQKQAAEQERLKQLEkERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1625 REEAERELEKWRQKANEALRLRLQAEEEAHKKSLAQEEAEKQ-----------KEEADREAKKRSKAE-ESALKQRDMAE 1692
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAaeakkkaeaeaAAKAAAEAKKKAEAEaKKKAAAEAKKK 218
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1655274923 1693 NELERQRRLAESTAQQKLAAEQELIRLRADFDNAEQQRSLLED 1735
Cdd:PRK09510 219 AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
45-147 |
3.93e-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: 40.36 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 45 VQKKTFTKWVNKHLIKSQRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR----FHKLQNVQIALDFLRHRQVKLV 120
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1655274923 121 NIRNDDIADGNPKLTLGLIWTIILHFQ 147
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1360-1617 |
3.96e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1360 QKKMAEMQ---AELDKQKQLAEAHakaIAKAEKEAQELKLRMQEEVsKRETAAVDAEK--------QKQNIQLELHELKN 1428
Cdd:pfam03528 7 QQRVAELEkenAEFYRLKQQLEAE---FNQKRAKFKELYLAKEEDL-KRQNAVLQEAQveldalqnQLALARAEMENIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1429 LSEQQIKDKSQQVDEaLKSRLRiEEEIHLIRIQLETTVKQKSNAEDELKQlrDRADAAEkLRKLAQEEAEKLRKQVSEET 1508
Cdd:pfam03528 83 VATVSENTKQEAIDE-VKSQWQ-EEVASLQAIMKETVREYEVQFHRRLEQ--ERAQWNQ-YRESAEREIADLRRRLSEGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1509 QKKRLaEEELKHKSEAERKAANEKQKALEDLENLRMQAEEAERQVKQAEVEKERQIQvAHVAAQQSAAAELrskQMSFAe 1588
Cdd:pfam03528 158 EEENL-EDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELEASKMKELN-HYLEAEKSCRTDL---EMYVA- 231
|
250 260
....*....|....*....|....*....
gi 1655274923 1589 nVSKLEESLkqehgtvlqLQQDAERLRKQ 1617
Cdd:pfam03528 232 -VLNTQKSV---------LQEDAEKLRKE 250
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1368-1501 |
3.99e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.73 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1368 AELDKQK---QLAEAHAK-AIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKsQQVDE 1443
Cdd:COG1566 74 ARLDPTDlqaALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDE 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1444 ALKSRLRIEEEIHLIRIQLETTVKQKSNAEdELKQLRDRADAAEKLRKLAQEEAEKLR 1501
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3451-3486 |
4.00e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 4.00e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1655274923 3451 LLEAQMVSGGIIDPVNSHRVPNDTAYQKNILSKEVA 3486
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1706-1923 |
4.04e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1706 AQQKLAAEQEliRLRADFDNAEQQRSLLEDELyRLKNeviAAQQERKQLEDE----LSKVRSEMDILIQLKSRAEKETMS 1781
Cdd:PRK05035 442 EQEKKKAEEA--KARFEARQARLEREKAAREA-RHKK---AAEARAAKDKDAvaaaLARVKAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1782 NTEkskqllEAEATKLRDLAEEASKLRAIAEEAKHQRQlAEEDAARQRAEAERILKEKLAAISDATRLKTEAEIALKEKE 1861
Cdd:PRK05035 516 NSA------VIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIAR 588
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1655274923 1862 AENERLRRQAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDtlKQRRV 1923
Cdd:PRK05035 589 AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP--RKAAV 648
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1219-1394 |
4.13e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1219 WLIRWIADAKQRQENIQAVPITDSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDYELQLVAYKAQVEPlt 1298
Cdd:PRK12704 23 FVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1299 splKKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDeekaAEKLKAEEQKKM----AEMQAELDKQK 1374
Cdd:PRK12704 101 ---KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER----ISGLTAEEAKEIllekVEEEARHEAAV 173
|
170 180
....*....|....*....|
gi 1655274923 1375 QLAEAHAKAIAKAEKEAQEL 1394
Cdd:PRK12704 174 LIKEIEEEAKEEADKKAKEI 193
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1375-1565 |
4.16e-03 |
|
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: 43.09 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1375 QLAEAHAKAIAKAEKEAQELKLRMQEEVSkretaavdaekqkqNIQLELHELKNlSEQQIKDKSQQVDEALKsrlRIEEE 1454
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREEELE--------------ELQEQLEDLES-SIQELEKEIKKLESSIK---QVEEE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1455 IHLIRIQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLrKQVSEETQKKRLAE-EELKHKSEAERKAANEKQ 1533
Cdd:pfam05667 372 LEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLiEEYRALKEAKSNKEDESQ 450
|
170 180 190
....*....|....*....|....*....|..
gi 1655274923 1534 KALEDLENLRMQAEEAERQVKQAEvEKERQIQ 1565
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKE-ELYKQLV 481
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2495-2598 |
4.23e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2495 LKKEKLIEDEKKKLESQFEEeikkAKALKDEQDRQRQQMEEeklkLKATMDAALNKQKEAEKDILNKQKEMQELERKRLE 2574
Cdd:PRK11281 48 LNKQKLLEAEDKLVQQDLEQ----TLALLDKIDRQKEETEQ----LKQQLAQAPAKLRQAQAELEALKDDNDEETRETLS 119
|
90 100
....*....|....*....|....
gi 1655274923 2575 QeRVLADENQKLREKLQQMEEAQK 2598
Cdd:PRK11281 120 T-LSLRQLESRLAQTLDQLQNAQN 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2078-2303 |
4.35e-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: 42.83 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2078 AKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADE 2157
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2158 EMAKHKK-LAEQTLKQKFQVEQELTKVKLQ---LEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELM 2233
Cdd:COG4942 98 ELEAQKEeLAELLRALYRLGRQPPLALLLSpedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2234 KLKVRIEEENQRLmKKDKDNTQKFLveeAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKM 2303
Cdd:COG4942 178 ALLAELEEERAAL-EALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3668-3704 |
4.37e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 4.37e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1655274923 3668 KQYLYGTGCVAGFT-TDSGSKMSIYQAMKRGFIQPDVA 3704
Cdd:smart00250 1 QRLLEAQSAIGGIIdPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
46-143 |
4.52e-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: 39.82 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 46 QKKTFTKWVNKHLIKS---------QRHVTDLYEDLRDGHNLISLLEVLSGDTLPREKGRMR-----FHKLQNVQIALDF 111
Cdd:cd21293 2 EKGSYVDHINRYLGDDpflkqflpiDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1655274923 112 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 143
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-635 |
4.54e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 367 VEKEWGRLHVAILERERLLRIEFERLERLQRIVNKVQMESGSCDEQLGNLE-TLLQTDIRLLNAGKPAQHTAEIERELDK 445
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 446 ADNTIRLLFNDVQILKDGRHPQAEQMYRRVFRIHERLVNLRSDYNLRLKSTTS-AIQATRLSPQESSMKARpelddvtlr 524
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDR--------- 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 525 yVQDLLEWVQENQRRIDEAEwgsdLPSVESQLGSH-RGLHQTVEDFRSKIERAKADENQLSPISRgKYREYLGRLDlQYA 603
Cdd:TIGR02168 416 -RERLQQEIEELLKKLEEAE----LKELQAELEELeEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELA-QLQ 488
|
250 260 270
....*....|....*....|....*....|..
gi 1655274923 604 KLLNSSKSRLRNLDSLHAFVSAATKELMWLND 635
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3336-3372 |
4.54e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 4.54e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1655274923 3336 KYLQGSESIAGIYLEPTKENISIYQAMKKKLLRHNTG 3372
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2152-2599 |
4.64e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2152 KQQADEEMAKHKkLAEQTLKQKFQVEQELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEE 2231
Cdd:PRK01156 203 KKQIADDEKSHS-ITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEER 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2232 LMKL------KVRIEEENQRLMKKDKDNTQKFLV-------EEAENMKKLAEDAARLSIEAQEAARLrqiaeDDLNQQRT 2298
Cdd:PRK01156 282 HMKIindpvyKNRNYINDYFKYKNDIENKKQILSnidaeinKYHAIIKKLSVLQKDYNDYIKKKSRY-----DDLNNQIL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2299 LAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLEDKQLMQQRLDEETEEYQRSLE--------------AER 2364
Cdd:PRK01156 357 ELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQdisskvsslnqrirALR 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2365 KRQLEIIAEAEKLKLQ----VSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEqmTEVKKMEFEKLNTSKEADDL 2440
Cdd:PRK01156 437 ENLDELSRNMEMLNGQsvcpVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKD--IDEKIVDLKKRKEYLESEEI 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2441 RKAITELEKEKArLKKEAEEHQNKSKEMADAQQK--QIEREMTVLQQTFLTEKEM----LLKKEKLIEDEkkKLESQFEE 2514
Cdd:PRK01156 515 NKSINEYNKIES-ARADLEDIKIKINELKDKHDKyeEIKNRYKSLKLEDLDSKRTswlnALAVISLIDIE--TNRSRSNE 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2515 eikKAKALKDEQDRQrQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADenqkLREKLQQME 2594
Cdd:PRK01156 592 ---IKKQLNDLESRL-QEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN----YKKQIAEID 663
|
....*
gi 1655274923 2595 EAQKS 2599
Cdd:PRK01156 664 SIIPD 668
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
32-140 |
4.75e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 43.01 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 32 LKATDGRKDERDRVqkktFTKWVNKHLIKSQrhVTDLYEDLRDGHNLISLLEVLSGD---TLPREKGR-------MRFHK 101
Cdd:COG5069 370 IEEFDAEGEFEARV----FTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKA 443
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 102 LQNVQIALDFLRHRQVKLVNIRNDDIADGNpKLTLGLIW 140
Cdd:COG5069 444 FENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVW 481
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1881-2040 |
4.81e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1881 LEDQANQHKLEIEEKIVLLKKSSDaEMERQKAIVDDTLKQRRVVEEEIRILKLNFEKASSgkldlelelnKLKNIAEETQ 1960
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------QLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1961 QSKLRAEEEAEKLRRLVLEEEM-----RRKEAEDKVKKIAAAEEEAARQRKAAQEELD----RLQKKADEVRKQKEEADK 2031
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEIlelmeRIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
|
....*....
gi 1655274923 2032 EAEKQIVAA 2040
Cdd:COG1579 171 KIPPELLAL 179
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1908-2111 |
5.01e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1908 ERQKAIVDDTLKQRRVVEEEIRILKLNFEKA---------SSGKLDLELELN-KLKNIAE-ETQQSKLRAEEEAEKLRRL 1976
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAeaaleefrqKNGLVDLSEEAKlLLQQLSElESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1977 VLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKA-----------DEVRKQKEEADKEAEKQIVAAQQAAL 2045
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2046 KCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEkakALARDAEAAKERAEreaALL--RQQAEEAERQKV 2111
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR---RLEREVEVARELYE---SLLqrLEEARLAEALTV 385
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2293-2465 |
5.20e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.77 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2293 LNQQRTLAEKMLKEKMQAIQEASRLKAEAEmLQRQKDLAQEQAQKLledkqlmqQRLDEETEEYQRSLE--AERKRQLEi 2370
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAAL-LEAKELLLRERNQQR--------QEARREREELQREEErlVQKEEQLD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2371 iAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQmteVKKMEFEKLNtskeaddlrkaiTELEKE 2450
Cdd:PRK12705 95 -ARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQ---ARKLLLKLLD------------AELEEE 158
|
170
....*....|....*....
gi 1655274923 2451 KA----RLKKEAEEHQNKS 2465
Cdd:PRK12705 159 KAqrvkKIEEEADLEAERK 177
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1373-1586 |
5.23e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1373 QKQLAEAHAKaIAKAEKEAQELKLR-----MQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQ---QIKDKSQQVDEA 1444
Cdd:COG3206 181 EEQLPELRKE-LEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAlraQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1445 LKSRlrieeeihliriQLETTVKQKSNAEDELKQLRDRADAAEKLRKLAQEEAEKLRKQVSEETQKkrlAEEELKHKSEA 1524
Cdd:COG3206 260 LQSP------------VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQR---ILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1655274923 1525 ERKAANEKQKALEDLEN--LRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSF 1586
Cdd:COG3206 325 LQAREASLQAQLAQLEArlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
41-149 |
5.26e-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: 39.97 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 41 ERDRVQKKTFTKWVNKHLIKSQrhVTDLYEDLRDGHNLISLLEVL---------SGDTLPREKGRMRfhKLQNVQIALDF 111
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1655274923 112 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 149
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1150-1373 |
5.32e-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: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1150 LEEELKKASAVSDKMSRVHSERDAELDQHRQHLSSLQDRWKAVFTQIDLR--QRELDQLGRQLGYYRESYDWLIRWIADA 1227
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1228 KQRQENIQAVpitdSKTLKEQLAKEKKLLEEIEKNKDKVDECQKYAKAYIDIIKDY-ELQLVAYKAQVepltspLKKTKL 1306
Cdd:COG4913 695 EELEAELEEL----EEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAA------LGDAVE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1307 DSASDNIIQEYVTLRTR----YSELMTLTSQYIK--------------FITDTQRRLED---------EEKAAEKLKAEE 1359
Cdd:COG4913 765 RELRENLEERIDALRARlnraEEELERAMRAFNRewpaetadldadleSLPEYLALLDRleedglpeyEERFKELLNENS 844
|
250
....*....|....
gi 1655274923 1360 QKKMAEMQAELDKQ 1373
Cdd:COG4913 845 IEFVADLLSKLRRA 858
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
810-854 |
5.35e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 5.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1655274923 810 VQAVCDFKQVE---ITVHKGDECALLNNSQPSKWKVMNRSGSEAVVPS 854
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1802-2046 |
5.37e-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: 43.02 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1802 EEASKLRAIAEEAKhQRQLAEEDAARQRAEAERILKEKLaaiSDATRLKTEAEIAlKEKEAENERLRRQAEDEAYQRKiL 1881
Cdd:pfam15709 331 EKASRDRLRAERAE-MRRLEVERKRREQEEQRRLQQEQL---ERAEKMREELELE-QQRRFEEIRLRKQRLEEERQRQ-E 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1882 EDQANQHKLEieekivllkkssdaEMERQKAivddtlkqrRVVEEEIRilklnfekassgkldlelelNKLKNIAEETQQ 1961
Cdd:pfam15709 405 EEERKQRLQL--------------QAAQERA---------RQQQEEFR--------------------RKLQELQRKKQQ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1962 SKL-RAEEEAEKLRrlvlEEEMRRKEaEDKVKKIAAAEEEAARQRKaAQEELDRLQKKADEVRKQKEEADKEAEKQivAA 2040
Cdd:pfam15709 442 EEAeRAEAEKQRQK----ELEMQLAE-EQKRLMEMAEEERLEYQRQ-KQEAEEKARLEAEERRQKEEEAARLALEE--AM 513
|
....*.
gi 1655274923 2041 QQAALK 2046
Cdd:pfam15709 514 KQAQEQ 519
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1957-2135 |
5.46e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1957 EETQQSKLRAEEEAEKLRRLVLE------EEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKADEvRKQKEEAD 2030
Cdd:pfam15709 329 EQEKASRDRLRAERAEMRRLEVErkrreqEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEE-RQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2031 KEAEKQIVAAQQAAlkcnmaEQQVQSVlaQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEA---- 2106
Cdd:pfam15709 408 RKQRLQLQAAQERA------RQQQEEF--RRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEErley 479
|
170 180
....*....|....*....|....*....
gi 1655274923 2107 ERQKvaaeqeAANQAKAQDDAERLRKDAE 2135
Cdd:pfam15709 480 QRQK------QEAEEKARLEAEERRQKEE 502
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2451-2574 |
5.48e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2451 KARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQfEEEIKKAKALKDEQDRQR 2530
Cdd:pfam05672 22 QAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE-EEAEEREQREQEEQERLQ 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1655274923 2531 QQMEEEKLKLkatmdaalnkQKEAEKDILNKQKEMQELERKRLE 2574
Cdd:pfam05672 101 KQKEEAEAKA----------REEAERQRQEREKIMQQEEQERLE 134
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2503-2592 |
5.66e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2503 DEKKKLESQFEeeiKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQervLADE 2582
Cdd:pfam03938 15 PEGKAAQAQLE---KKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQE---LQKK 88
|
90
....*....|
gi 1655274923 2583 NQKLREKLQQ 2592
Cdd:pfam03938 89 QQELLQPIQD 98
|
|
| PRK13455 |
PRK13455 |
F0F1 ATP synthase subunit B; Provisional |
1478-1599 |
5.77e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184062 [Multi-domain] Cd Length: 184 Bit Score: 40.94 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1478 QLRDRADAAEKLRklaqEEAEKL-----RKQVSEETQKKRLAEEElkhKSEAERkAANEKQKALEDLENLRMQAeeAERQ 1552
Cdd:PRK13455 62 GIRSELEEARALR----EEAQTLlasyeRKQREVQEQADRIVAAA---KDEAQA-AAEQAKADLEASIARRLAA--AEDQ 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655274923 1553 VKQAEVEKERQIQVAHVAAQQSAAAELRSKQMSFAENVSKLEESLKQ 1599
Cdd:PRK13455 132 IASAEAAAVKAVRDRAVSVAVAAAADVIAKQMTAADANALIDEAIKE 178
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1789-2352 |
5.88e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1789 LLEAEATKLRDLAEEASKLRAIAEEAKHQRQLAEE--DAARQR---AEAERILKEKLAAISDATRLKTEAEIALKEKEAE 1863
Cdd:COG3899 676 LEARGPEPLEERLFELAHHLNRAGERDRAARLLLRaaRRALARgayAEALRYLERALELLPPDPEEEYRLALLLELAEAL 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1864 NERLRRQAEDEAYQRkILEDQANQHKLEIEekIVLLKKSSDAEMERQKAIVDDTLKQRRVVEEEIRIL-KLNFEKASSGK 1942
Cdd:COG3899 756 YLAGRFEEAEALLER-ALAARALAALAALR--HGNPPASARAYANLGLLLLGDYEEAYEFGELALALAeRLGDRRLEARA 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1943 LDLELELNKLKNIAEETQQSKLRAEEEAEKL--RRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQKKAD 2020
Cdd:COG3899 833 LFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAA 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2021 EVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLR 2100
Cdd:COG3899 913 LAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALE 992
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2101 QQAEEAERQkVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQQADEEMAKHKKLAEQTLKQKFQVEQEL 2180
Cdd:COG3899 993 AAAAALLAL-LAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAA 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2181 TKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLMKKDKDNTQKFLVE 2260
Cdd:COG3899 1072 AAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLL 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2261 EAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLE 2340
Cdd:COG3899 1152 LAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAAL 1231
|
570
....*....|..
gi 1655274923 2341 DKQLMQQRLDEE 2352
Cdd:COG3899 1232 ALAAALLALRLL 1243
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1951-2108 |
5.95e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 42.55 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1951 KLKNIAEETQQSKLRAEEEAEKLR-RLVLEEEMRRKEAEdkvkkiaaaeeeaaRQRKAAQEELdrLQKKADEVRKQKEEA 2029
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRgKAERDAEHIKKTAK--------------RESKALKKEL--LLEAKEEARKYREEI 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1655274923 2030 DKEAEKQIVAAQQaalkcnMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAER 2108
Cdd:PRK00106 89 EQEFKSERQELKQ------IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELER 161
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1335-1425 |
5.99e-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: 40.11 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1335 IKFITDTQRRLEDEEKAAEKLKAEEQKKMAEMQAELDK-QKQLAEAHAKAIAKAEKEAQELKLRMQEEVSK-RETAAVDA 1412
Cdd:cd06503 25 LKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEaRAEAQEIIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEI 104
|
90
....*....|...
gi 1655274923 1413 EKQKQNIQLELHE 1425
Cdd:cd06503 105 EQEKEKALAELRK 117
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1948-2081 |
6.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1948 ELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEA-ARQRKAAQEELDRLQKKADEVRKQK 2026
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLlEEAEKEAQQAIKEAKKEADEIIKEL 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2027 EEADKEAEKQIVAAQQaalkcnmaeQQVQSVLAQQKEdsMMQNKLKEEYEKAKAL 2081
Cdd:PRK00409 594 RQLQKGGYASVKAHEL---------IEARKRLNKANE--KKEKKKKKQKEKQEEL 637
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1869-2136 |
6.12e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1869 RQAEDEAYQRKILEDQANQHKLEIEEKIvllkkssdAEMERQKAivddtlkqrrvvEEEIRILKLNFEKASSGKLDLELE 1948
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARFEARQ--------ARLEREKA------------AREARHKKAAEARAAKDKDAVAAA 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1949 LNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRK-AAQEELDRLQKKADEVRKQKE 2027
Cdd:PRK05035 492 LARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvAAAIARAKAKKAAQQAANAEA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2028 EADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAE 2107
Cdd:PRK05035 572 EEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAA 651
|
250 260
....*....|....*....|....*....
gi 1655274923 2108 RQKVAAEQEAANQAKAQDDAERLRKDAEF 2136
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAV 680
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1342-1423 |
6.15e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1342 QRRLEDEEKAAEKLKAEEQKKMAEMQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQEEVSKRETAAVDAEKQKQNIQL 1421
Cdd:COG2268 225 EAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA 304
|
..
gi 1655274923 1422 EL 1423
Cdd:COG2268 305 EL 306
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
619-712 |
6.25e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 39.22 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 619 LHAFVSAATKELMWLNDKEEEEVNYDWSDKNTNMTVKKENYSGLMRELELREKKVNDIQAMGDRLVKDGHPGKKTVEAFT 698
Cdd:pfam00435 3 LQQFFRDADDLESWIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERL 82
|
90
....*....|....
gi 1655274923 699 AALQTQWSWILQLC 712
Cdd:pfam00435 83 EELNERWEQLLELA 96
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1841-2109 |
6.44e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1841 AAISDATRLKTEAEIALKEKEAENERLRR-QAEDEAYQRKILEDQANQHKLEIEEKIVLLKKSSDAEMERQKAIVDDTLK 1919
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEReKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1920 QRRVVEEEIRILKLNFEKASSGKLDlELELNKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKEAEDKVKKiaaaee 1999
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAA-AAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIAR------ 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2000 eaARQRKAAQeeldrlqkKADEVRKQKEEADKEAEKQIVAAQQAALKCNMAEQQVQSVLAQQKEDsmmqNKLKEEYEKAK 2079
Cdd:PRK05035 589 --AKAKKAAQ--------QAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDP----RKAAVAAAIAR 654
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1655274923 2080 ALARDAEAAKERAERE-----------AALLRQQAEEAERQ 2109
Cdd:PRK05035 655 AKARKAAQQQANAEPEeaedpkkaavaAAIARAKAKKAAQQ 695
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1953-2173 |
6.69e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1953 KNIAEETQQSKLRAEEEAEKlrRLV---------LEEEMRRKEaedKVKKIAAAEEEAARQRKAAQEEldrlQKKADEVR 2023
Cdd:PRK07735 5 KDLEDLKKEAARRAKEEARK--RLVakhgaeiskLEEENREKE---KALPKNDDMTIEEAKRRAAAAA----KAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2024 KQKEEADKEA-EKQIVAAQQAALKCNMAEqqvQSVLAQQKEDSMMQNKlkeEYEKAKALARDAEAAKERAereAALLRQQ 2102
Cdd:PRK07735 76 KQKREGTEEVtEEEKAKAKAKAAAAAKAK---AAALAKQKREGTEEVT---EEEKAAAKAKAAAAAKAKA---AALAKQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2103 AEEAERQKVAAEQEAANQAKAQDDAERLRKDAEFEAAKLAQAEAAALKQKQqadEEMAKHKKLAEQTLKQK 2173
Cdd:PRK07735 147 REGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTE---EEKAKAKAKAAAAAKAK 214
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2462-2598 |
6.92e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2462 QNKSKEMADAQQ---KQIEREMTVLQQTFLTEKEML--LKKEKLIEDEKKKlesQFEEEIKKAK-ALKDEQDRQRQQMEE 2535
Cdd:PRK09510 68 QQQQKSAKRAEEqrkKKEQQQAEELQQKQAAEQERLkqLEKERLAAQEQKK---QAEEAAKQAAlKQKQAEEAAAKAAAA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1655274923 2536 EKLKLKATMDAALNKQKEAEKDilnKQKEMQELERKRLEQErvlADENQKLREKLQQMEEAQK 2598
Cdd:PRK09510 145 AKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKK 201
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2170-2598 |
7.02e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2170 LKQKFQVEQ-ELTKVKLQLEETDKQKSLLDDELQRLKDEVDDAMRQKASVEEELFKVKIQMEELMKLKVRIEEENQRLmk 2248
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDL-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2249 kdkdntqKFLVEEAENMKKLAEDAARLSIEAQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAEMLQRQK 2328
Cdd:PRK01156 266 -------SMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2329 DlaqEQAQKLLEDKQLMQQRLDEETEE-----YQRSLEAERKRQLEIIAEAEKLKLQVSQLseaqakaeeeAKKFKKQAD 2403
Cdd:PRK01156 339 N---DYIKKKSRYDDLNNQILELEGYEmdynsYLKSIESLKKKIEEYSKNIERMSAFISEI----------LKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2404 TIAARLHETEIATKEQMTEV------------KKMEFEK-------------LNTSKEADDLRKAITELEKEKARLKKEA 2458
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVsslnqriralreNLDELSRnmemlngqsvcpvCGTTLGEEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2459 EEHQNKSKEMADAQQKQIER---------EMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQFEEEIKKAKALKDEQDRQ 2529
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRkeyleseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2530 RQqmeEEKLKLKATMDA----ALNKQKEAEKDILNK-QKEMQELER-------------KRLEQE-RVLADENQKLREKL 2590
Cdd:PRK01156 566 KR---TSWLNALAVISLidieTNRSRSNEIKKQLNDlESRLQEIEIgfpddksyidksiREIENEaNNLNNKYNEIQENK 642
|
....*...
gi 1655274923 2591 QQMEEAQK 2598
Cdd:PRK01156 643 ILIEKLRG 650
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2231-2374 |
7.12e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2231 ELMKLKVRIEEENQRlmkkdkdntQKFLVEEAENMKKLAEDAARLSIEAQ-EAARLRQIAEDDLNQQRTLAEKMLKEKMQ 2309
Cdd:PTZ00491 684 ERQKMHDKAKAEEQR---------TKLLELQAESAAVESSGQSRAEALAEaEARLIEAEAEVEQAELRAKALRIEAEAEL 754
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655274923 2310 AIQEAsRLKAEAEMLQRQKDLAQEQAQKLledkqlmqqrLDEETEEYQRSLEAERKRQLEIIAEA 2374
Cdd:PTZ00491 755 EKLRK-RQELELEYEQAQNELEIAKAKEL----------ADIEATKFERIVEALGRETLIAIARA 808
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1968-2080 |
7.31e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1968 EEAEKLRRLVLEEEMRRKEAEDKVKKIAAAEEEAARQRKAAQEELDRLQkkaDEVRKQKEEADKEAEKQIVAAQQAALK- 2046
Cdd:PRK00409 513 EDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEAKKEADEi 589
|
90 100 110
....*....|....*....|....*....|....*...
gi 1655274923 2047 ----CNMAEQQVQSVLAQQKEDsmMQNKLKEEYEKAKA 2080
Cdd:PRK00409 590 ikelRQLQKGGYASVKAHELIE--ARKRLNKANEKKEK 625
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
2277-2618 |
7.33e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2277 IEAQEAARLRQIAEDDLNQQRTlaekmlkekmQAIQEASRLKAEAEMLQRQKDLAQEQAQKLLE--DKQLMQQR--LDEE 2352
Cdd:pfam15818 10 LEALEELRMRREAETQYEEQIG----------KIIVETQELKWQKETLQNQKETLAKQHKEAMAvfKKQLQMKMcaLEEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2353 TEEYQRSLEAERKrqlEIIAEAEKLK-LQVSQLSEAQAKaeeeakkfkkqadtiaarlheTEIATKEQMTEVKKMEFEK- 2430
Cdd:pfam15818 80 KGKYQLATEIKEK---EIEGLKETLKaLQVSKYSLQKKV---------------------SEMEQKLQLHLLAKEDHHKq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2431 LNtskEADDLRKAITE---LEKEK-ARLKKEAEEHQNKSKEMADAQQKQiEREMTVLQqtflteKEMLLKKEKLIedeKK 2506
Cdd:pfam15818 136 LN---EIEKYYATITGqfgLVKENhGKLEQNVQEAIQLNKRLSALNKKQ-ESEICSLK------KELKKVTSDLI---KS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2507 KLESQF---EEEIKKA-KALKDEQDRQRQQMEeekLKLKATMDAALNKQKEAEKDILNKQKEMQELERKRLEQERVLADE 2582
Cdd:pfam15818 203 KVTCQYkmgEENINLTiKEQKFQELQERLNME---LELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAE 279
|
330 340 350
....*....|....*....|....*....|....*.
gi 1655274923 2583 NQKLREKLQQMEeaQKSTLITEKHVTVVETVLNGQN 2618
Cdd:pfam15818 280 LKALKENNQTLE--RDNELQREKVKENEEKFLNLQN 313
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2050-2597 |
7.34e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2050 AEQQVQSVLAQQKEDSMMQNKLKEEYEKAKALARDAEAAKERAEREAALLRQQAEEAERQKVAAEQEAANqakaQDDAER 2129
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL----REQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2130 LRkdaefeaaklaqaeaaalkQKQQADEEMAKHKKLAEQTLKQKFQV----EQELTKVKLQLEETDKQKSLLDDELQRLK 2205
Cdd:pfam05557 78 NR-------------------LKKKYLEALNKKLNEKESQLADAREVisclKNELSELRRQIQRAELELQSTNSELEELQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2206 dEVDDAMRQKASVEEELFK-VKIQMEELMKLKVRIEEENQRLMKKDKDNtqkflvEEAENMKklaedaarlsieaqeaAR 2284
Cdd:pfam05557 139 -ERLDLLKAKASEAEQLRQnLEKQQSSLAEAEQRIKELEFEIQSQEQDS------EIVKNSK----------------SE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2285 LRQIAEDDLNQQRTLAE-KMLKEkmqAIQEASRLKAEAEMLQR---QKDLAQEQAQKLLEDKQLMQQRLDEETEEYQ--- 2357
Cdd:pfam05557 196 LARIPELEKELERLREHnKHLNE---NIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSWVKLAQdtg 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2358 ---RSLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEKLNTS 2434
Cdd:pfam05557 273 lnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2435 KEADDLRKAITELEKE---------KARLKKEAE----EHQNKSKEMaDAQQKQIEREMTVLQQTFLT-EKEMLLKKEKL 2500
Cdd:pfam05557 353 KERDGYRAILESYDKEltmsnyspqLLERIEEAEdmtqKMQAHNEEM-EAQLSVAEEELGGYKQQAQTlERELQALRQQE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2501 IEDEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAeKDILNKQKEMQELERKRLEQERVLA 2580
Cdd:pfam05557 432 SLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKT-KVLHLSMNPAAEAYQQRKNQLEKLQ 510
|
570
....*....|....*..
gi 1655274923 2581 DENQKLREKLQQMEEAQ 2597
Cdd:pfam05557 511 AEIERLKRLLKKLEDDL 527
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2003-2109 |
7.58e-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: 39.54 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2003 RQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQAAlkcNMAEQQVQsvlaQQKEDSMMQNKLKEEYEKAKALA 2082
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQ---QNYERELV----LHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*..
gi 1655274923 2083 RDAEAAKERAEREAALLRQQAEEAERQ 2109
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQKKE 100
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
2503-2592 |
7.63e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.59 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2503 DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATMDAALNKQKEAEkdILNKQKEMQELERKRLEQervLADE 2582
Cdd:COG2825 39 PEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEERQKKERE--LQKKQQELQRKQQEAQQD---LQKR 113
|
90
....*....|
gi 1655274923 2583 NQKLREKLQQ 2592
Cdd:COG2825 114 QQELLQPILE 123
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1348-1578 |
7.77e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1348 EEKAAEKLKAEEQKKMAE-------MQAELDKQKQLAEAHAKAIAKAEKEAQELKLRMQeevskRETAAVDAEKQKQNIQ 1420
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQdlqqalsLLDKIDASKQRAAAYQKALDDAPAELRELRQELA-----ALQAKAEAAPKEILAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1421 LELHELknlsEQQIKDKSQQVDEALKSRLRIEEEIHLIRIQLETTVKQKSNAEDELKQLRDRADAAeKLRKLAQEEAEKL 1500
Cdd:pfam12795 78 LSLEEL----EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGP-APPGEPLSEAQRW 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 1501 RKQVSEETQKKRLAEEELKHKSEAERKAANEKQKaleDLENLRMQAEEAERQVKQAEVEKERQIQVAHVAAQQSAAAE 1578
Cdd:pfam12795 153 ALQAELAALKAQIDMLEQELLSNNNRQDLLKARR---DLLTLRIQRLEQQLQALQELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2425-2604 |
7.90e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2425 KMEFEKLNTSKEADDLRKAITELEKEKARLKKEAEEhqnkskEMADAQQKQIER---EMTVLQQTFLTEKEMLLKKEKLI 2501
Cdd:pfam10174 323 KQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE------SFLNKKTKQLQDlteEKSTLAGEIRDLKDMLDVKERKI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2502 EDEKKKLESQFEEEIKKAKALKDEQDRQrQQMEEEKlklkATMDAALNKQKEA----EKDILNKQKEMQELERKRLEQER 2577
Cdd:pfam10174 397 NVLQKKIENLQEQLRDKDKQLAGLKERV-KSLQTDS----SNTDTALTTLEEAlsekERIIERLKEQREREDRERLEELE 471
|
170 180
....*....|....*....|....*....
gi 1655274923 2578 VLADENQKLREKL--QQMEEAQKSTLITE 2604
Cdd:pfam10174 472 SLKKENKDLKEKVsaLQPELTEKESSLID 500
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1302-1537 |
8.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1302 KKTKLDSASDNIIQEYVTLRTRYSELMTLTSQYIKFITDTQRRLEDEEKAAEKLKAEeqkkMAEMQAELDKQKQLAEAHA 1381
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1382 KAIAKAEKEAQELKL----RMQEEVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRIEEEihl 1457
Cdd:COG3883 93 RALYRSGGSVSYLDVllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1458 iRIQLETTVKQKSNAEDELKQlrDRADAAEKLRKLAQEEAEKLRKQVSEETQKKRLAEEELKHKSEAERKAANEKQKALE 1537
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSA--EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1797-1894 |
8.22e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1797 LRDLAEEASKLRAIAEEAKHQRQLAEEDAARQRAEAERIlkEKLAAisdatrlktEAEIALKEKEAENERLRRQA----- 1871
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAL--EGLAA---------ELEEKQQELEAQLEQLQEKAaetsq 212
|
90 100
....*....|....*....|...
gi 1655274923 1872 EDEAYQRKILEDQANQHKLEIEE 1894
Cdd:PRK11448 213 ERKQKRKEITDQAAKRLELSEEE 235
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2458-2598 |
8.59e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2458 AEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLESQfeeEIKKAKALKDEQDRQRQQMEEEK 2537
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ---EQKKQAEEAAKQAALKQKQAEEA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655274923 2538 LKLKAtmdAALNKQKEAEKDILNKQKEMQELERKRLEQERvlADENQKLREKLQQMEEAQK 2598
Cdd:PRK09510 138 AAKAA---AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE--AAKKAAAEAKKKAEAEAAA 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1313-1555 |
8.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1313 IIQEYVTLRTRYSELmtltSQYIKFITDTQRRLEDEEKAAEKLK--AEEQKKMAEMQAEL-DKQKQLAEAHA--KAIAKA 1387
Cdd:COG4913 615 LEAELAELEEELAEA----EERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIaELEAELERLDAssDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1388 EKEAQELKLRMQE---EVSKRETAAVDAEKQKQNIQLELHELKNLSEQQIKDKSQQVDEALKSRLRieeeiHLIRIQLET 1464
Cdd:COG4913 691 EEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-----AALGDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1465 TVKQksNAEDELKQLRDRADAAE-KLRKLAQE-----EAEKLRKQVS----EETQK--KRLAEEELKHKSEAERKAANEK 1532
Cdd:COG4913 766 ELRE--NLEERIDALRARLNRAEeELERAMRAfnrewPAETADLDADleslPEYLAllDRLEEDGLPEYEERFKELLNEN 843
|
250 260
....*....|....*....|...
gi 1655274923 1533 QKalEDLENLRMQAEEAERQVKQ 1555
Cdd:COG4913 844 SI--EFVADLLSKLRRAIREIKE 864
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1914-2042 |
8.68e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 41.31 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1914 VDDTLKQRRVVEEE-----IRILKLNFEKASSGKLDLELEL--NKLKNIAEETQQSKLRAEEEAEKLRRLVLEEEMRRKE 1986
Cdd:cd07647 24 LEDFLKQRAKAEEDygkalLKLSKSAGPGDEIGTLKSSWDSlrKETENVANAHIQLAQSLREEAEKLEEFREKQKEERKK 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1655274923 1987 AEDKVKKIAaaeeeaaRQRKAAQEELDRLQKKADEVRKQKEEADKEAEKQIVAAQQ 2042
Cdd:cd07647 104 TEDIMKRSQ-------KNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSSGAQP 152
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3784-3817 |
9.05e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 9.05e-03
10 20 30
....*....|....*....|....*....|....
gi 1655274923 3784 LEAQTSTGGIIDPEFQFHLPADVAIQRGYINKET 3817
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1348-1501 |
9.22e-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: 41.51 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 1348 EEKAAEKLK---AEEQKKMAEMQAELDKQKqlaeahakAIAKAEKEAQELKLRMQEEVskretaavdAEKqkqniqlelh 1424
Cdd:cd03406 169 EAMEAEKTKlliAEQHQKVVEKEAETERKR--------AVIEAEKDAEVAKIQMQQKI---------MEK---------- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1655274923 1425 elknlseqqikdksqqvdEALKSRLRIEEEIHLIRiqlettvkqksnaedelkqLRDRADaAEKLRKLAQEEAEKLR 1501
Cdd:cd03406 222 ------------------EAEKKISEIEDEMHLAR-------------------EKARAD-AEYYRALREAEANKLK 260
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2279-2600 |
9.59e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2279 AQEAARLRQIAEDDLNQQRTLAEKMLKEKMQAIQEASRLKAEAemLQRQKDlAQEQAQKLLEDKQLMQQRLDEETEEYQR 2358
Cdd:TIGR00606 236 SREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK--KQMEKD-NSELELKMEKVFQGTDEQLNDLYHNHQR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2359 SLEAERKRQLEIIAEAEKLKLQVSQLSEAQAKAEEEAKKFKKQADTIAARLHETEIATKEQMTEVKKMEFEK-LNTSKEA 2437
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERgPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2438 DDLRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIEDEKKKLEsqfeeeik 2517
Cdd:TIGR00606 393 KNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQ-------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2518 kakalkdeqdrQRQQMEEEKLKLKATMDAALNKQKEAEKDILNKQKEMQElerKRLEQERvlADENQKLREKLQQMEEAQ 2597
Cdd:TIGR00606 465 -----------QLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV---KSLQNEK--ADLDRKLRKLDQEMEQLN 528
|
...
gi 1655274923 2598 KST 2600
Cdd:TIGR00606 529 HHT 531
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2424-2576 |
9.93e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655274923 2424 KKMEFEKLNTSKEADD-LRKAITELEKEKARLKKEAEEHQNKSKEMADAQQKQIEREMTVLQQTFLTEKEMLLKKEKLIE 2502
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRiLEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1655274923 2503 DEKKKLESQFEEEIKKAKALKDEQDRQRQQMEEEKLKLKATmdAALNKQkEAEKDILNKQKEMQELER----KRLEQE 2576
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--SGLTAE-EAKEILLEKVEEEARHEAavliKEIEEE 181
|
|
| |
